|
Name |
Accession |
Description |
Interval |
E-value |
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-257 |
9.11e-145 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 405.62 E-value: 9.11e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFYPNTNRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKY 82
Cdd:COG1101 2 LELKNLSKTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 83 ISRVYQNPLQGTAPRMTVAQNLSLALRRGLKRGLKKGYTAEELEQFKALLTPLQLGLEERLDAEIGLLSGGQRQAVSLLM 162
Cdd:COG1101 82 IGRVFQDPMMGTAPSMTIEENLALAYRRGKRRGLRRGLTKKRRELFRELLATLGLGLENRLDTKVGLLSGGQRQALSLLM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 163 ATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKIIQVFEKEEKEALTE 242
Cdd:COG1101 162 ATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRIILDVSGEEKKKLTV 241
|
250
....*....|....*
gi 260158848 243 EKLYQLMAELDEADF 257
Cdd:COG1101 242 EDLLELFEEIRGEEL 256
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
3-231 |
3.49e-53 |
|
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: 171.55 E-value: 3.49e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFypntnRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAky 82
Cdd:cd03259 1 LELKGLSKTY-----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRN-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 83 ISRVYQNPlqgtA--PRMTVAQNLSLALRRglkRGLKKgytAEELEQFKALLtpLQLGLEERLDAEIGLLSGGQRQAVSL 160
Cdd:cd03259 74 IGMVFQDY----AlfPHLTVAENIAFGLKL---RGVPK---AEIRARVRELL--ELVGLEGLLNRYPHELSGGQQQRVAL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 260158848 161 LMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKIIQV 231
Cdd:cd03259 142 ARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQV 212
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-229 |
4.26e-49 |
|
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: 161.52 E-value: 4.26e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFyPNTNRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHI-YMGEAAVEHTAEY--ER 79
Cdd:cd03257 2 LEVKNLSVSF-PTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIiFDGKDLLKLSRRLrkIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 80 AKYISRVYQNPLQGTAPRMTVAQNLSLALRrglkrgLKKGYTAEELEQFKALLTPLQLGL-EERLDAEIGLLSGGQRQAV 158
Cdd:cd03257 81 RKEIQMVFQDPMSSLNPRMTIGEQIAEPLR------IHGKLSKKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 260158848 159 SLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKII 229
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
3-233 |
1.42e-48 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 159.94 E-value: 1.42e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTfYPNTNRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHI-YMGEAAVEHTAEyerak 81
Cdd:cd03293 1 LEVRNVSKT-YGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVlVDGEPVTGPGPD----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 82 yISRVYQNPLqgTAPRMTVAQNLSLALRRglkRGLKKgytAEELEQFKALLTplQLGLEERLDAEIGLLSGGQRQAVSLL 161
Cdd:cd03293 75 -RGYVFQQDA--LLPWLTVLDNVALGLEL---QGVPK---AEARERAEELLE--LVGLSGFENAYPHQLSGGMRQRVALA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 260158848 162 MATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMM--HRGKIIQVFE 233
Cdd:cd03293 144 RALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAEVE 217
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-245 |
2.14e-47 |
|
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: 164.31 E-value: 2.14e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFYPNTNRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKY 82
Cdd:COG1123 261 LEVRNLSKRYPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 83 ISR---VYQNPLQGTAPRMTVAQNLSLALRrglkrgLKKGYTAEELEQF-KALLTplQLGLEER-LDAEIGLLSGGQRQA 157
Cdd:COG1123 341 RRRvqmVFQDPYSSLNPRMTVGDIIAEPLR------LHGLLSRAERRERvAELLE--RVGLPPDlADRYPHELSGGQRQR 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 158 VSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKII------QV 231
Cdd:COG1123 413 VAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVedgpteEV 492
|
250
....*....|....
gi 260158848 232 FEkEEKEALTEEKL 245
Cdd:COG1123 493 FA-NPQHPYTRALL 505
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-229 |
9.00e-47 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 155.59 E-value: 9.00e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTfYPNTNRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGsfpLDK---GHIYMGEAAVEHTAEYER 79
Cdd:COG1136 5 LELRNLTKS-YGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGG---LDRptsGEVLIDGQDISSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 80 AKY----ISRVYQNP--LqgtaPRMTVAQNLSLALR-RGLKRglkkgytAEELEQFKALLTplQLGLEERLDAEIGLLSG 152
Cdd:COG1136 81 ARLrrrhIGFVFQFFnlL----PELTALENVALPLLlAGVSR-------KERRERARELLE--RVGLGDRLDHRPSQLSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 260158848 153 GQRQAVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLsDALRYGNRLMMMHRGKII 229
Cdd:COG1136 148 GQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRIV 223
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
3-228 |
6.34e-46 |
|
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: 153.03 E-value: 6.34e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTfYPNTNRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKY 82
Cdd:cd03255 1 IELKNLSKT-YGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 83 ----ISRVYQNP--LqgtaPRMTVAQNLSLALrrgLKRGLKKgytAEELEQFKALLTplQLGLEERLDAEIGLLSGGQRQ 156
Cdd:cd03255 80 rrrhIGFVFQSFnlL----PDLTALENVELPL---LLAGVPK---KERRERAEELLE--RVGLGDRLNHYPSELSGGQQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 260158848 157 AVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDAlRYGNRLMMMHRGKI 228
Cdd:cd03255 148 RVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
4-227 |
2.36e-45 |
|
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: 151.47 E-value: 2.36e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 4 RIENVHKTfYPNTNRShdALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKYI 83
Cdd:cd03225 1 ELKNLSFS-YPDGARP--ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 84 SRVYQNP-LQGTAPrmTVAQNLSLALR-RGLKRGLKKGYTAEELEQFkalltplqlGLEERLDAEIGLLSGGQRQAVSLL 161
Cdd:cd03225 78 GLVFQNPdDQFFGP--TVEEEVAFGLEnLGLPEEEIEERVEEALELV---------GLEGLRDRSPFTLSGGQKQRVAIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 260158848 162 MATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKeLTALMITHNLSDALRYGNRLMMMHRGK 227
Cdd:cd03225 147 GVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEG-KTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-248 |
4.21e-45 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 152.12 E-value: 4.21e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFypntnRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKY 82
Cdd:COG1120 2 LEAENLSVGY-----GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 83 ISRVYQNPlqGTAPRMTVAQNLSLAlRRGLKRGLKkGYTAEELEQFKALLTplQLGLEERLDAEIGLLSGGQRQAVSLLM 162
Cdd:COG1120 77 IAYVPQEP--PAPFGLTVRELVALG-RYPHLGLFG-RPSAEDREAVEEALE--RTGLEHLADRPVDELSGGERQRVLIAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 163 ATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKIiqVFEKEEKEALTE 242
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRI--VAQGPPEEVLTP 228
|
....*.
gi 260158848 243 EKLYQL 248
Cdd:COG1120 229 ELLEEV 234
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
3-248 |
4.65e-45 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 151.75 E-value: 4.65e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTfYPNTNRshdALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKY 82
Cdd:COG3638 3 LELRNLSKR-YPGGTP---ALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 83 ISR---VYQNP-LqgtAPRMTVAQN-LSLAL-RRGLKRGLKKGYTAEELEQFKALLTplQLGLEERLDAEIGLLSGGQRQ 156
Cdd:COG3638 79 RRRigmIFQQFnL---VPRLSVLTNvLAGRLgRTSTWRSLLGLFPPEDRERALEALE--RVGLADKAYQRADQLSGGQQQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 157 AVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKIiqVFEKeE 236
Cdd:COG3638 154 RVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRV--VFDG-P 230
|
250
....*....|..
gi 260158848 237 KEALTEEKLYQL 248
Cdd:COG3638 231 PAELTDAVLREI 242
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
2-231 |
6.88e-45 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 154.10 E-value: 6.88e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 2 DIRIENVHKTFypntnRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERak 81
Cdd:COG3842 5 ALELENVSKRY-----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKR-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 82 YISRVYQNPlqgtA--PRMTVAQNLSLALRRglkRGLKKgytAEELEQFKALLTplQLGLEERLDAEIGLLSGGQRQAVS 159
Cdd:COG3842 78 NVGMVFQDY----AlfPHLTVAENVAFGLRM---RGVPK---AEIRARVAELLE--LVGLEGLADRYPHQLSGGQQQRVA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 260158848 160 LlmAtlRT----PELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKIIQV 231
Cdd:COG3842 146 L--A--RAlapePRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQV 217
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-236 |
2.10e-44 |
|
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: 149.95 E-value: 2.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTfYPNTNRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKY 82
Cdd:COG1124 2 LEVRNLSVS-YGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 83 ISRVYQNPLQGTAPRMTVAQNLSLALRrglkrGLKKGYTAEELEQfkaLLTplQLGLEER-LDAEIGLLSGGQRQAVSLL 161
Cdd:COG1124 81 VQMVFQDPYASLHPRHTVDRILAEPLR-----IHGLPDREERIAE---LLE--QVGLPPSfLDRYPHQLSGGQRQRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 260158848 162 MATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKIIQVFEKEE 236
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVAD 225
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
3-251 |
5.24e-44 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 148.67 E-value: 5.24e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFypntnRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIY-MGEAAVEHTAEYeRAK 81
Cdd:COG1131 1 IEVRGLTKRY-----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvLGEDVARDPAEV-RRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 82 yISRVYQNPlqGTAPRMTVAQNLSLALR-RGLKRGLKKGYTAEELEQFkalltplqlGLEERLDAEIGLLSGGQRQAVSL 160
Cdd:COG1131 75 -IGYVPQEP--ALYPDLTVRENLRFFARlYGLPRKEARERIDELLELF---------GLTDAADRKVGTLSGGMKQRLGL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 161 LMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEkELTALMITHNLSDALRYGNRLMMMHRGKIIQVFEKEE-KEA 239
Cdd:COG1131 143 ALALLHDPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDElKAR 221
|
250
....*....|..
gi 260158848 240 LTEEKLYQLMAE 251
Cdd:COG1131 222 LLEDVFLELTGE 233
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
3-233 |
7.64e-44 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 149.08 E-value: 7.64e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTfYPNTNRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEhtaeyERAKY 82
Cdd:COG1116 8 LELRGVSKR-FPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT-----GPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 83 ISRVYQNP--LqgtaPRMTVAQNLSLALRRglkRGLKKGYTAEELEQFKALLtplqlGLEERLDAEIGLLSGGQRQAVSL 160
Cdd:COG1116 82 RGVVFQEPalL----PWLTVLDNVALGLEL---RGVPKAERRERARELLELV-----GLAGFEDAYPHQLSGGMRQRVAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 260158848 161 LMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHR--GKIIQVFE 233
Cdd:COG1116 150 ARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVEEID 224
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
3-248 |
7.81e-44 |
|
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: 148.48 E-value: 7.81e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTfYPNtnrSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGE---AAVEHTAEYER 79
Cdd:cd03256 1 IEVENLSKT-YPN---GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGtdiNKLKGKALRQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 80 AKYISRVYQNPlqGTAPRMTVAQN-LSLAL-RRGLKRGLKKGYTAEELEQFKALLTplQLGLEERLDAEIGLLSGGQRQA 157
Cdd:cd03256 77 RRQIGMIFQQF--NLIERLSVLENvLSGRLgRRSTWRSLFGLFPKEEKQRALAALE--RVGLLDKAYQRADQLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 158 VSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKIiqVFEKEEK 237
Cdd:cd03256 153 VAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRI--VFDGPPA 230
|
250
....*....|.
gi 260158848 238 EaLTEEKLYQL 248
Cdd:cd03256 231 E-LTDEVLDEI 240
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
3-229 |
8.66e-44 |
|
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: 147.97 E-value: 8.66e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFypntnRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKY 82
Cdd:cd03219 1 LEVRGLTKRF-----GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 83 -ISRVYQNPlqGTAPRMTVAQNLSLALRRGLKRGLKKGYTAEELEQFKA----LLTplQLGLEERLDAEIGLLSGGQRQA 157
Cdd:cd03219 76 gIGRTFQIP--RLFPELTVLENVMVAAQARTGSGLLLARARREEREAREraeeLLE--RVGLADLADRPAGELSYGQQRR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 260158848 158 VSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKeLTALMITHNLSDALRYGNRLMMMHRGKII 229
Cdd:cd03219 152 LEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERG-ITVLLVEHDMDVVMSLADRVTVLDQGRVI 222
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
3-230 |
3.99e-43 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 146.05 E-value: 3.99e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFypntnrsHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAky 82
Cdd:COG3840 2 LRLDDLTYRY-------GDFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERP-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 83 ISRVYQ-NPLqgtAPRMTVAQNLSLALRRGLKrglkkgYTAEELEQFKALLTplQLGLEERLDAEIGLLSGGQRQAVSLL 161
Cdd:COG3840 73 VSMLFQeNNL---FPHLTVAQNIGLGLRPGLK------LTAEQRAQVEQALE--RVGLAGLLDRLPGQLSGGQRQRVALA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 260158848 162 MATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKIIQ 230
Cdd:COG3840 142 RCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAA 210
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-229 |
7.42e-43 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 152.36 E-value: 7.42e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFypnTNRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLD---KGHIYMGEAAVEHTAEYER 79
Cdd:COG1123 5 LEVRDLSVRY---PGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 80 AKYISRVYQNPLQGTAPrMTVAQNLSLALR-RGLKRglkkgytAEELEQFKALLTplQLGLEERLDAEIGLLSGGQRQAV 158
Cdd:COG1123 82 GRRIGMVFQDPMTQLNP-VTVGDQIAEALEnLGLSR-------AEARARVLELLE--AVGLERRLDRYPHQLSGGQRQRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 260158848 159 SLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKII 229
Cdd:COG1123 152 AIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIV 222
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
4-229 |
9.56e-43 |
|
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: 143.73 E-value: 9.56e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 4 RIENVHKTFypntnRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKYI 83
Cdd:cd03214 1 EVENLSVGY-----GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 84 SrvyqnplqgtaprmTVAQNLSLalrrglkrglkkgytaeeleqfkalltplqLGLEERLDAEIGLLSGGQRQAVSLLMA 163
Cdd:cd03214 76 A--------------YVPQALEL------------------------------LGLAHLADRPFNELSGGERQRVLLARA 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 260158848 164 TLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKII 229
Cdd:cd03214 112 LAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
3-237 |
9.75e-43 |
|
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: 145.17 E-value: 9.75e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTfYPNtnrSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKY 82
Cdd:COG1122 1 IELENLSFS-YPG---GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 83 ISRVYQNP-LQGTAPrmTVAQNLSLALRRglkrglkKGYTAEELEQ--FKALltpLQLGLEERLDAEIGLLSGGQRQAVS 159
Cdd:COG1122 77 VGLVFQNPdDQLFAP--TVEEDVAFGPEN-------LGLPREEIRErvEEAL---ELVGLEHLADRPPHELSGGQKQRVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 160 L--LMAtLRtPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKeLTALMITHNLSDALRYGNRLMMMHRGKII------QV 231
Cdd:COG1122 145 IagVLA-ME-PEVLVLDEPTAGLDPRGRRELLELLKRLNKEG-KTVIIVTHDLDLVAELADRVIVLDDGRIVadgtprEV 221
|
....*.
gi 260158848 232 FEKEEK 237
Cdd:COG1122 222 FSDYEL 227
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-248 |
2.43e-42 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 144.46 E-value: 2.43e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFypntnRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHtaeyeRAKY 82
Cdd:COG1121 7 IELENLTVSY-----GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-----ARRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 83 ISRVYQnplQGTAPR---MTVAQNLSLALRRglKRGLKKGYTAEELEQFKALLTplQLGLEERLDAEIGLLSGGQRQAVS 159
Cdd:COG1121 77 IGYVPQ---RAEVDWdfpITVRDVVLMGRYG--RRGLFRRPSRADREAVDEALE--RVGLEDLADRPIGELSGGQQQRVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 160 LLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKeLTALMITHNLSDALRYGNRLMMMHRGkiiQVFEKEEKEA 239
Cdd:COG1121 150 LARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREG-KTILVVTHDLGAVREYFDRVLLLNRG---LVAHGPPEEV 225
|
....*....
gi 260158848 240 LTEEKLYQL 248
Cdd:COG1121 226 LTPENLSRA 234
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
3-228 |
6.67e-42 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 142.26 E-value: 6.67e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHktfYPNTNRSHdaLIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEhtaEYERAKY 82
Cdd:COG4619 1 LELEGLS---FRVGGKPI--LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLS---AMPPPEW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 83 ISRV-Y--QNPLQGtapRMTVAQNLSLALRRGLKRGlkkgytaeELEQFKALLTplQLGLEER-LDAEIGLLSGGQRQAV 158
Cdd:COG4619 73 RRQVaYvpQEPALW---GGTVRDNLPFPFQLRERKF--------DRERALELLE--RLGLPPDiLDKPVERLSGGERQRL 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 159 SLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKI 228
Cdd:COG4619 140 ALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
23-236 |
5.33e-41 |
|
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: 140.93 E-value: 5.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 23 LIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAkyISRVYQNplQGTAPRMTVAQ 102
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRD--ISYVPQN--YALFPHMTVYK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 103 NLSLALRrglKRGLKKGYTAEELEQFKALLtplqlGLEERLDAEIGLLSGGQRQAVSLLMATLRTPELLLLDEHTAALDP 182
Cdd:cd03299 91 NIAYGLK---KRKVDKKEIERKVLEIAEML-----GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 260158848 183 KTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKIIQVFEKEE 236
Cdd:cd03299 163 RTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEE 216
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
2-231 |
8.80e-39 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 138.28 E-value: 8.80e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 2 DIRIENVHKTFypntnRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAk 81
Cdd:COG3839 3 SLELENVSKSY-----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRN- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 82 yISRVYQNPlqgtA--PRMTVAQNLSLALRRglkRGLKKGYTAEELEQFKALLtplqlGLEERLDAEIGLLSGGQRQAVS 159
Cdd:COG3839 77 -IAMVFQSY----AlyPHMTVYENIAFPLKL---RKVPKAEIDRRVREAAELL-----GLEDLLDRKPKQLSGGQRQRVA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 260158848 160 LLMATLRTPELLLLDEHTAALDPK----TQRKIMQLTKEIieekELTALMITHNLSDALRYGNRLMMMHRGKIIQV 231
Cdd:COG3839 144 LGRALVREPKVFLLDEPLSNLDAKlrveMRAEIKRLHRRL----GTTTIYVTHDQVEAMTLADRIAVMNDGRIQQV 215
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
19-228 |
1.82e-38 |
|
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: 133.81 E-value: 1.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 19 SHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYM-GEaavehTAEYERaKYISRVYQNPLQGTAPR 97
Cdd:cd03235 11 GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVfGK-----PLEKER-KRIGYVPQRRSIDRDFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 98 MTVAQNLSLALRRglKRGLKKGYTAEeleQFKALLTPLQL-GLEERLDAEIGLLSGGQRQAVSLLMATLRTPELLLLDEH 176
Cdd:cd03235 85 ISVRDVVLMGLYG--HKGLFRRLSKA---DKAKVDEALERvGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 260158848 177 TAALDPKTQRKIMQLTKEIIEEkELTALMITHNLSDALRYGNRLMMMHRGKI 228
Cdd:cd03235 160 FAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
3-227 |
2.74e-38 |
|
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: 131.93 E-value: 2.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFypntnRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERA-- 80
Cdd:cd03229 1 LELKNVSKRY-----GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPlr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 81 KYISRVYQNPlqGTAPRMTVAQNLSLALrrglkrglkkgytaeeleqfkalltplqlgleerldaeigllSGGQRQAVSL 160
Cdd:cd03229 76 RRIGMVFQDF--ALFPHLTVLENIALGL------------------------------------------SGGQQQRVAL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 260158848 161 LMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGK 227
Cdd:cd03229 112 ARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-236 |
3.74e-38 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 136.43 E-value: 3.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 1 MDIRIENVHKTFypntnRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISG-SFPlDKGHIYM-GEAAVEHTAEYE 78
Cdd:COG1118 1 MSIEVRNISKRF-----GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGlETP-DSGRIVLnGRDLFTNLPPRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 79 RakYISRVYQNPlqgtA--PRMTVAQNLSLALRrglKRGLKKGYTAEELEQfkaLLTPLQL-GLEERLDAEiglLSGGQR 155
Cdd:COG1118 75 R--RVGFVFQHY----AlfPHMTVAENIAFGLR---VRPPSKAEIRARVEE---LLELVQLeGLADRYPSQ---LSGGQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 156 QAVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKIIQVFEKE 235
Cdd:COG1118 140 QRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPD 219
|
.
gi 260158848 236 E 236
Cdd:COG1118 220 E 220
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
3-231 |
4.45e-38 |
|
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: 132.76 E-value: 4.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFYPNTnrshdALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAky 82
Cdd:cd03301 1 VELENVTKRFGNVT-----ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRD-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 83 ISRVYQNplQGTAPRMTVAQNLSLALRRglkRGLKKGYTAEELEQFKALLtplqlGLEERLDAEIGLLSGGQRQAVSLLM 162
Cdd:cd03301 74 IAMVFQN--YALYPHMTVYDNIAFGLKL---RKVPKDEIDERVREVAELL-----QIEHLLDRKPKQLSGGQRQRVALGR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 260158848 163 ATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKIIQV 231
Cdd:cd03301 144 AIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQI 212
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
3-233 |
5.40e-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: 5.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHkTFYPntnRSHdALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKY 82
Cdd:cd03224 1 LEVENLN-AGYG---KSQ-ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 83 -ISRVYQNplQGTAPRMTVAQNLSLALRRGLKRGLKKGYtAEELEQFKAlltplqlgLEERLDAEIGLLSGGQRQAVSLL 161
Cdd:cd03224 76 gIGYVPEG--RRIFPELTVEENLLLGAYARRRAKRKARL-ERVYELFPR--------LKERRKQLAGTLSGGEQQMLAIA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 260158848 162 MATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEkELTALMITHNLSDALRYGNRLMMMHRGKIiqVFE 233
Cdd:cd03224 145 RALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRV--VLE 213
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-247 |
7.03e-38 |
|
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: 133.19 E-value: 7.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTfYPNtnrSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYE---- 78
Cdd:TIGR02315 2 LEVENLSKV-YPN---GKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrkl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 79 RAK--YISRVYQNplqgtAPRMTVAQNLsLALRRGLKRGLKKG---YTAEELEQFKALLTplQLGLEERLDAEIGLLSGG 153
Cdd:TIGR02315 78 RRRigMIFQHYNL-----IERLTVLENV-LHGRLGYKPTWRSLlgrFSEEDKERALSALE--RVGLADKAYQRADQLSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 154 QRQAVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKIiqVFE 233
Cdd:TIGR02315 150 QQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEI--VFD 227
|
250
....*....|....*.
gi 260158848 234 KEEKEALTE--EKLYQ 247
Cdd:TIGR02315 228 GAPSELDDEvlRHIYG 243
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
4-229 |
2.03e-37 |
|
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: 132.08 E-value: 2.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 4 RIENVHKTFYPNTnrshdALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKY- 82
Cdd:COG0411 6 EVRGLTKRFGGLV-----AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 83 ISRVYQNPlqGTAPRMTVAQNLSLALRRGLKRGLKKGYT---------AEELEQFKALLTplQLGLEERLDAEIGLLSGG 153
Cdd:COG0411 81 IARTFQNP--RLFPELTVLENVLVAAHARLGRGLLAALLrlprarreeREARERAEELLE--RVGLADRADEPAGNLSYG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 260158848 154 QRQAVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKII 229
Cdd:COG0411 157 QQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVI 232
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
3-227 |
7.29e-37 |
|
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: 128.27 E-value: 7.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTfYPNtnRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKY 82
Cdd:cd03228 1 IEFKNVSFS-YPG--RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 83 ISRVYQNP--LQGTaprmtVAQNLslalrrglkrglkkgytaeeleqfkalltplqlgleerldaeiglLSGGQRQAVSL 160
Cdd:cd03228 78 IAYVPQDPflFSGT-----IRENI---------------------------------------------LSGGQRQRIAI 107
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 260158848 161 LMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKelTALMITHNLSdALRYGNRLMMMHRGK 227
Cdd:cd03228 108 ARALLRDPPILILDEATSALDPETEALILEALRALAKGK--TVIVIAHRLS-TIRDADRIIVLDDGR 171
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
3-228 |
1.28e-36 |
|
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: 127.51 E-value: 1.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFypntnRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYM-GEAAVEHTAEYERak 81
Cdd:cd03230 1 IEVRNLSKRY-----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVlGKDIKKEPEEVKR-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 82 YISRVYQNPlqGTAPRMTVAQNLSLalrrglkrglkkgytaeeleqfkalltplqlgleerldaeigllSGGQRQAVSLL 161
Cdd:cd03230 74 RIGYLPEEP--SLYENLTVRENLKL--------------------------------------------SGGMKQRLALA 107
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 260158848 162 MATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEkELTALMITHNLSDALRYGNRLMMMHRGKI 228
Cdd:cd03230 108 QALLHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-236 |
1.79e-36 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 128.63 E-value: 1.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTfYPNtnrSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKY 82
Cdd:COG2884 2 IRFENVSKR-YPG---GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 83 ---ISRVYQNP--LqgtaPRMTVAQNLSLALR-RGLKRglkkgytAEELEQFKALLTplQLGLEERLDAEIGLLSGGQRQ 156
Cdd:COG2884 78 rrrIGVVFQDFrlL----PDRTVYENVALPLRvTGKSR-------KEIRRRVREVLD--LVGLSDKAKALPHELSGGEQQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 157 AVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEiIEEKELTALMITHNLSDALRYGNRLMMMHRGKIIQVFEKEE 236
Cdd:COG2884 145 RVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEE-INRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEARGV 223
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
3-229 |
1.70e-35 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 126.46 E-value: 1.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFypntnRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYER--- 79
Cdd:cd03261 1 IELRGLTKSF-----GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELyrl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 80 AKYISRVYQNPLQGTAprMTVAQNLSLALRRGLKrglkkgYTAEELEQfKALLTPLQLGLEERLDAEIGLLSGGQRQAVS 159
Cdd:cd03261 76 RRRMGMLFQSGALFDS--LTVFENVAFPLREHTR------LSEEEIRE-IVLEKLEAVGLRGAEDLYPAELSGGMKKRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 160 LLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKII 229
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIV 216
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-229 |
1.73e-35 |
|
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: 126.63 E-value: 1.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFypNTNRSHDaliDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKY 82
Cdd:COG1127 6 IEVRNLTKSF--GDRVVLD---GVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 83 ISR---VYQnplQG---TAprMTVAQNLSLALRRglkrglKKGYTAEELEQfKALLTpLQL-GLEERLD---AEiglLSG 152
Cdd:COG1127 81 RRRigmLFQ---GGalfDS--LTVFENVAFPLRE------HTDLSEAEIRE-LVLEK-LELvGLPGAADkmpSE---LSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 153 GQRQAVSLlmAtlRT----PELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKI 228
Cdd:COG1127 145 GMRKRVAL--A--RAlaldPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKI 220
|
.
gi 260158848 229 I 229
Cdd:COG1127 221 I 221
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-236 |
2.27e-35 |
|
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: 126.16 E-value: 2.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFyPNTNRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKY 82
Cdd:cd03258 2 IELKNVSKVF-GDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 83 ---ISRVYQ--NPLQgtapRMTVAQNLSLALRRGlkrGLKKgytAEELEQFKALLTplQLGLEERLDAEIGLLSGGQRQA 157
Cdd:cd03258 81 rrrIGMIFQhfNLLS----SRTVFENVALPLEIA---GVPK---AEIEERVLELLE--LVGLEDKADAYPAQLSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 260158848 158 VSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKIIQVFEKEE 236
Cdd:cd03258 149 VGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEE 227
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
3-231 |
2.34e-35 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 126.20 E-value: 2.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFYPNTnrshdALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAky 82
Cdd:cd03300 1 IELENVSKFYGGFV-----ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRP-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 83 ISRVYQNplQGTAPRMTVAQNLSLALRRglkRGLKKGYTAEELEQFKALLtplqlGLEERLDAEIGLLSGGQRQAVSLLM 162
Cdd:cd03300 74 VNTVFQN--YALFPHLTVFENIAFGLRL---KKLPKAEIKERVAEALDLV-----QLEGYANRKPSQLSGGQQQRVAIAR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 163 ATLRTPELLLLDEHTAALDPKTqRKIMQLT-KEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKIIQV 231
Cdd:cd03300 144 ALVNEPKVLLLDEPLGALDLKL-RKDMQLElKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQI 212
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
27-228 |
2.41e-35 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 126.24 E-value: 2.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 27 NLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMgeAAVEHTAEYERAKYISRVYQ-NPLqgtAPRMTVAQNLS 105
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTL--NGQDHTTTPPSRRPVSMLFQeNNL---FSHLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 106 LALRRGLKrglkkgYTAEELEQFKALLTplQLGLEERLDAEIGLLSGGQRQAVSLLMATLRTPELLLLDEHTAALDPKTQ 185
Cdd:PRK10771 94 LGLNPGLK------LNAAQREKLHAIAR--QMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALR 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 260158848 186 RKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKI 228
Cdd:PRK10771 166 QEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
3-228 |
4.92e-35 |
|
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: 124.56 E-value: 4.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFypntnRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAE--YERA 80
Cdd:cd03262 1 IEIKNLHKSF-----GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKniNELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 81 KYISRVYQN-PLqgtAPRMTVAQNLSLALRRglKRGLKKgytAEELEQFKALLTplQLGLEERLDAEIGLLSGGQRQAVS 159
Cdd:cd03262 76 QKVGMVFQQfNL---FPHLTVLENITLAPIK--VKGMSK---AEAEERALELLE--KVGLADKADAYPAQLSGGQQQRVA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 260158848 160 LLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKeLTALMITHNLSDALRYGNRLMMMHRGKI 228
Cdd:cd03262 146 IARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEG-MTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
18-229 |
6.39e-35 |
|
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: 124.53 E-value: 6.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 18 RSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEaaVEHTAEYERAKYISRVYQ-NPLqgtAP 96
Cdd:cd03298 9 SYGEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING--VDVTAAPPADRPVSMLFQeNNL---FA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 97 RMTVAQNLSLALRRGLKrglkkgYTAEELEQFKALLTplQLGLEERLDAEIGLLSGGQRQAVSLLMATLRTPELLLLDEH 176
Cdd:cd03298 84 HLTVEQNVGLGLSPGLK------LTAEDRQAIEVALA--RVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 260158848 177 TAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKII 229
Cdd:cd03298 156 FAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-230 |
1.17e-34 |
|
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: 131.49 E-value: 1.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 2 DIRIENVhkTF-YPNtnRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERA 80
Cdd:COG2274 473 DIELENV--SFrYPG--DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLR 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 81 KYISRVYQNP--LQGTaprmtVAQNLSLAlrrglkrglKKGYTAEELEQfkAL----LTPLQLGLEERLDAEIG----LL 150
Cdd:COG2274 549 RQIGVVLQDVflFSGT-----IRENITLG---------DPDATDEEIIE--AArlagLHDFIEALPMGYDTVVGeggsNL 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 151 SGGQRQAVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKelTALMITHNLSdALRYGNRLMMMHRGKIIQ 230
Cdd:COG2274 613 SGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGR--TVIIIAHRLS-TIRLADRIIVLDKGRIVE 689
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
3-258 |
3.44e-34 |
|
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: 124.49 E-value: 3.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFYPNTNRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERA-- 80
Cdd:TIGR04521 1 IKLKNVSYIYQPGTPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKdl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 81 -KYISRVYQNP---LQGTaprmTVA-------QNLslalrrglkrglkkGYTAEELEQ--FKALLtplQLGLEErldaEI 147
Cdd:TIGR04521 81 rKKVGLVFQFPehqLFEE----TVYkdiafgpKNL--------------GLSEEEAEErvKEALE---LVGLDE----EY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 148 GL-----LSGGQRQAVSL--LMATlrTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRL 220
Cdd:TIGR04521 136 LErspfeLSGGQMRRVAIagVLAM--EPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRV 213
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 260158848 221 MMMHRGKII------QVFEKE---EKEALTEEKLYQLMAELDEADFN 258
Cdd:TIGR04521 214 IVMHKGKIVldgtprEVFSDVdelEKIGLDVPEITELARKLKEKGLP 260
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
4-227 |
4.50e-34 |
|
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: 120.43 E-value: 4.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 4 RIENVHKTFYPNTnrshdALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKYI 83
Cdd:cd00267 1 EIENLSFRYGGRT-----ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 84 SRVYQnplqgtaprmtvaqnlslalrrglkrglkkgytaeeleqfkalltplqlgleerldaeiglLSGGQRQAVSLLMA 163
Cdd:cd00267 76 GYVPQ-------------------------------------------------------------LSGGQRQRVALARA 94
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 260158848 164 TLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKeLTALMITHNLSDALRYGNRLMMMHRGK 227
Cdd:cd00267 95 LLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEG-RTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-230 |
4.99e-34 |
|
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: 128.72 E-value: 4.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 2 DIRIENVHKTfYPNTNRshdALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAK 81
Cdd:COG4988 336 SIELEDVSFS-YPGGRP---ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 82 YISRVYQNP--LQGtaprmTVAQNLSLAlrrglkrglKKGYTAEELEQfkAL----LTPLQLGLEERLDAEIG----LLS 151
Cdd:COG4988 412 QIAWVPQNPylFAG-----TIRENLRLG---------RPDASDEELEA--ALeaagLDEFVAALPDGLDTPLGeggrGLS 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 260158848 152 GGQRQAVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKelTALMITHNLSDaLRYGNRLMMMHRGKIIQ 230
Cdd:COG4988 476 GGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLAL-LAQADRILVLDDGRIVE 551
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
3-258 |
5.53e-34 |
|
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: 123.69 E-value: 5.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTfYPNTNRshDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMG--EAAVEHTAEYERA 80
Cdd:TIGR04520 1 IEVENVSFS-YPESEK--PALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDglDTLDEENLWEIRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 81 KyISRVYQNP---LQGTaprmTVAQNLSLALR-RGLKRglkkgytaEELEQF--KALLtplQLGLEERLDAEIGLLSGGQ 154
Cdd:TIGR04520 78 K-VGMVFQNPdnqFVGA----TVEDDVAFGLEnLGVPR--------EEMRKRvdEALK---LVGMEDFRDREPHLLSGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 155 RQAVSL--LMAtLRtPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRyGNRLMMMHRGKII--- 229
Cdd:TIGR04520 142 KQRVAIagVLA-MR-PDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVaeg 218
|
250 260 270
....*....|....*....|....*....|....*..
gi 260158848 230 ---QVFEKEEKeaLTEEKL-----YQLMAELDEADFN 258
Cdd:TIGR04520 219 tprEIFSQVEL--LKEIGLdvpfiTELAKALKKRGIP 253
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-236 |
1.69e-33 |
|
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: 121.68 E-value: 1.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 1 MDIRIENVHKTFypntnRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERA 80
Cdd:cd03296 1 MSIEVRNVSKRF-----GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 81 kyISRVYQNplQGTAPRMTVAQNLSLALRrgLKRGLKKGYTAEELEQFKALLTPLQL-GLEERLDAEiglLSGGQRQAVS 159
Cdd:cd03296 76 --VGFVFQH--YALFRHMTVFDNVAFGLR--VKPRSERPPEAEIRAKVHELLKLVQLdWLADRYPAQ---LSGGQRQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 260158848 160 LLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKIIQVFEKEE 236
Cdd:cd03296 147 LARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDE 223
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-233 |
3.43e-33 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 120.48 E-value: 3.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFypntnRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTaEYERAKY 82
Cdd:COG1126 2 IEIENLHKSF-----GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDS-KKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 83 ISR---VYQNP-LqgtAPRMTVAQNLSLALRRGLKRGlkkgyTAEELEQFKALLTplQLGLEERLDAEIGLLSGGQRQAV 158
Cdd:COG1126 76 RRKvgmVFQQFnL---FPHLTVLENVTLAPIKVKKMS-----KAEAEERAMELLE--RVGLADKADAYPAQLSGGQQQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 159 ----SLLMAtlrtPELLLLDEHTAALDPktqrkimQLTKEIIE------EKELTALMITHNLSDALRYGNRLMMMHRGKI 228
Cdd:COG1126 146 aiarALAME----PKVMLFDEPTSALDP-------ELVGEVLDvmrdlaKEGMTMVVVTHEMGFAREVADRVVFMDGGRI 214
|
250
....*....|.
gi 260158848 229 I------QVFE 233
Cdd:COG1126 215 VeegppeEFFE 225
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-233 |
6.63e-33 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 120.74 E-value: 6.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 1 MDIRIENVHkTFYPNTNRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEyERA 80
Cdd:COG4525 2 SMLTVRHVS-VRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGA-DRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 81 KyisrVYQNplQGTAPRMTVAQNLSLALR-RGLKRglkkgytAEELEQFKALLTplQLGLEERLDAEIGLLSGGQRQAVS 159
Cdd:COG4525 80 V----VFQK--DALLPWLNVLDNVAFGLRlRGVPK-------AERRARAEELLA--LVGLADFARRRIWQLSGGMRQRVG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 260158848 160 LLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMM--HRGKIIQVFE 233
Cdd:COG4525 145 IARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMspGPGRIVERLE 220
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-229 |
1.37e-32 |
|
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: 121.31 E-value: 1.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFyPNTNRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFP---LDKGHIY--------MGEAAV 71
Cdd:COG0444 2 LEVRNLKVYF-PTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILfdgedllkLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 72 EHTaeyeRAKYISRVYQNPLqgTA--PRMTVAQNLSLALRrgLKRGLKKgytAEELEQFKALLTplQLGL---EERLDA- 145
Cdd:COG0444 81 RKI----RGREIQMIFQDPM--TSlnPVMTVGDQIAEPLR--IHGGLSK---AEARERAIELLE--RVGLpdpERRLDRy 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 146 --EiglLSGGQRQAVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMM 223
Cdd:COG0444 148 phE---LSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVM 224
|
....*.
gi 260158848 224 HRGKII 229
Cdd:COG0444 225 YAGRIV 230
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-230 |
2.59e-32 |
|
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: 118.10 E-value: 2.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 2 DIRIENVHKTFypntNRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAK 81
Cdd:cd03254 2 EIEFENVNFSY----DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 82 YISRVYQNP--LQGTaprmtVAQNLSLAlrrglkrglKKGYTAEELEQFKALLTPLQLG--LEERLDAEIG----LLSGG 153
Cdd:cd03254 78 MIGVVLQDTflFSGT-----IMENIRLG---------RPNATDEEVIEAAKEAGAHDFImkLPNGYDTVLGenggNLSQG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 260158848 154 QRQAVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKelTALMITHNLSdALRYGNRLMMMHRGKIIQ 230
Cdd:cd03254 144 ERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGR--TSIIIAHRLS-TIKNADKILVLDDGKIIE 217
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-230 |
5.18e-32 |
|
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: 123.34 E-value: 5.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 2 DIRIENVhkTF-YPNTNRshDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERA 80
Cdd:COG4987 333 SLELEDV--SFrYPGAGR--PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 81 KYISRVYQNP--LQGTaprmtVAQNLSLAlrrglkrglKKGYTAEELEQfkAL----LTPLQLGLEERLDAEIG----LL 150
Cdd:COG4987 409 RRIAVVPQRPhlFDTT-----LRENLRLA---------RPDATDEELWA--ALervgLGDWLAALPDGLDTWLGeggrRL 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 151 SGGQRQAVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKelTALMITHNLSdALRYGNRLMMMHRGKIIQ 230
Cdd:COG4987 473 SGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLA-GLERMDRILVLEDGRIVE 549
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-237 |
6.30e-32 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 118.58 E-value: 6.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVhkTF-YPNTNRShdALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAK 81
Cdd:PRK13635 6 IRVEHI--SFrYPDAATY--ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 82 YISRVYQNP---LQGTaprmTVAQNLSLALR-RGLKRglkkgytAEELEQFKALLTplQLGLEERLDAEIGLLSGGQRQA 157
Cdd:PRK13635 82 QVGMVFQNPdnqFVGA----TVQDDVAFGLEnIGVPR-------EEMVERVDQALR--QVGMEDFLNREPHRLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 158 VSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRyGNRLMMMHRGKII------QV 231
Cdd:PRK13635 149 VAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILeegtpeEI 227
|
....*.
gi 260158848 232 FEKEEK 237
Cdd:PRK13635 228 FKSGHM 233
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
3-231 |
1.19e-31 |
|
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: 116.51 E-value: 1.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVhkTFYPNtnrSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPL-----DKGHIYMGEAAVEHTAE- 76
Cdd:cd03260 1 IELRDL--NVYYG---DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVd 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 77 -YERAKYISRVYQNPlqgTAPRMTVAQNLSLALRrglKRGLKKGYTAEELEqfKALLTPLQLGLEERLDAEIGLLSGGQR 155
Cdd:cd03260 76 vLELRRRVGMVFQKP---NPFPGSIYDNVAYGLR---LHGIKLKEELDERV--EEALRKAALWDEVKDRLHALGLSGGQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 260158848 156 QAVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIieEKELTALMITHNLSDALRYGNRLMMMHRGKIIQV 231
Cdd:cd03260 148 QRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAEL--KKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEF 221
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-236 |
2.55e-31 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 119.17 E-value: 2.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFypntnRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAky 82
Cdd:PRK11607 20 LEIRNLTKSF-----DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRP-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 83 ISRVYQNplQGTAPRMTVAQNLSLalrrGLKRG-LKKGYTAEELEQFKALLTplqlgLEERLDAEIGLLSGGQRQAVSLL 161
Cdd:PRK11607 93 INMMFQS--YALFPHMTVEQNIAF----GLKQDkLPKAEIASRVNEMLGLVH-----MQEFAKRKPHQLSGGQRQRVALA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 260158848 162 MATLRTPELLLLDEHTAALDPKTqRKIMQL-TKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKIIQVFEKEE 236
Cdd:PRK11607 162 RSLAKRPKLLLLDEPMGALDKKL-RDRMQLeVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEE 236
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
4-229 |
2.59e-31 |
|
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: 115.46 E-value: 2.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 4 RIENVHkTFYpntNRSHdALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKY- 82
Cdd:COG0410 5 EVENLH-AGY---GGIH-VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 83 ISRVYQNplQGTAPRMTVAQNLSLALRRGLKRGLKKGYTAEELEQFkalltPLqlgLEERLDAEIGLLSGGQRQAVSLLM 162
Cdd:COG0410 80 IGYVPEG--RRIFPSLTVEENLLLGAYARRDRAEVRADLERVYELF-----PR---LKERRRQRAGTLSGGEQQMLAIGR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 260158848 163 ATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKeLTALMITHNLSDALRYGNRLMMMHRGKII 229
Cdd:COG0410 150 ALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREG-VTILLVEQNARFALEIADRAYVLERGRIV 215
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-230 |
4.39e-31 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 120.65 E-value: 4.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 2 DIRIENVhkTF-YPNtnrSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAV-EHTAEYER 79
Cdd:COG1132 339 EIEFENV--SFsYPG---DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIrDLTLESLR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 80 AKyISRVYQNP--LQGTaprmtVAQNLSLAlrrglkrglKKGYTAEELEQF--KALLTPLQLGLEERLDAEIG----LLS 151
Cdd:COG1132 414 RQ-IGVVPQDTflFSGT-----IRENIRYG---------RPDATDEEVEEAakAAQAHEFIEALPDGYDTVVGergvNLS 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 260158848 152 GGQRQAVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKelTALMITHNLSdALRYGNRLMMMHRGKIIQ 230
Cdd:COG1132 479 GGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGR--TTIVIAHRLS-TIRNADRILVLDDGRIVE 554
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
3-236 |
4.62e-31 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 115.09 E-value: 4.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFypntNRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKY 82
Cdd:cd03295 1 IEFENVTKRY----GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 83 ISRVYQNplQGTAPRMTVAQNLSLALRrglkrgLKKGYTAEELEQFKALLTPLQLGLEERLDAEIGLLSGGQRQAVSLLM 162
Cdd:cd03295 77 IGYVIQQ--IGLFPHMTVEENIALVPK------LLKWPKEKIRERADELLALVGLDPAEFADRYPHELSGGQQQRVGVAR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 260158848 163 ATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKIIQVFEKEE 236
Cdd:cd03295 149 ALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDE 222
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
3-229 |
5.87e-31 |
|
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: 114.14 E-value: 5.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFypnTNRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEaavehtaeYERAKY 82
Cdd:cd03263 1 LQIRNLTKTY---KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYING--------YSIRTD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 83 ISRVYQN----PlQGTA--PRMTVAQNLSLALRrgLKrGLKKGYTAEELEQFKalltpLQLGLEERLDAEIGLLSGGQRQ 156
Cdd:cd03263 70 RKAARQSlgycP-QFDAlfDELTVREHLRFYAR--LK-GLPKSEIKEEVELLL-----RVLGLTDKANKRARTLSGGMKR 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 260158848 157 AVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKelTALMITHNLSDALRYGNRLMMMHRGKII 229
Cdd:cd03263 141 KLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
23-252 |
7.69e-31 |
|
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: 114.49 E-value: 7.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 23 LIDINLTIHKGDFITIVGGNGAGKSTFLNAISG-SFPLDKGHIYMGEAAVEHTAEYerakyiSRVYQNplQGTAPRMTVA 101
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGlAQPTSGGVILEGKQITEPGPDR------MVVFQN--YSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 102 QNLSLALRRGLkRGLKKGYTAEELEQFKALLtplqlGLEERLDAEIGLLSGGQRQAVSLLMATLRTPELLLLDEHTAALD 181
Cdd:TIGR01184 73 ENIALAVDRVL-PDLSKSERRAIVEEHIALV-----GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 182 PKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRG---KIIQVFE------KEEKEALTEEKLYQLMAEL 252
Cdd:TIGR01184 147 ALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGpaaNIGQILEvpfprpRDRLEVVEDPSYYDLRNEA 226
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
3-236 |
1.30e-30 |
|
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: 114.66 E-value: 1.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFYPNTNRSHD-------------------ALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGH 63
Cdd:cd03294 1 IKIKGLYKIFGKNPQKAFKllakgkskeeilkktgqtvGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 64 IYM-GE--AAVEHTAEYE-RAKYISRVYQNplQGTAPRMTVAQNLSLALR-RGLKRGLKKGYTAEELEQfkalltplqLG 138
Cdd:cd03294 81 VLIdGQdiAAMSRKELRElRRKKISMVFQS--FALLPHRTVLENVAFGLEvQGVPRAEREERAAEALEL---------VG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 139 LEERLDAEIGLLSGGQRQAVSLLMATLRTPELLLLDEHTAALDPkTQRKIMQ-LTKEIIEEKELTALMITHNLSDALRYG 217
Cdd:cd03294 150 LEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDP-LIRREMQdELLRLQAELQKTIVFITHDLDEALRLG 228
|
250
....*....|....*....
gi 260158848 218 NRLMMMHRGKIIQVFEKEE 236
Cdd:cd03294 229 DRIAIMKDGRLVQVGTPEE 247
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-244 |
1.35e-30 |
|
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: 114.18 E-value: 1.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFypntnRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYM-GEAAVEHTAEYERAk 81
Cdd:COG4555 2 IEVENLSKKY-----GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIdGEDVRKEPREARRQ- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 82 yISRVYQNPlqGTAPRMTVAQNLS-LALRRGLKRGLKKGYTAEELEQFkalltplqlGLEERLDAEIGLLSGGQRQAVSL 160
Cdd:COG4555 76 -IGVLPDER--GLYDRLTVRENIRyFAELYGLFDEELKKRIEELIELL---------GLEEFLDRRVGELSTGMKKKVAL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 161 LMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKeLTALMITHNLSDALRYGNRLMMMHRGKIIQVFEKEEKEAL 240
Cdd:COG4555 144 ARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEG-KTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE 222
|
....
gi 260158848 241 TEEK 244
Cdd:COG4555 223 IGEE 226
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
25-222 |
2.98e-30 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 112.19 E-value: 2.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 25 DINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLD---KGHIYMGEAAVEHTAEYERAkyISRVYQNPLqgTAPRMTVA 101
Cdd:COG4136 19 PLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQRR--IGILFQDDL--LFPHLSVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 102 QNLSLALRRGLKRGLKKGYTAEELEQfkalltplqLGLEERLDAEIGLLSGGQRQAVSLLMATLRTPELLLLDEHTAALD 181
Cdd:COG4136 95 ENLAFALPPTIGRAQRRARVEQALEE---------AGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 260158848 182 PKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMM 222
Cdd:COG4136 166 AALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAAGRVLDL 206
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-258 |
2.49e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 111.68 E-value: 2.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 1 MDIRIENVHKTFYPNTNRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGeaAVEHTAEYERA 80
Cdd:PRK13637 1 MSIKIENLTHIYMEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIID--GVDITDKKVKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 81 KYISR----VYQNPlQGTAPRMTVAQNLSLALRRglkRGLKKGytaEELEQFKALLTPLQLGLEERLDAEIGLLSGGQRQ 156
Cdd:PRK13637 79 SDIRKkvglVFQYP-EYQLFEETIEKDIAFGPIN---LGLSEE---EIENRVKRAMNIVGLDYEDYKDKSPFELSGGQKR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 157 AVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKII------Q 230
Cdd:PRK13637 152 RVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCElqgtprE 231
|
250 260 270
....*....|....*....|....*....|.
gi 260158848 231 VF---EKEEKEALTEEKLYQLMAELDEADFN 258
Cdd:PRK13637 232 VFkevETLESIGLAVPQVTYLVRKLRKKGFN 262
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1-230 |
3.29e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 111.65 E-value: 3.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 1 MDIRIENVHKTFYPNTNRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERA 80
Cdd:PRK13634 1 MDITFQKVEHRYQYKTPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 81 KYISR----VYQNPlQGTAPRMTVAQNLSLAlrrGLKRGLKKgytAEELEQFKALLTPLQLGlEERLDAEIGLLSGGQRQ 156
Cdd:PRK13634 81 KPLRKkvgiVFQFP-EHQLFEETVEKDICFG---PMNFGVSE---EDAKQKAREMIELVGLP-EELLARSPFELSGGQMR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 260158848 157 AVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKIIQ 230
Cdd:PRK13634 153 RVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFL 226
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
24-230 |
4.36e-29 |
|
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: 109.31 E-value: 4.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 24 IDINLTIhKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVE------HTAEYERAkyISRVYQNplQGTAPR 97
Cdd:cd03297 15 LKIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFdsrkkiNLPPQQRK--IGLVFQQ--YALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 98 MTVAQNLSLalrrglkrGLKKGYTAEELEQFKALLTplQLGLEERLDAEIGLLSGGQRQAVSLLMATLRTPELLLLDEHT 177
Cdd:cd03297 90 LNVRENLAF--------GLKRKRNREDRISVDELLD--LLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 260158848 178 AALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKIIQ 230
Cdd:cd03297 160 SALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQY 212
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
3-228 |
6.34e-29 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 109.41 E-value: 6.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFYPNTnrshdALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAky 82
Cdd:PRK09493 2 IEFKNVSKHFGPTQ-----VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERL-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 83 ISR----VYQnplQ-GTAPRMTVAQNLSLALRRglKRGLKKgytAEELEQFKALLTplQLGLEERLDAEIGLLSGGQRQA 157
Cdd:PRK09493 75 IRQeagmVFQ---QfYLFPHLTALENVMFGPLR--VRGASK---EEAEKQARELLA--KVGLAERAHHYPSELSGGQQQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 260158848 158 VSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKeLTALMITHNLSDALRYGNRLMMMHRGKI 228
Cdd:PRK09493 145 VAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEG-MTMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-249 |
5.73e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 111.26 E-value: 5.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFYPNTnrshdALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEH--TAEYERA 80
Cdd:COG1129 5 LEMRGISKSFGGVK-----ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFrsPRDAQAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 81 KyISRVYQNPLQgtAPRMTVAQNLSLA---LRRGLKRglkkgyTAEELEQFKALLTplQLGLEERLDAEIGLLSGGQRQA 157
Cdd:COG1129 80 G-IAIIHQELNL--VPNLSVAENIFLGrepRRGGLID------WRAMRRRARELLA--RLGLDIDPDTPVGDLSVAQQQL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 158 VSLLMATLRTPELLLLDEHTAALDPK-TQR--KIMqltkeiieeKELTA-----LMITHNLSDALRYGNRLMMMHRGKII 229
Cdd:COG1129 149 VEIARALSRDARVLILDEPTASLTEReVERlfRII---------RRLKAqgvaiIYISHRLDEVFEIADRVTVLRDGRLV 219
|
250 260
....*....|....*....|
gi 260158848 230 QVFEKEEkeaLTEEKLYQLM 249
Cdd:COG1129 220 GTGPVAE---LTEDELVRLM 236
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-249 |
7.13e-28 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 111.27 E-value: 7.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFYPNTnrshdALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVE----HTAeye 78
Cdd:COG3845 6 LELRGITKRFGGVV-----ANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRirspRDA--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 79 RAKYISRVYQNPLQgtAPRMTVAQNLSLAL--RRGLKRGLKKgyTAEELEQFKAlltplQLGLEERLDAEIGLLSGGQRQ 156
Cdd:COG3845 78 IALGIGMVHQHFML--VPNLTVAENIVLGLepTKGGRLDRKA--ARARIRELSE-----RYGLDVDPDAKVEDLSVGEQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 157 AVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEkELTALMITHNLSDALRYGNRLMMMHRGKIIQVFEKEE 236
Cdd:COG3845 149 RVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAE-GKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAE 227
|
250
....*....|...
gi 260158848 237 keaLTEEKLYQLM 249
Cdd:COG3845 228 ---TSEEELAELM 237
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
25-178 |
1.13e-27 |
|
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: 103.88 E-value: 1.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 25 DINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHI-YMGEAAVEHTAEYERAKyISRVYQNPLQGtaPRMTVAQN 103
Cdd:pfam00005 3 NVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTIlLDGQDLTDDERKSLRKE-IGYVFQDPQLF--PRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 260158848 104 LSLALRrglKRGLKKGYTAEELEQFKALLtPLQLGLEERLDAEIGLLSGGQRQAVSLLMATLRTPELLLLDEHTA 178
Cdd:pfam00005 80 LRLGLL---LKGLSKREKDARAEEALEKL-GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
3-231 |
1.88e-27 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 108.50 E-value: 1.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFypntnRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHT-AEyerAK 81
Cdd:PRK09452 15 VELRGISKSF-----DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVpAE---NR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 82 YISRVYQNplQGTAPRMTVAQNLSLALRrglkrgLKKGYTAEELEQFKALLTPLQlgLEERLDAEIGLLSGGQRQAVSLL 161
Cdd:PRK09452 87 HVNTVFQS--YALFPHMTVFENVAFGLR------MQKTPAAEITPRVMEALRMVQ--LEEFAQRKPHQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 260158848 162 MATLRTPELLLLDEHTAALDPKTqRKIMQLtkeiiEEKEL------TALMITHNLSDALRYGNRLMMMHRGKIIQV 231
Cdd:PRK09452 157 RAVVNKPKVLLLDESLSALDYKL-RKQMQN-----ELKALqrklgiTFVFVTHDQEEALTMSDRIVVMRDGRIEQD 226
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
3-230 |
2.98e-27 |
|
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: 104.20 E-value: 2.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFypntnRSHDALIDINLTIHKGdFITIVGGNGAGKSTFLNAISGSFPLDKGHIYM-GEAAVEHTAEYERAk 81
Cdd:cd03264 1 LQLENLTKRY-----GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIdGQDVLKQPQKLRRR- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 82 yISRVYQNPlqGTAPRMTVAQNLS-LALRRGLKRGLKKGYTAEELEQfkalltplqLGLEERLDAEIGLLSGGQRQAVSL 160
Cdd:cd03264 74 -IGYLPQEF--GVYPNFTVREFLDyIAWLKGIPSKEVKARVDEVLEL---------VNLGDRAKKKIGSLSGGMRRRVGI 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 161 LMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKelTALMITHNLSDALRYGNRLMMMHRGKIIQ 230
Cdd:cd03264 142 AQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKGKLVF 209
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-191 |
1.07e-26 |
|
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: 102.94 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 1 MDIRIENVHKTFypntnrsHDALI--DINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHI-YMGEAAVEHTAEY 77
Cdd:COG4133 1 MMLEAENLSCRR-------GERLLfsGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVlWNGEPIRDAREDY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 78 ERAkyisRVYQNPLQGTAPRMTVAQNLSLALRrglkrgLKKGYTAEEleQFKALLTplQLGLEERLDAEIGLLSGGQRQA 157
Cdd:COG4133 74 RRR----LAYLGHADGLKPELTVRENLRFWAA------LYGLRADRE--AIDEALE--AVGLAGLADLPVRQLSAGQKRR 139
|
170 180 190
....*....|....*....|....*....|....
gi 260158848 158 VSLLMATLRTPELLLLDEHTAALDPKTQRKIMQL 191
Cdd:COG4133 140 VALARLLLSPAPLWLLDEPFTALDAAGVALLAEL 173
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
4-250 |
1.21e-26 |
|
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: 103.37 E-value: 1.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 4 RIENVHkTFYpntNRSHdALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKY- 82
Cdd:TIGR03410 2 EVSNLN-VYY---GQSH-ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 83 ISRVYQNplQGTAPRMTVAQNLSLALRrGLKRGLKKgYTAEELEQFKALltplqlglEERLDAEIGLLSGGQRQAVSLLM 162
Cdd:TIGR03410 77 IAYVPQG--REIFPRLTVEENLLTGLA-ALPRRSRK-IPDEIYELFPVL--------KEMLGRRGGDLSGGQQQQLAIAR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 163 ATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKIIqvfEKEEKEALTE 242
Cdd:TIGR03410 145 ALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVV---ASGAGDELDE 221
|
....*...
gi 260158848 243 EKLYQLMA 250
Cdd:TIGR03410 222 DKVRRYLA 229
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-229 |
1.80e-26 |
|
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: 100.97 E-value: 1.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFYPNTnrshdALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYE-RAK 81
Cdd:cd03216 1 LELRGITKRFGGVK-----ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 82 YISRVYQnplqgtaprmtvaqnlslalrrglkrglkkgytaeeleqfkalltplqlgleerldaeiglLSGGQRQAVSLL 161
Cdd:cd03216 76 GIAMVYQ-------------------------------------------------------------LSVGERQMVEIA 94
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 260158848 162 MATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKeLTALMITHNLSDALRYGNRLMMMHRGKII 229
Cdd:cd03216 95 RALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQG-VAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
4-229 |
2.28e-26 |
|
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: 101.95 E-value: 2.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 4 RIENVHKTFYPNTNRshdaLIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEaavEHTAEYERAKYI 83
Cdd:cd03226 1 RIENISFSYKKGTEI----LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 84 SRVYQNP---LQGTaprmTVAQNlslaLRRGLKRGLKKGYTAEEleqfkaLLTPLQL-GLEERLDAEiglLSGGQRQAVS 159
Cdd:cd03226 74 GYVMQDVdyqLFTD----SVREE----LLLGLKELDAGNEQAET------VLKDLDLyALKERHPLS---LSGGQKQRLA 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 160 LLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKElTALMITHNLSDALRYGNRLMMMHRGKII 229
Cdd:cd03226 137 IAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGK-AVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
3-253 |
6.13e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 102.38 E-value: 6.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFYPNTNrshDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYM-GEAAVEHTAEYERaK 81
Cdd:PRK13632 8 IKVENVSFSYPNSEN---NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIdGITISKENLKEIR-K 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 82 YISRVYQNP---LQGTaprmTVAQNLSLALRrglkrglKKGYTAEELEQFKALLTpLQLGLEERLDAEIGLLSGGQRQAV 158
Cdd:PRK13632 84 KIGIIFQNPdnqFIGA----TVEDDIAFGLE-------NKKVPPKKMKDIIDDLA-KKVGMEDYLDKEPQNLSGGQKQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 159 SLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRyGNRLMMMHRGKIIQVfeKEEKE 238
Cdd:PRK13632 152 AIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQ--GKPKE 228
|
250
....*....|....*
gi 260158848 239 ALTEEKLYQLmAELD 253
Cdd:PRK13632 229 ILNNKEILEK-AKID 242
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-230 |
7.30e-26 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 101.63 E-value: 7.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 1 MDIRIENVHKtFYPntnrSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAI-------SGSFPLDKGHIYMGEAAVEH 73
Cdd:PRK11124 1 MSIQLNGINC-FYG----AHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprSGTLNIAGNHFDFSKTPSDK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 74 TAEYERAKyISRVYQNplQGTAPRMTVAQNLSLALRRGLkrGLKKgytAEELEQFKALLTPLQLglEERLDAEIGLLSGG 153
Cdd:PRK11124 76 AIRELRRN-VGMVFQQ--YNLWPHLTVQQNLIEAPCRVL--GLSK---DQALARAEKLLERLRL--KPYADRFPLHLSGG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 260158848 154 QRQAVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEiIEEKELTALMITHNLSDALRYGNRLMMMHRGKIIQ 230
Cdd:PRK11124 146 QQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRE-LAETGITQVIVTHEVEVARKTASRVVYMENGHIVE 221
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
3-229 |
1.27e-25 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 102.85 E-value: 1.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFyPNTNRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGsfpLDK---GHIYMGEaaVEHTAEYER 79
Cdd:COG1135 2 IELENLSKTF-PTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINL---LERptsGSVLVDG--VDLTALSER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 80 A-----KYISRVYQ--NPLQgtapRMTVAQNLSLALRRGlkrGLKKGYTAE---ELeqfkalltpLQL-GLEERLDAEIG 148
Cdd:COG1135 76 ElraarRKIGMIFQhfNLLS----SRTVAENVALPLEIA---GVPKAEIRKrvaEL---------LELvGLSDKADAYPS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 149 LLSGGQRQAVS----LlmATlrTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMH 224
Cdd:COG1135 140 QLSGGQKQRVGiaraL--AN--NPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLE 215
|
....*
gi 260158848 225 RGKII 229
Cdd:COG1135 216 NGRIV 220
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-229 |
1.72e-25 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 99.97 E-value: 1.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 2 DIRIENVhkTF-YPNTnrSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERA 80
Cdd:cd03245 2 RIEFRNV--SFsYPNQ--EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 81 KYISRVYQNP--LQGTaprmtVAQNLSLALRRGlkrglkkgyTAEELEQFKAL--LTPLQLGLEERLDAEIG----LLSG 152
Cdd:cd03245 78 RNIGYVPQDVtlFYGT-----LRDNITLGAPLA---------DDERILRAAELagVTDFVNKHPNGLDLQIGergrGLSG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 260158848 153 GQRQAVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKelTALMITHNLSdALRYGNRLMMMHRGKII 229
Cdd:cd03245 144 GQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDK--TLIIITHRPS-LLDLVDRIIVMDSGRIV 217
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-236 |
2.24e-25 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 102.47 E-value: 2.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 1 MDIRIENVHKTFypntNRSHdALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTaeYERA 80
Cdd:PRK10851 1 MSIEIANIKKSF----GRTQ-VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL--HARD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 81 KYISRVYQNplQGTAPRMTVAQNLSLALRRGLKRglKKGYTAEELEQFKALLTPLQLG-LEERLDAEiglLSGGQRQAVS 159
Cdd:PRK10851 74 RKVGFVFQH--YALFRHMTVFDNIAFGLTVLPRR--ERPNAAAIKAKVTQLLEMVQLAhLADRYPAQ---LSGGQKQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 260158848 160 LLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKIIQVFEKEE 236
Cdd:PRK10851 147 LARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQ 223
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
3-229 |
3.16e-25 |
|
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: 99.53 E-value: 3.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTF-----------------YPNTNRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIy 65
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 66 mgeaavehtaeyERAKYISrvyqNPLQGTA---PRMTVAQNlslALRRGLKRGLKKGYTAEELEQFKALltplqLGLEER 142
Cdd:cd03220 80 ------------TVRGRVS----SLLGLGGgfnPELTGREN---IYLNGRLLGLSRKEIDEKIDEIIEF-----SELGDF 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 143 LDAEIGLLSGGQRQAVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKElTALMITHNLSDALRYGNRLMM 222
Cdd:cd03220 136 IDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGK-TVILVSHDPSSIKRLCDRALV 214
|
....*..
gi 260158848 223 MHRGKII 229
Cdd:cd03220 215 LEKGKIR 221
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
25-229 |
5.02e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 99.85 E-value: 5.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 25 DINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKYisrvyqnplqgtapRMTVAQNL 104
Cdd:PRK13548 20 DVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARR--------------RAVLPQHS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 105 SLA--------LRRGL-KRGLKKGYTAEELEQfkAL-LTPLqLGLEERLDAEiglLSGGQRQAVSL------LMATLRTP 168
Cdd:PRK13548 86 SLSfpftveevVAMGRaPHGLSRAEDDALVAA--ALaQVDL-AHLAGRDYPQ---LSGGEQQRVQLarvlaqLWEPDGPP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 260158848 169 ELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKII 229
Cdd:PRK13548 160 RWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLV 220
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
3-248 |
5.84e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 100.06 E-value: 5.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTfYPNTNrshDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYM-GEAAVEHTAEYERAK 81
Cdd:PRK13644 2 IRLENVSYS-YPDGT---PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVsGIDTGDFSKLQGIRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 82 YISRVYQNPLQGTAPRmTVAQNLSlalrrglkrglkkgYTAEELeqfkaLLTPLQlgLEERLD---AEIGL--------- 149
Cdd:PRK13644 78 LVGIVFQNPETQFVGR-TVEEDLA--------------FGPENL-----CLPPIE--IRKRVDralAEIGLekyrhrspk 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 150 -LSGGQRQAVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEiIEEKELTALMITHNLSDaLRYGNRLMMMHRGKI 228
Cdd:PRK13644 136 tLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKK-LHEKGKTIVYITHNLEE-LHDADRIIVMDRGKI 213
|
250 260
....*....|....*....|
gi 260158848 229 iqVFEKEEKEALTEEKLYQL 248
Cdd:PRK13644 214 --VLEGEPENVLSDVSLQTL 231
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
3-230 |
9.06e-25 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 98.62 E-value: 9.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTF--YPNTNRS---------------HDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIY 65
Cdd:COG1134 5 IEVENVSKSYrlYHEPSRSlkelllrrrrtrreeFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 66 M-GEAA--VEHTAeyerakyisrvyqnplqGTAPRMTVAQNLSLalrRGLKRGLKKGYTAE---ELEQFkAlltplqlGL 139
Cdd:COG1134 85 VnGRVSalLELGA-----------------GFHPELTGRENIYL---NGRLLGLSRKEIDEkfdEIVEF-A-------EL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 140 EERLDAEIGLLSGGQ--RQAVSLLMATlrTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKElTALMITHNLSDALRYG 217
Cdd:COG1134 137 GDFIDQPVKTYSSGMraRLAFAVATAV--DPDILLVDEVLAVGDAAFQKKCLARIRELRESGR-TVIFVSHSMGAVRRLC 213
|
250
....*....|...
gi 260158848 218 NRLMMMHRGKIIQ 230
Cdd:COG1134 214 DRAIWLEKGRLVM 226
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
19-215 |
9.85e-25 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 97.30 E-value: 9.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 19 SHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHiymgeaaVEHTAEyERAKYIsrvyqnPLQGTAPR- 97
Cdd:NF040873 4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGT-------VRRAGG-ARVAYV------PQRSEVPDs 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 98 --MTVAQNLSLAL--RRGLKRGLKKGYTA---EELEQfkalltplqLGLEERLDAEIGLLSGGQRQAVSLLMATLRTPEL 170
Cdd:NF040873 70 lpLTVRDLVAMGRwaRRGLWRRLTRDDRAavdDALER---------VGLADLAGRQLGELSGGQRQRALLAQGLAQEADL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 260158848 171 LLLDEHTAALDPKTQRKIMQLTKEIIEEKeLTALMITHNLSDALR 215
Cdd:NF040873 141 LLLDEPTTGLDAESRERIIALLAEEHARG-ATVVVVTHDLELVRR 184
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-230 |
1.02e-24 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 98.55 E-value: 1.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 1 MDIRIENVHKtFYPntnrSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAI-------SGSFPLdKGHIYMGEAAVEH 73
Cdd:COG4161 1 MSIQLKNINC-FYG----SHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLnlletpdSGQLNI-AGHQFDFSQKPSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 74 TAEYERAKYISRVYQNplQGTAPRMTVAQNLSLALRRGLkrGLKKgytAEELEQFKALLTplQLGLEERLDAEIGLLSGG 153
Cdd:COG4161 75 KAIRLLRQKVGMVFQQ--YNLWPHLTVMENLIEAPCKVL--GLSK---EQAREKAMKLLA--RLRLTDKADRFPLHLSGG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 260158848 154 QRQAVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEiIEEKELTALMITHNLSDALRYGNRLMMMHRGKIIQ 230
Cdd:COG4161 146 QQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRE-LSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIE 221
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
25-247 |
1.29e-24 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 98.65 E-value: 1.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 25 DINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKyisrvyqnplqgtapRMTV-AQN 103
Cdd:COG4559 19 DVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELAR---------------RRAVlPQH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 104 LSLALrrglkrglkkGYTAEEL-------------EQFKALLTPLQL----GLEERLDAEiglLSGGQRQAVSL--LMAT 164
Cdd:COG4559 84 SSLAF----------PFTVEEVvalgraphgssaaQDRQIVREALALvglaHLAGRSYQT---LSGGEQQRVQLarVLAQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 165 LRTPE-----LLLLDEHTAALDPKTQRKIMQLTKEIIEEKeLTALMITHNLSDALRYGNRLMMMHRGKIiqVFEKEEKEA 239
Cdd:COG4559 151 LWEPVdggprWLFLDEPTSALDLAHQHAVLRLARQLARRG-GGVVAVLHDLNLAAQYADRILLLHQGRL--VAQGTPEEV 227
|
....*...
gi 260158848 240 LTEEKLYQ 247
Cdd:COG4559 228 LTDELLER 235
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
3-228 |
1.29e-24 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 97.48 E-value: 1.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTfYPNTNRshdALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKY 82
Cdd:cd03292 1 IEFINVTKT-YPNGTA---ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 83 ---ISRVYQNPLqgTAPRMTVAQNLSLALRRGLKRGlkkgytAEELEQFKALLTplQLGLEERLDAEIGLLSGGQRQAVS 159
Cdd:cd03292 77 rrkIGVVFQDFR--LLPDRNVYENVAFALEVTGVPP------REIRKRVPAALE--LVGLSHKHRALPAELSGGEQQRVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 260158848 160 LLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEiIEEKELTALMITHNLSDALRYGNRLMMMHRGKI 228
Cdd:cd03292 147 IARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKK-INKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
3-231 |
1.58e-24 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 100.30 E-value: 1.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTfYPNtnrSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAky 82
Cdd:PRK11650 4 LKLQAVRKS-YDG---KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRD-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 83 ISRVYQNplqgTA--PRMTVAQNLSLalrrGLK-RGLKKGYTAEELEQFKALltplqLGLEERLDAEIGLLSGGQRQAVS 159
Cdd:PRK11650 78 IAMVFQN----YAlyPHMSVRENMAY----GLKiRGMPKAEIEERVAEAARI-----LELEPLLDRKPRELSGGQRQRVA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 260158848 160 LLMATLRTPELLLLDEHTAALDPKTqRKIMQLtkEIieeKEL------TALMITHNLSDALRYGNRLMMMHRGKIIQV 231
Cdd:PRK11650 145 MGRAIVREPAVFLFDEPLSNLDAKL-RVQMRL--EI---QRLhrrlktTSLYVTHDQVEAMTLADRVVVMNGGVAEQI 216
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
22-242 |
1.82e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 98.67 E-value: 1.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 22 ALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKYISRVYQNP---LQGTAPRM 98
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQNPdnqFVGSIVKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 99 TVA---QNLSLAlrrglkrglkkgyTAEELEQFKALLTplQLGLEERLDAEIGLLSGGQRQAVSLLMATLRTPELLLLDE 175
Cdd:PRK13648 104 DVAfglENHAVP-------------YDEMHRRVSEALK--QVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 260158848 176 HTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRyGNRLMMMHRGKIIQ------VFEKEekEALTE 242
Cdd:PRK13648 169 ATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKegtpteIFDHA--EELTR 238
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
5-254 |
3.10e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 98.33 E-value: 3.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 5 IENVHKTF-YPNTNRShdALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSF-PLDKGHIYMGEAAVEHTAE--YERA 80
Cdd:PRK13640 6 VEFKHVSFtYPDSKKP--ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlPDDNPNSKITVDGITLTAKtvWDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 81 KYISRVYQNP---LQGTaprmTVAQNLSLALR-RGLKRGLKKGYTAEELEQfkalltplqLGLEERLDAEIGLLSGGQRQ 156
Cdd:PRK13640 84 EKVGIVFQNPdnqFVGA----TVGDDVAFGLEnRAVPRPEMIKIVRDVLAD---------VGMLDYIDSEPANLSGGQKQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 157 AVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDAlRYGNRLMMMHRGKII------Q 230
Cdd:PRK13640 151 RVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLaqgspvE 229
|
250 260
....*....|....*....|....*..
gi 260158848 231 VFEKEE--KEA-LTEEKLYQLMAELDE 254
Cdd:PRK13640 230 IFSKVEmlKEIgLDIPFVYKLKNKLKE 256
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
3-230 |
3.30e-24 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 96.92 E-value: 3.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVhkTF-YPNTNRShdALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVehtAEYERA- 80
Cdd:cd03251 1 VEFKNV--TFrYPGDGPP--VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDV---RDYTLAs 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 81 --KYISRVYQNPLQGTAprmTVAQNLSLAlrrglkrglKKGYTAEELEQF--KALLTPLQLGLEERLDAEIG----LLSG 152
Cdd:cd03251 74 lrRQIGLVSQDVFLFND---TVAENIAYG---------RPGATREEVEEAarAANAHEFIMELPEGYDTVIGergvKLSG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 260158848 153 GQRQAVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKelTALMITHNLSdALRYGNRLMMMHRGKIIQ 230
Cdd:cd03251 142 GQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNR--TTFVIAHRLS-TIENADRIVVLEDGKIVE 216
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
3-229 |
4.92e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 97.88 E-value: 4.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFYPNTNRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKY 82
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 83 ISR----VYQNPlQGTAPRMTVAQNLSLALRR-GLKRGLKKGYTAEELEqfkalLTPLQLGLEERLDAEiglLSGGQRQA 157
Cdd:PRK13643 82 VRKkvgvVFQFP-ESQLFEETVLKDVAFGPQNfGIPKEKAEKIAAEKLE-----MVGLADEFWEKSPFE---LSGGQMRR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 260158848 158 VSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTkEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKII 229
Cdd:PRK13643 153 VAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLF-ESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHII 223
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
3-229 |
5.15e-24 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 98.72 E-value: 5.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTfYPNTNRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGsfpLDK---GHIYMGeaAVEHTAEYER 79
Cdd:PRK11153 2 IELKNISKV-FPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINL---LERptsGRVLVD--GQDLTALSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 80 A-----KYISRVYQ--NPLqgtAPRmTVAQNLSLALR-RGLKRGLKKGYTAEELEQfkalltplqLGLEERLDAEIGLLS 151
Cdd:PRK11153 76 ElrkarRQIGMIFQhfNLL---SSR-TVFDNVALPLElAGTPKAEIKARVTELLEL---------VGLSDKADRYPAQLS 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 260158848 152 GGQRQAVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKII 229
Cdd:PRK11153 143 GGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLV 220
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
26-230 |
6.10e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 100.30 E-value: 6.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 26 INLTIHKGDFITIVGGNGAGKSTFLNAISGSFPldkghiYMGEAAVEHT--AEYERA---KYISRVYQNPLqgtAPRMTV 100
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP------YQGSLKINGIelRELDPEswrKHLSWVGQNPQ---LPHGTL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 101 AQNLSLAlrrglkrglKKGYTAEELEQF--KALLTPLQLGLEERLDAEIG----LLSGGQRQAVSLLMATLRTPELLLLD 174
Cdd:PRK11174 440 RDNVLLG---------NPDASDEQLQQAleNAWVSEFLPLLPQGLDTPIGdqaaGLSVGQAQRLALARALLQPCQLLLLD 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 260158848 175 EHTAALDPKTQRKIMQLTKEIIEEKelTALMITHNLSDALRYgNRLMMMHRGKIIQ 230
Cdd:PRK11174 511 EPTASLDAHSEQLVMQALNAASRRQ--TTLMVTHQLEDLAQW-DQIWVMQDGQIVQ 563
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
25-245 |
6.24e-24 |
|
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: 96.69 E-value: 6.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 25 DINLTIHKGDFITIVGGNGAGKSTFLNAISG-SFPLDKGHIY-MGEaavehtaeyERAK-----------YISRVYQNPL 91
Cdd:COG1119 21 DISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVRlFGE---------RRGGedvwelrkrigLVSPALQLRF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 92 QgtaPRMTVAQnlslALRRGL--KRGLKKGYTAEELEQFKALLTplQLGLEERLDAEIGLLSGGQRQAVSLLMATLRTPE 169
Cdd:COG1119 92 P---RDETVLD----VVLSGFfdSIGLYREPTDEQRERARELLE--LLGLAHLADRPFGTLSQGEQRRVLIARALVKDPE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 260158848 170 LLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKIIQVFEKEekEALTEEKL 245
Cdd:COG1119 163 LLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKE--EVLTSENL 236
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
3-228 |
1.09e-23 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 96.02 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFypntnRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAI-------SGSFPLDKGHIYM-----GEAA 70
Cdd:COG4598 9 LEVRDLHKSF-----GDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCInlletpdSGEIRVGGEEIRLkpdrdGELV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 71 VEHTAEYE--RAKyISRVYQN-PLQgtaPRMTVAQNLSLALRRGLKRGlkkgyTAEELEQFKALLTplQLGLEERLDAEI 147
Cdd:COG4598 84 PADRRQLQriRTR-LGMVFQSfNLW---SHMTVLENVIEAPVHVLGRP-----KAEAIERAEALLA--KVGLADKRDAYP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 148 GLLSGGQRQAVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKElTALMITHNLSDALRYGNRLMMMHRGK 227
Cdd:COG4598 153 AHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGR-TMLVVTHEMGFARDVSSHVVFLHQGR 231
|
.
gi 260158848 228 I 228
Cdd:COG4598 232 I 232
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
3-229 |
1.13e-23 |
|
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: 95.04 E-value: 1.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFYPNTnrshdALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYM-GE---AAVEHTAEY- 77
Cdd:cd03269 1 LEVENVTKRFGRVT-----ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFdGKpldIAARNRIGYl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 78 --ERAKYisrvyqnplqgtaPRMTVAQNLS-LALRRGLKRGLKKGYTAEELEQFkalltplqlGLEERLDAEIGLLSGGQ 154
Cdd:cd03269 76 peERGLY-------------PKMKVIDQLVyLAQLKGLKKEEARRRIDEWLERL---------ELSEYANKRVEELSKGN 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 260158848 155 RQAVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEiIEEKELTALMITHNLSDALRYGNRLMMMHRGKII 229
Cdd:cd03269 134 QQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRE-LARAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-230 |
1.13e-23 |
|
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: 95.25 E-value: 1.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 2 DIRIENVHKTFYPNTNrshDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAK 81
Cdd:cd03244 2 DIEFKNVSLRYRPNLP---PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 82 YISRVYQNPL--QGTaprmtVAQNLslalrrglkrGLKKGYTAEELE------QFKALLTPLQLGLEERLDAEIGLLSGG 153
Cdd:cd03244 79 RISIIPQDPVlfSGT-----IRSNL----------DPFGEYSDEELWqalervGLKEFVESLPGGLDTVVEEGGENLSVG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 260158848 154 QRQAVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEiiEEKELTALMITHNLSDALRYgNRLMMMHRGKIIQ 230
Cdd:cd03244 144 QRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIRE--AFKDCTVLTIAHRLDTIIDS-DRILVLDKGRVVE 217
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
24-229 |
1.18e-23 |
|
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: 97.86 E-value: 1.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 24 IDINLTIHKGDF------------IT-IVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAE------YERAkyIS 84
Cdd:COG4148 3 LEVDFRLRRGGFtldvdftlpgrgVTaLFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARgiflppHRRR--IG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 85 RVYQNP-LqgtAPRMTVAQNLSLALRRGlkrglKKGYTAEELEQFKALLtplqlGLEERLDAEIGLLSGGQRQAVSLLMA 163
Cdd:COG4148 81 YVFQEArL---FPHLSVRGNLLYGRKRA-----PRAERRISFDEVVELL-----GIGHLLDRRPATLSGGERQRVAIGRA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 260158848 164 TLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKII 229
Cdd:COG4148 148 LLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVV 213
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-229 |
1.24e-23 |
|
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: 95.13 E-value: 1.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFYPNTNRSHdALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYM-GEAAVEHTAEYERAk 81
Cdd:cd03266 2 ITADALTKRFRDVKKTVQ-AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVdGFDVVKEPAEARRR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 82 yISRVYQNplQGTAPRMTVAQNLSLALR-RGLKRglkkgytaeelEQFKALLTPL--QLGLEERLDAEIGLLSGGQRQAV 158
Cdd:cd03266 80 -LGFVSDS--TGLYDRLTARENLEYFAGlYGLKG-----------DELTARLEELadRLGMEELLDRRVGGFSTGMRQKV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 260158848 159 SLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKElTALMITHNLSDALRYGNRLMMMHRGKII 229
Cdd:cd03266 146 AIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGK-CILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
3-229 |
1.46e-23 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 95.54 E-value: 1.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFypntnRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKY 82
Cdd:COG4604 2 IEIKNVSKRY-----GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 83 ISRVYQNPlqGTAPRMTVAQ------------NLSLALRRglkrglkkgYTAEELEQFKalLTPLQlglEERLDAeiglL 150
Cdd:COG4604 77 LAILRQEN--HINSRLTVRElvafgrfpyskgRLTAEDRE---------IIDEAIAYLD--LEDLA---DRYLDE----L 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 260158848 151 SGGQRQAVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKII 229
Cdd:COG4604 137 SGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVV 215
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-229 |
1.98e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 98.74 E-value: 1.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 2 DIRIENVHKTfYPNtnRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAK 81
Cdd:PRK11160 338 SLTLNNVSFT-YPD--QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 82 YISRVYQNP--LQGTaprmtVAQNLSLALRrglkrglkkgyTAEElEQFKALLTplQLGLE------ERLDAEIG----L 149
Cdd:PRK11160 415 AISVVSQRVhlFSAT-----LRDNLLLAAP-----------NASD-EALIEVLQ--QVGLEklleddKGLNAWLGeggrQ 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 150 LSGGQRQAVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKelTALMITHNLSdALRYGNRLMMMHRGKII 229
Cdd:PRK11160 476 LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNK--TVLMITHRLT-GLEQFDRICVMDNGQII 552
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
3-230 |
2.17e-23 |
|
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: 94.81 E-value: 2.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFYPNTNRSHdALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGsfpLDK---GHIY--------MGE--- 68
Cdd:COG4181 9 IELRGLTKTVGTGAGELT-ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAG---LDRptsGTVRlagqdlfaLDEdar 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 69 AAVehtaeyeRAKYISRVYQN-PLQGTaprMTVAQNLSLAL-RRGLKRGLKKGytAEELEqfkalltplQLGLEERLDAE 146
Cdd:COG4181 85 ARL-------RARHVGFVFQSfQLLPT---LTALENVMLPLeLAGRRDARARA--RALLE---------RVGLGHRLDHY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 147 IGLLSGGQRQAVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGnRLMMMHRG 226
Cdd:COG4181 144 PAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCD-RVLRLRAG 222
|
....
gi 260158848 227 KIIQ 230
Cdd:COG4181 223 RLVE 226
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
3-227 |
3.04e-23 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 93.69 E-value: 3.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFYPNTNRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAavehtaeyeraky 82
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 83 ISRVYQNP-LQgtapRMTVAQNLSLALRrglkrglkkgYTAEELEQ-FKA--LLTPLQLgLEERLDAEIG----LLSGGQ 154
Cdd:cd03250 68 IAYVSQEPwIQ----NGTIRENILFGKP----------FDEERYEKvIKAcaLEPDLEI-LPDGDLTEIGekgiNLSGGQ 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 260158848 155 RQAVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQ--LTKEIIEEKelTALMITHNLSdALRYGNRLMMMHRGK 227
Cdd:cd03250 133 KQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLNNK--TRILVTHQLQ-LLPHADQIVVLDNGR 204
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1-258 |
3.26e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 95.67 E-value: 3.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 1 MDIRIENVHKTFYPNTNRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIymgEAAVEH-TAEY-- 77
Cdd:PRK13641 1 MSIKFENVDYIYSPGTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTI---TIAGYHiTPETgn 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 78 ----ERAKYISRVYQNPlqgtaprmtVAQNLSLALRRGLKRGLKK-GYTAEELEQfKALLTPLQLGLEERLDAEIGL-LS 151
Cdd:PRK13641 78 knlkKLRKKVSLVFQFP---------EAQLFENTVLKDVEFGPKNfGFSEDEAKE-KALKWLKKVGLSEDLISKSPFeLS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 152 GGQRQAVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKElTALMITHNLSDALRYGNRLMMMHRGKII-- 229
Cdd:PRK13641 148 GGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGH-TVILVTHNMDDVAEYADDVLVLEHGKLIkh 226
|
250 260 270
....*....|....*....|....*....|....*.
gi 260158848 230 ----QVFEKEE---KEALTEEKLYQLMAELDEADFN 258
Cdd:PRK13641 227 aspkEIFSDKEwlkKHYLDEPATSRFASKLEKGGFK 262
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-228 |
4.02e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 95.18 E-value: 4.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 1 MDIRIENVHKTFYPNTNRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYM-GEAAVEHTAEYER 79
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIdGDLLTEENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 80 AKyISRVYQNP---LQGTaprmTVAQNLSLALR-RGLKRGLKKGYTAEELEQfkalltplqLGLEERLDAEIGLLSGGQR 155
Cdd:PRK13650 81 HK-IGMVFQNPdnqFVGA----TVEDDVAFGLEnKGIPHEEMKERVNEALEL---------VGMQDFKEREPARLSGGQK 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 260158848 156 QAVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLsDALRYGNRLMMMHRGKI 228
Cdd:PRK13650 147 QRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDL-DEVALSDRVLVMKNGQV 218
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-230 |
4.88e-23 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 97.86 E-value: 4.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 2 DIRIENVHKTfYPNTNRshDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAK 81
Cdd:TIGR02203 330 DVEFRNVTFR-YPGRDR--PALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 82 YISRVYQNPlqgTAPRMTVAQNLSLALRRGLKRglkkgytaEELEQF--KALLTPLQLGLEERLDAEIG----LLSGGQR 155
Cdd:TIGR02203 407 QVALVSQDV---VLFNDTIANNIAYGRTEQADR--------AEIERAlaAAYAQDFVDKLPLGLDTPIGengvLLSGGQR 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 260158848 156 QAVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKelTALMITHNLSdALRYGNRLMMMHRGKIIQ 230
Cdd:TIGR02203 476 QRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGR--TTLVIAHRLS-TIEKADRIVVMDDGRIVE 547
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
25-248 |
6.37e-23 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 94.28 E-value: 6.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 25 DINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKYISRVYQNplqGTAPRMTVAQNL 104
Cdd:PRK10253 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQN---ATTPGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 105 slaLRRGlKRGLKKGYTAEELEQFKALLTPLQ-LGLEERLDAEIGLLSGGQRQAVSLLMATLRTPELLLLDEHTAALDPK 183
Cdd:PRK10253 102 ---VARG-RYPHQPLFTRWRKEDEEAVTKAMQaTGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIS 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 260158848 184 TQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKIiqVFEKEEKEALTE---EKLYQL 248
Cdd:PRK10253 178 HQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKI--VAQGAPKEIVTAeliERIYGL 243
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
3-229 |
1.02e-22 |
|
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: 93.17 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTF----------------YPNTNRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFpldkgHIYM 66
Cdd:cd03267 1 IEVSNLSKSYrvyskepgligslkslFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLL-----QPTS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 67 GEAAVEHTAEYER----AKYISRVYqnplqgtAPRMTVAQNL----SLALRRGLKRgLKKGYTAEELEQFKALLTplqlg 138
Cdd:cd03267 76 GEVRVAGLVPWKRrkkfLRRIGVVF-------GQKTQLWWDLpvidSFYLLAAIYD-LPPARFKKRLDELSELLD----- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 139 LEERLDAEIGLLSGGQRQAVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGN 218
Cdd:cd03267 143 LEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALAR 222
|
250
....*....|.
gi 260158848 219 RLMMMHRGKII 229
Cdd:cd03267 223 RVLVIDKGRLL 233
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-216 |
1.34e-22 |
|
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: 96.20 E-value: 1.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTfYPNTNrshDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKY 82
Cdd:TIGR02857 322 LEFSGVSVA-YPGRR---PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQ 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 83 ISRVYQNP--LQGTaprmtVAQNLSLAlrrglkrglKKGYTAEELEQF--KALLTPLQLGLEERLDAEIG----LLSGGQ 154
Cdd:TIGR02857 398 IAWVPQHPflFAGT-----IAENIRLA---------RPDASDAEIREAleRAGLDEFVAALPQGLDTPIGeggaGLSGGQ 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 260158848 155 RQAVSLLMATLRTPELLLLDEHTAALDPKTQrkimQLTKEIIEE--KELTALMITHNLSDALRY 216
Cdd:TIGR02857 464 AQRLALARAFLRDAPLLLLDEPTAHLDAETE----AEVLEALRAlaQGRTVLLVTHRLALAALA 523
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-256 |
1.79e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 93.37 E-value: 1.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFYPNTNrshdALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAE--YERA 80
Cdd:PRK13636 6 LKVEELNYNYSDGTH----ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKglMKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 81 KYISRVYQNPlQGTAPRMTVAQNLSLALrrgLKRGLKKGYTAEELEQFKAlltplQLGLEERLDAEIGLLSGGQRQAVSL 160
Cdd:PRK13636 82 ESVGMVFQDP-DNQLFSASVYQDVSFGA---VNLKLPEDEVRKRVDNALK-----RTGIEHLKDKPTHCLSFGQKKRVAI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 161 LMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKII------QVFEK 234
Cdd:PRK13636 153 AGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVIlqgnpkEVFAE 232
|
250 260
....*....|....*....|....*
gi 260158848 235 EE---KEALTEEKLYQLMAELDEAD 256
Cdd:PRK13636 233 KEmlrKVNLRLPRIGHLMEILKEKD 257
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-228 |
2.02e-22 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 92.82 E-value: 2.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 5 IENVHKTFYPNTnrshdALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKYI- 83
Cdd:PRK11247 15 LNAVSKRYGERT-----VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTRLMFQd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 84 SRVYqnplqgtaPRMTVAQNLSLalrrglkrGLKKGYTAEELEQFKALltplqlGLEERLDAEIGLLSGGQRQAVSLLMA 163
Cdd:PRK11247 90 ARLL--------PWKKVIDNVGL--------GLKGQWRDAALQALAAV------GLADRANEWPAALSGGQKQRVALARA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 260158848 164 TLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKI 228
Cdd:PRK11247 148 LIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
23-245 |
3.26e-22 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 91.83 E-value: 3.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 23 LIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPlDKGHIYMGEAAVEHTAEYERAKYisRVY--QNplQGTAPRMTV 100
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAELARH--RAYlsQQ--QSPPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 101 AQNLSLALRRGLkrglkkgyTAEELEQFKALLTPlQLGLEERLDAEIGLLSGGQRQAVsLLMATL--------RTPELLL 172
Cdd:COG4138 87 FQYLALHQPAGA--------SSEAVEQLLAQLAE-ALGLEDKLSRPLTQLSGGEWQRV-RLAAVLlqvwptinPEGQLLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 260158848 173 LDEHTAALDPKTQRKIMQLTKEIIEEKeLTALMITHNLSDALRYGNRLMMMHRGKIiqVFEKEEKEALTEEKL 245
Cdd:COG4138 157 LDEPMNSLDVAQQAALDRLLRELCQQG-ITVVMSSHDLNHTLRHADRVWLLKQGKL--VASGETAEVMTPENL 226
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
3-236 |
4.02e-22 |
|
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: 90.89 E-value: 4.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFypNTNRshdALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGH-IYMGEAAVEHTAEYERAk 81
Cdd:cd03265 1 IEVENLVKKY--GDFE---AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRaTVAGHDVVREPREVRRR- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 82 yISRVYQNPlqGTAPRMTVAQNLSLALR-RGLKRGLKKGYTAEELEQFkalltplqlGLEERLDAEIGLLSGGQRQAVSL 160
Cdd:cd03265 75 -IGIVFQDL--SVDDELTGWENLYIHARlYGVPGAERRERIDELLDFV---------GLLEAADRLVKTYSGGMRRRLEI 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 260158848 161 LMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKIIQVFEKEE 236
Cdd:cd03265 143 ARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-261 |
5.83e-22 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 91.61 E-value: 5.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFYpntnrSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDK---GHIYMGEAAVEHTAEYER 79
Cdd:PRK09984 5 IRVEKLAKTFN-----QHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagSHIELLGRTVQREGRLAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 80 AKYISRVYQNPLQ---GTAPRMTVAQNLSL-AL-RRGLKRGLKKGYTAEELEQFKALLTplQLGLEERLDAEIGLLSGGQ 154
Cdd:PRK09984 80 DIRKSRANTGYIFqqfNLVNRLSVLENVLIgALgSTPFWRTCFSWFTREQKQRALQALT--RVGMVHFAHQRVSTLSGGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 155 RQAVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGkiiQVFEK 234
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQG---HVFYD 234
|
250 260
....*....|....*....|....*..
gi 260158848 235 EEKEALTEEKLYQLMAELDEADFNQES 261
Cdd:PRK09984 235 GSSQQFDNERFDHLYRSINRVEENAKA 261
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1-231 |
7.85e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 91.76 E-value: 7.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 1 MDIRIENVHKTFYPNTNRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAeyeRA 80
Cdd:PRK13646 1 MTIRFDNVSYTYQKGTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKT---KD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 81 KYISRVYQNplQGTAPRMTVAQNLSLALRRGLKRGLKK-GYTAEELEQfKALLTPLQLGLEERLDAEIGL-LSGGQRQAV 158
Cdd:PRK13646 78 KYIRPVRKR--IGMVFQFPESQLFEDTVEREIIFGPKNfKMNLDEVKN-YAHRLLMDLGFSRDVMSQSPFqMSGGQMRKI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 260158848 159 SLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKIIQV 231
Cdd:PRK13646 155 AIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQ 227
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
5-261 |
8.93e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 92.48 E-value: 8.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 5 IENVHKTFYPNTnrshdaLID-INLTIHKGDFITIVGGNGAGKSTFLNAISGsfpLDK---GHIYMGEAAVEHTAEYERA 80
Cdd:PRK11432 9 LKNITKRFGSNT------VIDnLNLTIKQGTMVTLLGPSGCGKTTVLRLVAG---LEKpteGQIFIDGEDVTHRSIQQRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 81 kyISRVYQNplQGTAPRMTVAQNLSLALR-RGLKRGLKKGYTAEELEqfkalLTPLQlGLEERLDAEIgllSGGQRQAVS 159
Cdd:PRK11432 80 --ICMVFQS--YALFPHMSLGENVGYGLKmLGVPKEERKQRVKEALE-----LVDLA-GFEDRYVDQI---SGGQQQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 160 LLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKIIQVFEKEEkea 239
Cdd:PRK11432 147 LARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQE--- 223
|
250 260
....*....|....*....|..
gi 260158848 240 lteekLYQLMAELDEADFNQES 261
Cdd:PRK11432 224 -----LYRQPASRFMASFMGDA 240
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
23-237 |
1.50e-21 |
|
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: 90.63 E-value: 1.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 23 LIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHI-YMGEAAVEHTAEYERA--KYISRVYQNPLQGTAPRMT 99
Cdd:TIGR02769 27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVsFRGQDLYQLDRKQRRAfrRDVQLVFQDSPSAVNPRMT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 100 VAQNLSLALRRGLKrgLKKgytAEELEQFKALLTPLQLGLE--ERLDAEiglLSGGQRQAVSLLMATLRTPELLLLDEHT 177
Cdd:TIGR02769 107 VRQIIGEPLRHLTS--LDE---SEQKARIAELLDMVGLRSEdaDKLPRQ---LSGGQLQRINIARALAVKPKLIVLDEAV 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 178 AALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKIIQVFEKEEK 237
Cdd:TIGR02769 179 SNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQL 238
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
26-246 |
1.94e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 89.97 E-value: 1.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 26 INLTIHKGDFITIVGGNGAGKSTFL---NAISGSFPLDK--GHIYMGEAAVEHTAEYERAKYISRVYQ--NPLqgtaPRM 98
Cdd:PRK14247 22 VNLEIPDNTITALMGPSGSGKSTLLrvfNRLIELYPEARvsGEVYLDGQDIFKMDVIELRRRVQMVFQipNPI----PNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 99 TVAQNLSLALRrgLKRGLKKgyTAEELEQFKALLTPLQLGLE--ERLDAEIGLLSGGQRQAVSLLMATLRTPELLLLDEH 176
Cdd:PRK14247 98 SIFENVALGLK--LNRLVKS--KKELQERVRWALEKAQLWDEvkDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEP 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 260158848 177 TAALDPKTQRKIMQLTKEIieEKELTALMITHNLSDALRYGNRLMMMHRGKIIQVFEKEE-----KEALTEE----KLY 246
Cdd:PRK14247 174 TANLDPENTAKIESLFLEL--KKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREvftnpRHELTEKyvtgRLY 250
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
3-231 |
2.03e-21 |
|
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: 89.52 E-value: 2.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTfYPnTNRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKY 82
Cdd:cd03249 1 IEFKNVSFR-YP-SRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 83 ISRVYQNPLQGTaprMTVAQNLSLAlrrglkrglKKGYTAEELEQF--KALLTPLQLGLEERLDAEIG----LLSGGQRQ 156
Cdd:cd03249 79 IGLVSQEPVLFD---GTIAENIRYG---------KPDATDEEVEEAakKANIHDFIMSLPDGYDTLVGergsQLSGGQKQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 260158848 157 AVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKelTALMITHNLSdALRYGNRLMMMHRGKIIQV 231
Cdd:cd03249 147 RIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGR--TTIVIAHRLS-TIRNADLIAVLQNGQVVEQ 218
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-229 |
2.84e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 90.17 E-value: 2.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFypntnRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAI-------SGS-----FPLDKGHI----YM 66
Cdd:COG4152 2 LELKGLTKRF-----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIIlgilapdSGEvlwdgEPLDPEDRrrigYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 67 GEaavehtaeyERAKYisrvyqnplqgtaPRMTVAQNLS-LALRRGLKRglkkgytAEELEQFKALLTplQLGLEERLDA 145
Cdd:COG4152 77 PE---------ERGLY-------------PKMKVGEQLVyLARLKGLSK-------AEAKRRADEWLE--RLGLGDRANK 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 146 EIGLLSGGQRQAVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQltkEIIEEKE--LTALMITHNLSDALRYGNRLMMM 223
Cdd:COG4152 126 KVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKD---VIRELAAkgTTVIFSSHQMELVEELCDRIVII 202
|
....*.
gi 260158848 224 HRGKII 229
Cdd:COG4152 203 NKGRKV 208
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
3-223 |
3.14e-21 |
|
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: 89.03 E-value: 3.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFypnT--NRSH---DALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIY---------MGE 68
Cdd:COG4778 5 LEVENLSKTF---TlhLQGGkrlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILvrhdggwvdLAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 69 AAvEHTAEYERAKYISRVYQNpLQgTAPRMT----VAQNLslaLRRGLKRglkkgytAEELEQFKALLTplQLGLEERL- 143
Cdd:COG4778 82 AS-PREILALRRRTIGYVSQF-LR-VIPRVSaldvVAEPL---LERGVDR-------EEARARARELLA--RLNLPERLw 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 144 DAEIGLLSGGQRQAVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLtkeiIEEKEL--TA-LMITHNLSDALRYGNRL 220
Cdd:COG4778 147 DLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVEL----IEEAKArgTAiIGIFHDEEVREAVADRV 222
|
...
gi 260158848 221 MMM 223
Cdd:COG4778 223 VDV 225
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
13-210 |
3.38e-21 |
|
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: 92.42 E-value: 3.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 13 YPNTNRshdALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKYISRVYQNP-L 91
Cdd:TIGR02868 344 YPGAPP---VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAhL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 92 QGTaprmTVAQNLSLAlrrglkrglKKGYTAEELEqfKAL----LTPLQLGLEERLDAEIG----LLSGGQRQAVSLLMA 163
Cdd:TIGR02868 421 FDT----TVRENLRLA---------RPDATDEELW--AALervgLADWLRALPDGLDTVLGeggaRLSGGERQRLALARA 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 260158848 164 TLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKelTALMITHNL 210
Cdd:TIGR02868 486 LLADAPILLLDEPTEHLDAETADELLEDLLAALSGR--TVVLITHHL 530
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
3-229 |
3.41e-21 |
|
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: 87.37 E-value: 3.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTfYPNTNRShdALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVeHTAEYERAKY 82
Cdd:cd03247 1 LSINNVSFS-YPEQEQQ--VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPV-SDLEKALSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 83 ISRVYQNP-LQGTaprmTVAQNLSlalRRglkrglkkgytaeeleqfkalltplqlgleerldaeiglLSGGQRQAVSLL 161
Cdd:cd03247 77 ISVLNQRPyLFDT----TLRNNLG---RR---------------------------------------FSGGERQRLALA 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 260158848 162 MATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKelTALMITHNLSdALRYGNRLMMMHRGKII 229
Cdd:cd03247 111 RILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDK--TLIWITHHLT-GIEHMDKILFLENGKII 175
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
3-252 |
3.50e-21 |
|
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: 89.08 E-value: 3.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFYPNtnrSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYM-GEAAVEHTAEYERAK 81
Cdd:cd03252 1 ITFEHVRFRYKPD---GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVdGHDLALADPAWLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 82 yISRVYQnplQGTAPRMTVAQNLSLAlRRGLKRglKKGYTAEELEQFKALLTPLQLGLEERLDAEIGLLSGGQRQAVSLL 161
Cdd:cd03252 78 -VGVVLQ---ENVLFNRSIRDNIALA-DPGMSM--ERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 162 MATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKelTALMITHNLSdALRYGNRLMMMHRGKIIQvfEKEEKEALT 241
Cdd:cd03252 151 RALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGR--TVIIIAHRLS-TVKNADRIIVMEKGRIVE--QGSHDELLA 225
|
250
....*....|.
gi 260158848 242 EEKLYQLMAEL 252
Cdd:cd03252 226 ENGLYAYLYQL 236
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-211 |
3.91e-21 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 92.00 E-value: 3.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 2 DIRIENVhkTF-YPNTNrsHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYM-GEAAVEHTAEYER 79
Cdd:PRK11176 341 DIEFRNV--TFtYPGKE--VPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLdGHDLRDYTLASLR 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 80 aKYISRVYQN-PLQGTaprmTVAQNLSLALrrglkrglKKGYTAEELEQFKALLTPLQL--GLEERLDAEIG----LLSG 152
Cdd:PRK11176 417 -NQVALVSQNvHLFND----TIANNIAYAR--------TEQYSREQIEEAARMAYAMDFinKMDNGLDTVIGengvLLSG 483
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 260158848 153 GQRQAVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIieEKELTALMITHNLS 211
Cdd:PRK11176 484 GQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLS 540
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
3-228 |
5.94e-21 |
|
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: 86.89 E-value: 5.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVhkTF-YPNTNRShdALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAK 81
Cdd:cd03246 1 LEVENV--SFrYPGAEPP--VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 82 YIsrvyqnplqgtaprmtvaqnlslalrrglkrglkkGYTAEELEQFKALLtplqlgleerldAEIgLLSGGQRQAVSLL 161
Cdd:cd03246 77 HV-----------------------------------GYLPQDDELFSGSI------------AEN-ILSGGQRQRLGLA 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 260158848 162 MATLRTPELLLLDEHTAALDPKTQRKIMQLTKEiIEEKELTALMITHNLSdALRYGNRLMMMHRGKI 228
Cdd:cd03246 109 RALYGNPRILVLDEPNSHLDVEGERALNQAIAA-LKAAGATRIVIAHRPE-TLASADRILVLEDGRV 173
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-254 |
7.77e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 89.30 E-value: 7.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 2 DIRIENVHKTFYPNTNRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGE----AAVEHTAEY 77
Cdd:PRK13645 6 DIILDNVSYTYAKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipANLKKIKEV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 78 ER-AKYISRVYQNPlQGTAPRMTVAQNLSLAlrrGLKRGLKKgytAEELEQFKALLTPLQLGlEERLDAEIGLLSGGQRQ 156
Cdd:PRK13645 86 KRlRKEIGLVFQFP-EYQLFQETIEKDIAFG---PVNLGENK---QEAYKKVPELLKLVQLP-EDYVKRSPFELSGGQKR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 157 AVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKII------Q 230
Cdd:PRK13645 158 RVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVIsigspfE 237
|
250 260
....*....|....*....|....*..
gi 260158848 231 VFEKEE---KEALTEEKLYQLMAELDE 254
Cdd:PRK13645 238 IFSNQElltKIEIDPPKLYQLMYKLKN 264
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
25-230 |
1.26e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 90.53 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 25 DINLTIHKGDFITIVGGNGAGKST-------FLNAISGSFPldKGHI-YMGEA---AVEHTAEYERAKYISRVYQNPLQG 93
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSVtalsilrLLPSPPVVYP--SGDIrFHGESllhASEQTLRGVRGNKIAMIFQEPMVS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 94 TAPRMTVAQNLS--LALRRGLKRGLKKGYTAEELEQfkalltplqLGLEE---RLDAEIGLLSGGQRQAVSLLMATLRTP 168
Cdd:PRK15134 105 LNPLHTLEKQLYevLSLHRGMRREAARGEILNCLDR---------VGIRQaakRLTDYPHQLSGGERQRVMIAMALLTRP 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 260158848 169 ELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKIIQ 230
Cdd:PRK15134 176 ELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVE 237
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
2-231 |
1.32e-20 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 89.70 E-value: 1.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 2 DIRIENVHKTFypntnrsHDALI--DINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYER 79
Cdd:PRK11000 3 SVTLRNVTKAY-------GDVVIskDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 80 AkyISRVYQNplQGTAPRMTVAQNLSLalrrGLK-RGLKKGYTAEELEQFKALltpLQLG--LEERLDAeiglLSGGQRQ 156
Cdd:PRK11000 76 G--VGMVFQS--YALYPHLSVAENMSF----GLKlAGAKKEEINQRVNQVAEV---LQLAhlLDRKPKA----LSGGQRQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 260158848 157 AVSLLMATLRTPELLLLDEHTAALDPKTQrkiMQLTKEIIE-EKELTALMI--THNLSDALRYGNRLMMMHRGKIIQV 231
Cdd:PRK11000 141 RVAIGRTLVAEPSVFLLDEPLSNLDAALR---VQMRIEISRlHKRLGRTMIyvTHDQVEAMTLADKIVVLDAGRVAQV 215
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
3-237 |
1.51e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 88.22 E-value: 1.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFYPNT-NRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIY---MGEAAVEHTAEYE 78
Cdd:PRK13633 5 IKCKNVSYKYESNEeSTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYvdgLDTSDEENLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 79 RAKyiSRVYQNP---LQGTAPRMTVA---QNLSLA---LRRGLKRGLKKgytaeeleqfkalltplqLGLEERLDAEIGL 149
Cdd:PRK13633 85 NKA--GMVFQNPdnqIVATIVEEDVAfgpENLGIPpeeIRERVDESLKK------------------VGMYEYRRHAPHL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 150 LSGGQRQAVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRyGNRLMMMHRGKII 229
Cdd:PRK13633 145 LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVV 223
|
250
....*....|....
gi 260158848 230 ------QVFEKEEK 237
Cdd:PRK13633 224 megtpkEIFKEVEM 237
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
22-230 |
1.77e-20 |
|
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: 90.57 E-value: 1.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 22 ALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKYISRVYQNPLQGTAprmTVA 101
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSG---SIL 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 102 QNLSLALRRGLKRglKKGYTAEELEQFKALLTPLQLGLEERLDAEIGLLSGGQRQAVSLLMATLRTPELLLLDEHTAALD 181
Cdd:TIGR01193 566 ENLLLGAKENVSQ--DEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLD 643
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 260158848 182 PKTQRKIMqltKEIIEEKELTALMITHNLSDALRyGNRLMMMHRGKIIQ 230
Cdd:TIGR01193 644 TITEKKIV---NNLLNLQDKTIIFVAHRLSVAKQ-SDKIIVLDHGKIIE 688
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
3-229 |
2.17e-20 |
|
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: 86.83 E-value: 2.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFypntnRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAK- 81
Cdd:cd03218 1 LRAENLSKRY-----GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 82 ---YIsrvyqnPLQGTAPR-MTVAQNLSLALRRglkRGLKKGYTAEELEQfkaLLTPLQLgleERLDAEIGL-LSGGQRQ 156
Cdd:cd03218 76 gigYL------PQEASIFRkLTVEENILAVLEI---RGLSKKEREEKLEE---LLEEFHI---THLRKSKASsLSGGERR 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 260158848 157 AVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKelTALMIT-HNLSDALRYGNRLMMMHRGKII 229
Cdd:cd03218 141 RVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRG--IGVLITdHNVRETLSITDRAYIIYEGKVL 212
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
3-228 |
2.50e-20 |
|
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: 86.37 E-value: 2.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVhkTF-YPnTNRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYM-GEAAVEHTAEYERA 80
Cdd:cd03248 12 VKFQNV--TFaYP-TRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLdGKPISQYEHKYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 81 KyISRVYQNPlqgTAPRMTVAQNLSLALRRGLKRGLKKGYTAEELEQFkalLTPLQLGLEERLDAEIGLLSGGQRQAVSL 160
Cdd:cd03248 89 K-VSLVGQEP---VLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSF---ISELASGYDTEVGEKGSQLSGGQKQRVAI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 260158848 161 LMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKelTALMITHNLSDALRyGNRLMMMHRGKI 228
Cdd:cd03248 162 ARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-233 |
2.93e-20 |
|
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: 89.36 E-value: 2.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFYPNTNRSHdALIDINLTIHKGDFITIVGGNGAGKS-TFLnAISGSFPlDKGHIYMGEAAVE-----HTAE 76
Cdd:COG4172 7 LSVEDLSVAFGQGGGTVE-AVKGVSFDIAAGETLALVGESGSGKSvTAL-SILRLLP-DPAAHPSGSILFDgqdllGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 77 YE----RAKYISRVYQNPLqgTA--PRMTVAQNLSLALRrgLKRGLKKgytAEELEQFKALLTplQLGL---EERLDA-- 145
Cdd:COG4172 84 RElrriRGNRIAMIFQEPM--TSlnPLHTIGKQIAEVLR--LHRGLSG---AAARARALELLE--RVGIpdpERRLDAyp 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 146 -EiglLSGGQRQAVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMH 224
Cdd:COG4172 155 hQ---LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMR 231
|
250
....*....|....*
gi 260158848 225 RGKII------QVFE 233
Cdd:COG4172 232 QGEIVeqgptaELFA 246
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-243 |
3.59e-20 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 86.63 E-value: 3.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHkTFYpntnRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNA------------ISGSFPLDKGHIYMGEAA 70
Cdd:COG1117 12 IEVRNLN-VYY----GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRClnrmndlipgarVEGEILLDGEDIYDPDVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 71 VEHtaeyERAKyISRVYQ--NPLqgtaPrMTVAQNLSLALRRglkRGLKKGYTAEEL-EqfKALltpLQLGL-EE---RL 143
Cdd:COG1117 87 VVE----LRRR-VGMVFQkpNPF----P-KSIYDNVAYGLRL---HGIKSKSELDEIvE--ESL---RKAALwDEvkdRL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 144 DAEIGLLSGGQRQ--------AVSllmatlrtPELLLLDEHTAALDPKTQRKIMQLtkeIIEEKE-LTALMITHNLSDAL 214
Cdd:COG1117 149 KKSALGLSGGQQQrlciaralAVE--------PEVLLMDEPTSALDPISTAKIEEL---ILELKKdYTIVIVTHNMQQAA 217
|
250 260 270
....*....|....*....|....*....|....*
gi 260158848 215 RYGNRLMMMHRGKII------QVFEKEEKEaLTEE 243
Cdd:COG1117 218 RVSDYTAFFYLGELVefgpteQIFTNPKDK-RTED 251
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-248 |
4.04e-20 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 89.39 E-value: 4.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 2 DIRIENVhkTFYPNTNRShdALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAK 81
Cdd:PRK10790 340 RIDIDNV--SFAYRDDNL--VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 82 YISRVYQNPLQGTAprmTVAQNLSLalrrGLKRGLKKGYTAEELEQFKALLTPLQLGLEERLDAEIGLLSGGQRQAVSLL 161
Cdd:PRK10790 416 GVAMVQQDPVVLAD---TFLANVTL----GRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALA 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 162 MATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIieEKELTALMITHNLS---DAlrygNRLMMMHRGkiiQVFEKEEKE 238
Cdd:PRK10790 489 RVLVQTPQILILDEATANIDSGTEQAIQQALAAV--REHTTLVVIAHRLStivEA----DTILVLHRG---QAVEQGTHQ 559
|
250
....*....|....*
gi 260158848 239 ALTEEK-----LYQL 248
Cdd:PRK10790 560 QLLAAQgrywqMYQL 574
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
14-229 |
4.33e-20 |
|
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: 85.79 E-value: 4.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 14 PNTNRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDK---GHIYM-GEAAVEHTAEYErakyISRVYQN 89
Cdd:cd03234 14 KNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFnGQPRKPDQFQKC----VAYVRQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 90 PLqgTAPRMTVAQNLSLALRRGLKRGLKKGYTAEELEQFKALltplQLGLEERLDAEIGLLSGGQRQAVSLLMATLRTPE 169
Cdd:cd03234 90 DI--LLPGLTVRETLTYTAILRLPRKSSDAIRKKRVEDVLLR----DLALTRIGGNLVKGISGGERRRVSIAVQLLWDPK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 170 LLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKII 229
Cdd:cd03234 164 VLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIV 223
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
26-243 |
5.66e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 86.69 E-value: 5.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 26 INLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKYISRVYQNPlQGTAPRMTVAQNLS 105
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNP-DNQFVGATVEDDVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 106 LALRrglKRGLKKGYTAEELEQfkALLTPLQLGLEERldaEIGLLSGGQRQAVSLLMATLRTPELLLLDEHTAALDPKTQ 185
Cdd:PRK13642 105 FGME---NQGIPREEMIKRVDE--ALLAVNMLDFKTR---EPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGR 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 260158848 186 RKIMQLTKEIIEEKELTALMITHNLSDALRyGNRLMMMHRGKIIQVFEKEEKEALTEE 243
Cdd:PRK13642 177 QEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSED 233
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
22-227 |
8.50e-20 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 86.70 E-value: 8.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 22 ALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSfpLDKGHIYMGEAAV---------EHTAEYERAKYISRVYQNPLQ 92
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGL--LAANGRIGGSATFngreilnlpEKELNKLRAEQISMIFQDPMT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 93 GTAPRMTVAQNLSLALRrgLKRGLKKGYTAEE-LEQFKALLTPlqlglEERldAEIGL----LSGGQRQAVSLLMATLRT 167
Cdd:PRK09473 109 SLNPYMRVGEQLMEVLM--LHKGMSKAEAFEEsVRMLDAVKMP-----EAR--KRMKMypheFSGGMRQRVMIAMALLCR 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 168 PELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGK 227
Cdd:PRK09473 180 PKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 239
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
13-229 |
1.03e-19 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 88.24 E-value: 1.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 13 YPNTNRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNaISGSfpLDKGHIYMGEAAVEHTAEYE-------RAKYISR 85
Cdd:PRK10535 14 YPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGC--LDKPTSGTYRVAGQDVATLDadalaqlRREHFGF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 86 VYQNplQGTAPRMTVAQNLSL-ALRRGLKRglkkgytAEELEQFKALLTplQLGLEERLDAEIGLLSGGQRQAVSLLMAT 164
Cdd:PRK10535 91 IFQR--YHLLSHLTAAQNVEVpAVYAGLER-------KQRLLRAQELLQ--RLGLEDRVEYQPSQLSGGQQQRVSIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 260158848 165 LRTPELLLLDEHTAALDPKTQRKIMQLTKEiIEEKELTALMITHNLSDALRyGNRLMMMHRGKII 229
Cdd:PRK10535 160 MNGGQVILADEPTGALDSHSGEEVMAILHQ-LRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
3-249 |
1.13e-19 |
|
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: 84.97 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHktFYPNTNRshDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYM-GEAAVEHTAEYERAK 81
Cdd:cd03253 1 IEFENVT--FAYDPGR--PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIdGQDIREVTLDSLRRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 82 YisrvyqnplqGTAPRMTVAQNLSLA--LRRGlkrglKKGYTAEELEQF--KALLTPLQLGLEERLDAEIG----LLSGG 153
Cdd:cd03253 77 I----------GVVPQDTVLFNDTIGynIRYG-----RPDATDEEVIEAakAAQIHDKIMRFPDGYDTIVGerglKLSGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 154 QRQAVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKelTALMITHNLS---DAlrygNRLMMMHRGKIIQ 230
Cdd:cd03253 142 EKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGR--TTIVIAHRLStivNA----DKIIVLKDGRIVE 215
|
250
....*....|....*....
gi 260158848 231 vfEKEEKEALTEEKLYQLM 249
Cdd:cd03253 216 --RGTHEELLAKGGLYAEM 232
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
25-236 |
1.13e-19 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 87.40 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 25 DINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYE----RAKYISRVYQNplQGTAPRMTV 100
Cdd:PRK10070 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevRRKKIAMVFQS--FALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 101 AQNLSLALRRGlkrglkkGYTAEELEQfKALLTPLQLGLEERLDAEIGLLSGGQRQAVSLLMATLRTPELLLLDEHTAAL 180
Cdd:PRK10070 124 LDNTAFGMELA-------GINAEERRE-KALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSAL 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 260158848 181 DPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKIIQVFEKEE 236
Cdd:PRK10070 196 DPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDE 251
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
16-233 |
1.91e-19 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 87.05 E-value: 1.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 16 TNRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGsfpLDK--GHIYMGEAAVEHTAEYERAKYISR---VYQNP 90
Cdd:COG4172 295 TVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR---LIPseGEIRFDGQDLDGLSRRALRPLRRRmqvVFQDP 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 91 LQGTAPRMTVAQNLS---LALRRGLKRglkkgytAEELEQFKALLTplqlglEERLDAEIGL-----LSGGQRQAVSLLM 162
Cdd:COG4172 372 FGSLSPRMTVGQIIAeglRVHGPGLSA-------AERRARVAEALE------EVGLDPAARHrypheFSGGQRQRIAIAR 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 260158848 163 ATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLS--DALryGNRLMMMHRGKII------QVFE 233
Cdd:COG4172 439 ALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAvvRAL--AHRVMVMKDGKVVeqgpteQVFD 515
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
22-226 |
2.46e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 84.37 E-value: 2.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 22 ALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEyERAKyisrVYQNplQGTAPRMTVA 101
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGA-ERGV----VFQN--EGLLPWRNVQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 102 QNLSLALR-RGLKRglkkgytAEELEQFKALLTplQLGLEERLDAEIGLLSGGQRQAVSLLMATLRTPELLLLDEHTAAL 180
Cdd:PRK11248 89 DNVAFGLQlAGVEK-------MQRLEIAHQMLK--KVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 260158848 181 DPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRG 226
Cdd:PRK11248 160 DAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
22-236 |
3.09e-19 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 85.14 E-value: 3.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 22 ALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHI-YMGEAAVEHTAEYERA--KYISRVYQNPLQGTAPRM 98
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVaWLGKDLLGMKDDEWRAvrSDIQMIFQDPLASLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 99 TVAQNLslalrrglkrglkkgytAEELEQFKALLTPLQLglEERLDA---EIGLL-----------SGGQRQAVSLLMAT 164
Cdd:PRK15079 116 TIGEII-----------------AEPLRTYHPKLSRQEV--KDRVKAmmlKVGLLpnlinryphefSGGQCQRIGIARAL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 260158848 165 LRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKIIQVFEKEE 236
Cdd:PRK15079 177 ILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDE 248
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-236 |
4.41e-19 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 86.01 E-value: 4.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFYPNTNRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIY--MGEAAVEHT----AE 76
Cdd:TIGR03269 280 IKVRNVSKRYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrVGDEWVDMTkpgpDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 77 YERAK-YISRVYQNplQGTAPRMTVAQNLSLALrrglkrGLKkgyTAEELEQFKALLTPLQLGLEERLDAEI-----GLL 150
Cdd:TIGR03269 360 RGRAKrYIGILHQE--YDLYPHRTVLDNLTEAI------GLE---LPDELARMKAVITLKMVGFDEEKAEEIldkypDEL 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 151 SGGQRQAVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKIIQ 230
Cdd:TIGR03269 429 SEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVK 508
|
....*.
gi 260158848 231 VFEKEE 236
Cdd:TIGR03269 509 IGDPEE 514
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1-261 |
1.00e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 83.26 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 1 MDIRIENVHKTFYPNTNRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERA 80
Cdd:PRK13649 1 MGINLQNVSYTYQAGTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 81 KYISR----VYQNPlQGTAPRMTVAQNLSLALRrglKRGLKKgYTAEELEQFKALLTPLQLGLEERLDAEiglLSGGQRQ 156
Cdd:PRK13649 81 KQIRKkvglVFQFP-ESQLFEETVLKDVAFGPQ---NFGVSQ-EEAEALAREKLALVGISESLFEKNPFE---LSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 157 AVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEiIEEKELTALMITHNLSDALRYGNRLMMMHRGKII------Q 230
Cdd:PRK13649 153 RVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKK-LHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVlsgkpkD 231
|
250 260 270
....*....|....*....|....*....|....*
gi 260158848 231 VFEK----EEKEaLTEEKLYQLMAELDEADFNQES 261
Cdd:PRK13649 232 IFQDvdflEEKQ-LGVPKITKFAQRLADRGISFSS 265
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
23-228 |
1.22e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 84.51 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 23 LIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAeyerAKYISRVYQNPLQGTA------- 95
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALS----ARAASRRVASVPQDTSlsfefdv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 96 ---------PRMTVAQNLSLALRRGLKRGLKKGYTAeeleQFkalltplqlgleerLDAEIGLLSGGQRQAVSLLMATLR 166
Cdd:PRK09536 95 rqvvemgrtPHRSRFDTWTETDRAAVERAMERTGVA----QF--------------ADRPVTSLSGGERQRVLLARALAQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 260158848 167 TPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKElTALMITHNLSDALRYGNRLMMMHRGKI 228
Cdd:PRK09536 157 ATPVLLLDEPTASLDINHQVRTLELVRRLVDDGK-TAVAAIHDLDLAARYCDELVLLADGRV 217
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
7-260 |
1.47e-18 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 84.76 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 7 NVHKTFYPNTnrSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHI-YMGEAAVEHTAEYERAKyISR 85
Cdd:PRK10789 317 NIRQFTYPQT--DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIrFHDIPLTKLQLDSWRSR-LAV 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 86 VYQNPLQGTAprmTVAQNLSLAlrrglkrglKKGYTAEELEQFKALLTPLQ--LGLEERLDAEIG----LLSGGQRQAVS 159
Cdd:PRK10789 394 VSQTPFLFSD---TVANNIALG---------RPDATQQEIEHVARLASVHDdiLRLPQGYDTEVGergvMLSGGQKQRIS 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 160 LLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKelTALMITHNLSdALRYGNRLMMMHRGKIIQvfeKEEKEA 239
Cdd:PRK10789 462 IARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGR--TVIISAHRLS-ALTEASEILVMQHGHIAQ---RGNHDQ 535
|
250 260
....*....|....*....|....*....
gi 260158848 240 LTEE-----KLY---QLMAELDEADFNQE 260
Cdd:PRK10789 536 LAQQsgwyrDMYryqQLEAALDDAPEIRE 564
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
23-247 |
1.52e-18 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 81.90 E-value: 1.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 23 LIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPlDKGHIYMGEAAVEHTAEYERAKYisRVYQNPLQGTAPRMTVAQ 102
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAELARH--RAYLSQQQTPPFAMPVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 103 NLSLALRRGLkrglkkgytaeELEQFKALLTPL--QLGLEERLDAEIGLLSGGQRQAVSLLMATLR-----TPE--LLLL 173
Cdd:PRK03695 89 YLTLHQPDKT-----------RTEAVASALNEVaeALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdiNPAgqLLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 260158848 174 DEHTAALDPKTQRKIMQLTKEIIeEKELTALMITHNLSDALRYGNRLMMMHRGKIIQvfEKEEKEALTEEKLYQ 247
Cdd:PRK03695 158 DEPMNSLDVAQQAALDRLLSELC-QQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLA--SGRRDEVLTPENLAQ 228
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
19-230 |
1.61e-18 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 82.43 E-value: 1.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 19 SHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHI-YMGEAAVEHTAEYERA--KYISRVYQNPLQGTA 95
Cdd:PRK10419 24 HQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVsWRGEPLAKLNRAQRKAfrRDIQMVFQDSISAVN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 96 PRMTVAQNLSLALRRGLkrGLKKgytAEELEQFKALLTPLQLGlEERLDAEIGLLSGGQRQAVSLLMATLRTPELLLLDE 175
Cdd:PRK10419 104 PRKTVREIIREPLRHLL--SLDK---AERLARASEMLRAVDLD-DSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 260158848 176 HTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKIIQ 230
Cdd:PRK10419 178 AVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-241 |
1.75e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 82.98 E-value: 1.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFYPNTNRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERA-- 80
Cdd:PRK13631 22 LRVKNLYCVFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELit 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 81 --------------KYISRVYQNPlQGTAPRMTVAQNLS---LALrrglkrGLKKgYTAEELEQFkaLLTPLQLGlEERL 143
Cdd:PRK13631 102 npyskkiknfkelrRRVSMVFQFP-EYQLFKDTIEKDIMfgpVAL------GVKK-SEAKKLAKF--YLNKMGLD-DSYL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 144 DAEIGLLSGGQRQAVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKElTALMITHNLSDALRYGNRLMMM 223
Cdd:PRK13631 171 ERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNK-TVFVITHTMEHVLEVADEVIVM 249
|
250 260
....*....|....*....|....
gi 260158848 224 HRGKII------QVFEKEEKEALT 241
Cdd:PRK13631 250 DKGKILktgtpyEIFTDQHIINST 273
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
20-228 |
3.55e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 81.17 E-value: 3.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 20 HDALIDINLTIHKGDFITIVGGNGAGKSTFLNAIS-------GSFPLDKGHIYM-----GEAAV--EHTAEYERAKyISR 85
Cdd:PRK10619 18 HEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINflekpseGSIVVNGQTINLvrdkdGQLKVadKNQLRLLRTR-LTM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 86 VYQNplQGTAPRMTVAQNLSLALRRGLkrGLKKGYTAEELEQFKAlltplQLGLEERLDAEIGL-LSGGQRQAVSLLMAT 164
Cdd:PRK10619 97 VFQH--FNLWSHMTVLENVMEAPIQVL--GLSKQEARERAVKYLA-----KVGIDERAQGKYPVhLSGGQQQRVSIARAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 260158848 165 LRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKElTALMITHNLSDALRYGNRLMMMHRGKI 228
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
3-240 |
3.82e-18 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 80.95 E-value: 3.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFYPNTnrshdALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKY 82
Cdd:PRK11264 4 IEVKNLVKKFHGQT-----VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 83 ISR--------VYQNplQGTAPRMTVAQNLSlalrrglkRG---LKKGYTAEELEQFKALLTplQLGLEERLDAEIGLLS 151
Cdd:PRK11264 79 LIRqlrqhvgfVFQN--FNLFPHRTVLENII--------EGpviVKGEPKEEATARARELLA--KVGLAGKETSYPRRLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 152 GGQRQAVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKElTALMITHNLSDALRYGNRLMMMHRGKIIqv 231
Cdd:PRK11264 147 GGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIV-- 223
|
....*....
gi 260158848 232 fEKEEKEAL 240
Cdd:PRK11264 224 -EQGPAKAL 231
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
26-229 |
4.39e-18 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 80.80 E-value: 4.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 26 INLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERA-KYISRVYQNPlqgtapR----MTV 100
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIArMGVVRTFQHV------RlfreMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 101 AQNLSLALRRGLKRGLKKGY---------TAEELEQFKALLTplQLGLEERLDAEIGLLSGGQ--RQAVSLLMATlrTPE 169
Cdd:PRK11300 98 IENLLVAQHQQLKTGLFSGLlktpafrraESEALDRAATWLE--RVGLLEHANRQAGNLAYGQqrRLEIARCMVT--QPE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 170 LLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKII 229
Cdd:PRK11300 174 ILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPL 233
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
22-236 |
4.93e-18 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 81.70 E-value: 4.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 22 ALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKYISR---VYQNPLQGTAPRM 98
Cdd:COG4608 33 AVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLRRRmqmVFQDPYASLNPRM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 99 TVAQNLSLALR-RGLKRGlkkgytAEELEQFKALLTplQLGLE----ERLDAEiglLSGGQRQAVSLLMATLRTPELLLL 173
Cdd:COG4608 113 TVGDIIAEPLRiHGLASK------AERRERVAELLE--LVGLRpehaDRYPHE---FSGGQRQRIGIARALALNPKLIVC 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 260158848 174 DEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSdALRY-GNRLMMMHRGKIIQVFEKEE 236
Cdd:COG4608 182 DEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLS-VVRHiSDRVAVMYLGKIVEIAPRDE 244
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-243 |
5.30e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 80.66 E-value: 5.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 1 MDIRIENVHKTFYPNTNrshDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEY--- 77
Cdd:PRK14267 1 MKFAIETVNLRVYYGSN---HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRNIYspd 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 78 ----ERAKYISRVYQNPlqGTAPRMTVAQNLSLALRrgLKRGLKKGYTAEELEQFKALLTPLQLGLEERLDAEIGLLSGG 153
Cdd:PRK14267 78 vdpiEVRREVGMVFQYP--NPFPHLTIYDNVAIGVK--LNGLVKSKKELDERVEWALKKAALWDEVKDRLNDYPSNLSGG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 154 QRQAVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIieEKELTALMITHNLSDALRYGNRLMMMHRGKIIQ--- 230
Cdd:PRK14267 154 QRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEvgp 231
|
250
....*....|....*.
gi 260158848 231 ---VFEKEEKEaLTEE 243
Cdd:PRK14267 232 trkVFENPEHE-LTEK 246
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
21-209 |
5.87e-18 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 79.39 E-value: 5.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 21 DALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAE--YERAKYISRVYQNP-LQGTAPr 97
Cdd:TIGR01166 6 EVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKglLERRQRVGLVFQDPdDQLFAA- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 98 mTVAQNLSLALRrglKRGLKKgytAEELEQFKALLTPLQL-GLEERLdaeIGLLSGGQRQAVSLLMATLRTPELLLLDEH 176
Cdd:TIGR01166 85 -DVDQDVAFGPL---NLGLSE---AEVERRVREALTAVGAsGLRERP---THCLSGGEKKRVAIAGAVAMRPDVLLLDEP 154
|
170 180 190
....*....|....*....|....*....|...
gi 260158848 177 TAALDPKTQRKIMQLTKEIIEEKeLTALMITHN 209
Cdd:TIGR01166 155 TAGLDPAGREQMLAILRRLRAEG-MTVVISTHD 186
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
22-245 |
8.81e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 80.51 E-value: 8.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 22 ALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAE--YERAKYISRVYQNP-LQGTAPrm 98
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKslLEVRKTVGIVFQNPdDQLFAP-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 99 TVAQNLSLAlrrGLKRGLKKgytaEELEQ--FKALLTPLQLGLEERLDAEiglLSGGQRQAVSLLMATLRTPELLLLDEH 176
Cdd:PRK13639 95 TVEEDVAFG---PLNLGLSK----EEVEKrvKEALKAVGMEGFENKPPHH---LSGGQKKRVAIAGILAMKPEIIVLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 260158848 177 TAALDPKTQRKIMQLTKEiIEEKELTALMITHNLSDALRYGNRLMMMHRGKIIQvfEKEEKEALTEEKL 245
Cdd:PRK13639 165 TSGLDPMGASQIMKLLYD-LNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIK--EGTPKEVFSDIET 230
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
25-229 |
1.70e-17 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 80.69 E-value: 1.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 25 DINLTI-HKGdfIT-IVGGNGAGKSTFLNAISGSFPLDKGHIYMG-------EAAVEHTAEYERAKYI---SRVYqnplq 92
Cdd:PRK11144 16 TVNLTLpAQG--ITaIFGRSGAGKTSLINAISGLTRPQKGRIVLNgrvlfdaEKGICLPPEKRRIGYVfqdARLF----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 93 gtaPRMTVAQNLslalRRGLKRGLKkgytaeelEQFKALLTplQLGLEERLDAEIGLLSGGQRQAVSLLMATLRTPELLL 172
Cdd:PRK11144 89 ---PHYKVRGNL----RYGMAKSMV--------AQFDKIVA--LLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 260158848 173 LDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKII 229
Cdd:PRK11144 152 MDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVK 208
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-230 |
2.36e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 81.16 E-value: 2.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 2 DIRIENVhkTF-YPNTNRshdALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYM-GEAAVEHTAEYER 79
Cdd:PRK13657 334 AVEFDDV--SFsYDNSRQ---GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIdGTDIRTVTRASLR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 80 aKYISRVYQNPlqGTAPRmTVAQNLSLAlrrglkrglKKGYTAEELEQF--KALLTPLQLGLEERLDAEIG----LLSGG 153
Cdd:PRK13657 409 -RNIAVVFQDA--GLFNR-SIEDNIRVG---------RPDATDEEMRAAaeRAQAHDFIERKPDGYDTVVGergrQLSGG 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 260158848 154 QRQAVSLLMATLRTPELLLLDEHTAALDPKTQRKImqltKEIIEE--KELTALMITHNLSdALRYGNRLMMMHRGKIIQ 230
Cdd:PRK13657 476 ERQRLAIARALLKDPPILILDEATSALDVETEAKV----KAALDElmKGRTTFIIAHRLS-TVRNADRILVFDNGRVVE 549
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
3-236 |
5.61e-17 |
|
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: 80.08 E-value: 5.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVhkTFYPnTNRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEhtaEYERAKY 82
Cdd:TIGR01842 317 LSVENV--TIVP-PGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLK---QWDRETF 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 83 ISRVYQNPLQGTAPRMTVAQNLSlalRRGLKRGLKKGYTAEELEQFKALLtplqLGLEERLDAEIGL----LSGGQRQAV 158
Cdd:TIGR01842 391 GKHIGYLPQDVELFPGTVAENIA---RFGENADPEKIIEAAKLAGVHELI----LRLPDGYDTVIGPggatLSGGQRQRI 463
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 260158848 159 SLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEiIEEKELTALMITHNLSdALRYGNRLMMMHRGKIIQVFEKEE 236
Cdd:TIGR01842 464 ALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKA-LKARGITVVVITHRPS-LLGCVDKILVLQDGRIARFGERDE 539
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-208 |
6.25e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 79.72 E-value: 6.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFypntnrsHDALI--DINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGeaaveHTAEyera 80
Cdd:COG0488 316 LELEGLSKSY-------GDKTLldDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG-----ETVK---- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 81 kyISRVYQNpLQGTAPRMTVAQNLslalrRGLKRGLKKGYTAEELEQFkaLLTPlqlgleERLDAEIGLLSGGQRQAVSL 160
Cdd:COG0488 380 --IGYFDQH-QEELDPDKTVLDEL-----RDGAPGGTEQEVRGYLGRF--LFSG------DDAFKPVGVLSGGEKARLAL 443
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 260158848 161 LMATLRTPELLLLDEHTAALDPKtqrkimqlTKEIIEEK----ELTALMITH 208
Cdd:COG0488 444 AKLLLSPPNVLLLDEPTNHLDIE--------TLEALEEAlddfPGTVLLVSH 487
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
26-228 |
1.00e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 79.32 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 26 INLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKY-ISRVYQNPLqgTAPRMTVAQNL 104
Cdd:PRK15439 30 IDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLgIYLVPQEPL--LFPNLSVKENI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 105 SLALRRglkrglkkgyTAEELEQFKALLTplQLGLEERLDAEIGLLSGGQRQAVSLLMATLRTPELLLLDEHTAALDP-K 183
Cdd:PRK15439 108 LFGLPK----------RQASMQKMKQLLA--ALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPaE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 260158848 184 TQRKIMQLTKeiIEEKELTALMITHNLSDALRYGNRLMMMHRGKI 228
Cdd:PRK15439 176 TERLFSRIRE--LLAQGVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
3-230 |
1.02e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 77.52 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFYPNT---NRSH-DALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYE 78
Cdd:PRK15112 5 LEVRNLSKTFRYRTgwfRRQTvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 79 RAKYISRVYQNPLQGTAPRMTVAQNLSLALRrglkrgLKKGYTAEELEQfKALLTPLQLGL-EERLDAEIGLLSGGQRQA 157
Cdd:PRK15112 85 RSQRIRMIFQDPSTSLNPRQRISQILDFPLR------LNTDLEPEQREK-QIIETLRQVGLlPDHASYYPHMLAPGQKQR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 260158848 158 VSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKIIQ 230
Cdd:PRK15112 158 LGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVE 230
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
22-240 |
1.26e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 78.08 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 22 ALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYM-GEAAVEHTAEYERA--KYISRVYQNPLQGTAPRM 98
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYqGQDLLKADPEAQKLlrQKIQIVFQNPYGSLNPRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 99 TVAQNLS--LALRRGLKRglkkgytAEELEQFKALLTplQLGLE-ERLDAEIGLLSGGQRQAVSLLMATLRTPELLLLDE 175
Cdd:PRK11308 110 KVGQILEepLLINTSLSA-------AERREKALAMMA--KVGLRpEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADE 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 260158848 176 HTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKIIqvfEKEEKEAL 240
Cdd:PRK11308 181 PVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCV---EKGTKEQI 242
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-247 |
1.44e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 76.59 E-value: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 1 MDIRIENVHKTfYPNTNrshdALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERA 80
Cdd:PRK11231 1 MTLRTENLTVG-YGTKR----ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 81 KYISRVYQNPL--QGTAPRMTVAQN----LSLALRRGlkrglkkgytaeelEQFKALLTPL--QLGLEERLDAEIGLLSG 152
Cdd:PRK11231 76 RRLALLPQHHLtpEGITVRELVAYGrspwLSLWGRLS--------------AEDNARVNQAmeQTRINHLADRRLTDLSG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 153 GQRQAVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKElTALMITHNLSDALRYGNRLMMMHRGKIIQvf 232
Cdd:PRK11231 142 GQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGK-TVVTVLHDLNQASRYCDHLVVLANGHVMA-- 218
|
250
....*....|....*
gi 260158848 233 EKEEKEALTEEKLYQ 247
Cdd:PRK11231 219 QGTPEEVMTPGLLRT 233
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
3-229 |
1.55e-16 |
|
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: 75.72 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFypntnRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHI-YMGEAAVEHTAEYERAK 81
Cdd:cd03268 1 LKTNDLTKTY-----GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEItFDGKSYQKNIEALRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 82 YISRVyqnplQGTAPRMTVAQNLSLALRrgLKRGLKKgytaeelEQFKALLTplqLGLEERLDAEIGLLSGGQRQAVSLL 161
Cdd:cd03268 76 ALIEA-----PGFYPNLTARENLRLLAR--LLGIRKK-------RIDEVLDV---VGLKDSAKKKVKGFSLGMKQRLGIA 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 162 MATLRTPELLLLDEHTAALDPKtqrKIMQLTKEIIEEKE--LTALMITHNLSDALRYGNRLMMMHRGKII 229
Cdd:cd03268 139 LALLGNPDLLILDEPTNGLDPD---GIKELRELILSLRDqgITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
4-230 |
1.62e-16 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 78.61 E-value: 1.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 4 RIENVHKTF-YPNtNRSHDALIDINLTIHKGDFITIVGGNGAGKST-------FLNAISGSFPLDkghiymGEAAVEHTA 75
Cdd:TIGR00958 478 LIEFQDVSFsYPN-RPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTvaallqnLYQPTGGQVLLD------GVPLVQYDH 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 76 EYERAKyISRVYQNPLqgtAPRMTVAQNLSLALRRGLKRGLKKGYTAEELEQFKAlltplqlGLEERLDAEIG----LLS 151
Cdd:TIGR00958 551 HYLHRQ-VALVGQEPV---LFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIM-------EFPNGYDTEVGekgsQLS 619
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 260158848 152 GGQRQAVSLLMATLRTPELLLLDEHTAALDPKTQrkimQLTKEIIEEKELTALMITHNLSDAlRYGNRLMMMHRGKIIQ 230
Cdd:TIGR00958 620 GGQKQRIAIARALVRKPRVLILDEATSALDAECE----QLLQESRSRASRTVLLIAHRLSTV-ERADQILVLKKGSVVE 693
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-229 |
2.66e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 76.66 E-value: 2.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 1 MDIRIENVHKTFYPNTNRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHI-YMGEAAVEHTAEYER 79
Cdd:PRK13651 1 MQIKVKNIVKIFNKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIeWIFKDEKNKKKTKEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 80 AKYISRVYqnpLQGTAPRmtvaqnlSLALRRGLKRGLKKGYTAEELEQFKA------LLTPLQLGLE----ERLDAEI-- 147
Cdd:PRK13651 81 EKVLEKLV---IQKTRFK-------KIKKIKEIRRRVGVVFQFAEYQLFEQtiekdiIFGPVSMGVSkeeaKKRAAKYie 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 148 --GL-----------LSGGQRQAVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKElTALMITHNLSDAL 214
Cdd:PRK13651 151 lvGLdesylqrspfeLSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNVL 229
|
250
....*....|....*
gi 260158848 215 RYGNRLMMMHRGKII 229
Cdd:PRK13651 230 EWTKRTIFFKDGKII 244
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
25-255 |
2.72e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 77.75 E-value: 2.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 25 DINLTIHKGDfitIVG--G-NGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAK----YIS--RVyqnpLQGTA 95
Cdd:COG1129 270 DVSFSVRAGE---ILGiaGlVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRagiaYVPedRK----GEGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 96 PRMTVAQNLSLALRRGLKRG--LKKGYTAEELEQFKALL---TPlqlgleeRLDAEIGLLSGGQRQAVSL--LMATlrTP 168
Cdd:COG1129 343 LDLSIRENITLASLDRLSRGglLDRRRERALAEEYIKRLrikTP-------SPEQPVGNLSGGNQQKVVLakWLAT--DP 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 169 ELLLLDEHTAALDPKTQRKIMQLTKEIIEEKeLTALMITHNLSDALRYGNRLMMMHRGKIIQVFEKEEkeaLTEEKLYQL 248
Cdd:COG1129 414 KVLILDEPTRGIDVGAKAEIYRLIRELAAEG-KAVIVISSELPELLGLSDRILVMREGRIVGELDREE---ATEEAIMAA 489
|
....*..
gi 260158848 249 MAELDEA 255
Cdd:COG1129 490 ATGGAAA 496
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-249 |
5.33e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 76.87 E-value: 5.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 22 ALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVE--HTAEYERAKyISRVYQNpLQgTAPRMT 99
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfaSTTAALAAG-VAIIYQE-LH-LVPEMT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 100 VAQNLSLAL---RRGL-KRGLKKGYTAEELEqfkalltplQLGLEERLDAEIGLLSGGQRQAVSLLMATLRTPELLLLDE 175
Cdd:PRK11288 96 VAENLYLGQlphKGGIvNRRLLNYEAREQLE---------HLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDE 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 260158848 176 HTAALdpkTQRKIMQLTKEIieeKELTA-----LMITHNLSDALRYGNRLMMMHRGKIIQVFEKEEKeaLTEEKLYQLM 249
Cdd:PRK11288 167 PTSSL---SAREIEQLFRVI---RELRAegrviLYVSHRMEEIFALCDAITVFKDGRYVATFDDMAQ--VDRDQLVQAM 237
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
25-230 |
5.39e-16 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 75.35 E-value: 5.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 25 DINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHI-Y-MGEAAVEHTA---EYERaKYISR-----VYQNPLQGt 94
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhYrMRDGQLRDLYalsEAER-RRLLRtewgfVHQHPRDG- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 95 aprmtvaqnlslaLRRGLKRGlkkGYTAEEL------------EQFKALLTPLQLGLEeRLDAEIGLLSGGQRQavSLLM 162
Cdd:PRK11701 102 -------------LRMQVSAG---GNIGERLmavgarhygdirATAGDWLERVEIDAA-RIDDLPTTFSGGMQQ--RLQI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 163 A-TLRT-PELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKIIQ 230
Cdd:PRK11701 163 ArNLVThPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVE 232
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
25-229 |
9.12e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 75.64 E-value: 9.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 25 DINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKyISRVYQnpLQGTAPRMTVAQNL 104
Cdd:PRK13536 59 GLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARAR-IGVVPQ--FDNLDLEFTVRENL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 105 slalrrgLKRGLKKGYTAEELEqfkALLTPLQ--LGLEERLDAEIGLLSGGQRQAVSLLMATLRTPELLLLDEHTAALDP 182
Cdd:PRK13536 136 -------LVFGRYFGMSTREIE---AVIPSLLefARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDP 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 260158848 183 KTQRKIMQLTKEIIeEKELTALMITHNLSDALRYGNRLMMMHRGKII 229
Cdd:PRK13536 206 HARHLIWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVLEAGRKI 251
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
23-220 |
1.02e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 74.05 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 23 LIDINLTIHKGDFITIVGGNGAGKSTFLNAISGsfpLDKGHiyMGEAAV----------EHTAEYeRAKYISRVYQNPLq 92
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAG---LDDGS--SGEVSLvgqplhqmdeEARAKL-RAKHVGFVFQSFM- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 93 gTAPRMTVAQNLSL-ALRRGLKRGLKKgytaeelEQFKALLTplQLGLEERLDAEIGLLSGGQRQAVSLLMATLRTPELL 171
Cdd:PRK10584 99 -LIPTLNALENVELpALLRGESSRQSR-------NGAKALLE--QLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 260158848 172 LLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRL 220
Cdd:PRK10584 169 FADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRL 217
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-235 |
1.81e-15 |
|
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: 73.60 E-value: 1.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 29 TIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKYISRVYQnplqgtaprmtvaqnlslal 108
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKADYEGTVRD-------------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 109 rrgLKRGLKKGYTaeELEQFKA-LLTPLQLglEERLDAEIGLLSGGQRQAVSLLMATLRTPELLLLDEHTAALDPKTQRK 187
Cdd:cd03237 81 ---LLSSITKDFY--THPYFKTeIAKPLQI--EQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLM 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 260158848 188 IMQLTKEIIEEKELTALMITHNLSDALRYGNRLMmmhrgkiiqVFEKE 235
Cdd:cd03237 154 ASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLI---------VFEGE 192
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-254 |
2.50e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 75.10 E-value: 2.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 5 IENVHKTFypntnrSHDALI-DINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAV------EHTAEY 77
Cdd:COG0488 1 LENLSKSF------GGRPLLdDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRigylpqEPPLDD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 78 ERakyisRVYQNPLQGTAPRMTVAQNLSLALRRG------LKR--------GLKKGYTAEelEQFKALLTplQLGL-EER 142
Cdd:COG0488 75 DL-----TVLDTVLDGDAELRALEAELEELEAKLaepdedLERlaelqeefEALGGWEAE--ARAEEILS--GLGFpEED 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 143 LDAEIGLLSGGQRQAVSLLMATLRTPELLLLDEHTAALDpktqrkimqltKEIIE--EKEL-----TALMITHnlsDalR 215
Cdd:COG0488 146 LDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD-----------LESIEwlEEFLknypgTVLVVSH---D--R 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 260158848 216 Y-----GNRLMMMHRGKIIQ--------VFEKEEKEAL---TEEKLYQLMAELDE 254
Cdd:COG0488 210 YfldrvATRILELDRGKLTLypgnysayLEQRAERLEQeaaAYAKQQKKIAKEEE 264
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
13-222 |
3.27e-15 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 72.54 E-value: 3.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 13 YPNTNRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISG-SFPLDKGHIYMGEA--AVEHTAEYE-RAKYISRVYQ 88
Cdd:PRK11629 15 YQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGlDTPTSGDVIFNGQPmsKLSSAAKAElRNQKLGFIYQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 89 npLQGTAPRMTVAQNLSLALRRGLKRglkkgyTAEELEQFKALLTplQLGLEERLDAEIGLLSGGQRQAVSLLMATLRTP 168
Cdd:PRK11629 95 --FHHLLPDFTALENVAMPLLIGKKK------PAEINSRALEMLA--AVGLEHRANHRPSELSGGERQRVAIARALVNNP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 260158848 169 ELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMM 222
Cdd:PRK11629 165 RLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEM 218
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
23-209 |
5.12e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 72.05 E-value: 5.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 23 LIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHI-YMGEAAVEHTAEYERaKYISRVYQNP-LQGTaprmTV 100
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLlFEGEDISTLKPEIYR-QQVSYCAQTPtLFGD----TV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 101 AQNLSLALR-RGLKRGLKKgyTAEELEQFKALLTPLQLGLEErldaeiglLSGGQRQAVSLLMATLRTPELLLLDEHTAA 179
Cdd:PRK10247 98 YDNLIFPWQiRNQQPDPAI--FLDDLERFALPDTILTKNIAE--------LSGGEKQRISLIRNLQFMPKVLLLDEITSA 167
|
170 180 190
....*....|....*....|....*....|
gi 260158848 180 LDPKTQRKIMQLTKEIIEEKELTALMITHN 209
Cdd:PRK10247 168 LDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
22-229 |
5.16e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 72.22 E-value: 5.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 22 ALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEH--TAEYERaKYISRVYQNplQGTAPRMT 99
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwqTAKIMR-EAVAIVPEG--RRVFSRMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 100 VAQNLSLAlrrglkrglkkGYTA--EELEQFKALLTPLQLGLEERLDAEIGLLSGGQRQAVSLLMATLRTPELLLLDEHT 177
Cdd:PRK11614 97 VEENLAMG-----------GFFAerDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 260158848 178 AALDPKTQRKIMQlTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKII 229
Cdd:PRK11614 166 LGLAPIIIQQIFD-TIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
37-230 |
5.83e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 72.82 E-value: 5.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 37 TIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEY------ERAKYISRVYQNPlqGTAPrMTVAQNLsLALRR 110
Cdd:PRK14271 51 SLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFnyrdvlEFRRRVGMLFQRP--NPFP-MSIMDNV-LAGVR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 111 GLKRGLKKGYTAEEleqfKALLTPLQL--GLEERLDAEIGLLSGGQRQAVSLLMATLRTPELLLLDEHTAALDPKTQRKI 188
Cdd:PRK14271 127 AHKLVPRKEFRGVA----QARLTEVGLwdAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKI 202
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 260158848 189 MQLTKEIIEekELTALMITHNLSDALRYGNRLMMMHRGKIIQ 230
Cdd:PRK14271 203 EEFIRSLAD--RLTVIIVTHNLAQAARISDRAALFFDGRLVE 242
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
22-229 |
6.91e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 72.81 E-value: 6.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 22 ALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGS-FPlDKGHIY-MGEAAVEHTAEYerAKYISRVYQNplqgtapRMT 99
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGIlVP-TSGEVRvLGYVPFKRRKEF--ARRIGVVFGQ-------RSQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 100 VAQNL----SLALrrglkrgLKKGY--TAEELEQFKALLTPLqLGLEERLDAEIGLLSGGQRQAVSLLMATLRTPELLLL 173
Cdd:COG4586 107 LWWDLpaidSFRL-------LKAIYriPDAEYKKRLDELVEL-LDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 260158848 174 DEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKII 229
Cdd:COG4586 179 DEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRII 234
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
3-236 |
7.52e-15 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 73.63 E-value: 7.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVhkTF-YPNTNRshDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAK 81
Cdd:COG4618 331 LSVENL--TVvPPGSKR--PILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 82 YISRVYQNP--LQGTaprmtVAQNLS---------------LA------LRrglkrgLKKGYtaeeleqfkalltplqlg 138
Cdd:COG4618 407 HIGYLPQDVelFDGT-----IAENIArfgdadpekvvaaakLAgvhemiLR------LPDGY------------------ 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 139 lEERLDAEIGLLSGGQRQAVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKeLTALMITHNLSdALRYGN 218
Cdd:COG4618 458 -DTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARG-ATVVVITHRPS-LLAAVD 534
|
250
....*....|....*...
gi 260158848 219 RLMMMHRGKIIQVFEKEE 236
Cdd:COG4618 535 KLLVLRDGRVQAFGPRDE 552
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
25-245 |
1.02e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 73.11 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 25 DINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYM-GEAAVEHTAEYERAK---YISRVYQNplQGTAPRMTV 100
Cdd:PRK10762 270 DVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLdGHEVVTRSPQDGLANgivYISEDRKR--DGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 101 AQNLSL-ALRRGLKRGLKKGYTAEEL--EQFKALL---TPlqlgleeRLDAEIGLLSGGQRQAVSLLMATLRTPELLLLD 174
Cdd:PRK10762 348 KENMSLtALRYFSRAGGSLKHADEQQavSDFIRLFnikTP-------SMEQAIGLLSGGNQQKVAIARGLMTRPKVLILD 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 260158848 175 EHTAALDPKTQRKIMQLTKEIIEEKeLTALMITHNLSDALRYGNRLMMMHRGKIIQVFEKEEKealTEEKL 245
Cdd:PRK10762 421 EPTRGVDVGAKKEIYQLINQFKAEG-LSIILVSSEMPEVLGMSDRILVMHEGRISGEFTREQA---TQEKL 487
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-250 |
1.07e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 73.32 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVhkTFYPNTNRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLD-KGHIYMG--EAAVEHTAEYER 79
Cdd:TIGR02633 258 LEARNL--TCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINgkPVDIRNPAQAIR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 80 AKYISRVYQNPLQGTAPRMTVAQNLSLALrrgLKRGLKKGYTAEELEQfKALLTPLQlgleeRL-------DAEIGLLSG 152
Cdd:TIGR02633 336 AGIAMVPEDRKRHGIVPILGVGKNITLSV---LKSFCFKMRIDAAAEL-QIIGSAIQ-----RLkvktaspFLPIGRLSG 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 153 GQRQAVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKeLTALMITHNLSDALRYGNRLMMMHRGKIIQVF 232
Cdd:TIGR02633 407 GNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEG-VAIIVVSSELAEVLGLSDRVLVIGEGKLKGDF 485
|
250
....*....|....*...
gi 260158848 233 EKEEkeaLTEEklyQLMA 250
Cdd:TIGR02633 486 VNHA---LTQE---QVLA 497
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
19-229 |
1.24e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 71.76 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 19 SHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKYISRVYQNPL-QGTAPr 97
Cdd:PRK13652 16 SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPDdQIFSP- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 98 mTVAQNLSLAlrrGLKRGLKKGYTAEELEQfkALLTplqLGLEERLDAEIGLLSGGQRQAVSLLMATLRTPELLLLDEHT 177
Cdd:PRK13652 95 -TVEQDIAFG---PINLGLDEETVAHRVSS--ALHM---LGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 260158848 178 AALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKII 229
Cdd:PRK13652 166 AGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIV 217
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-228 |
1.67e-14 |
|
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: 73.12 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 5 IENVHKTFYPNTNRSHDALidiNLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKYis 84
Cdd:TIGR01257 931 VKNLVKIFEPSGRPAVDRL---NITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSL-- 1005
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 85 rvyqnplqGTAPR-------MTVAQNLslalrrgLKRGLKKGYTAEELE-QFKALLTplQLGLEERLDAEIGLLSGGQRQ 156
Cdd:TIGR01257 1006 --------GMCPQhnilfhhLTVAEHI-------LFYAQLKGRSWEEAQlEMEAMLE--DTGLHHKRNEEAQDLSGGMQR 1068
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 260158848 157 AVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKelTALMITHNLSDALRYGNRLMMMHRGKI 228
Cdd:TIGR01257 1069 KLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGR--TIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-214 |
1.76e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 72.53 E-value: 1.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 29 TIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYmgeaaVEHTAEYeRAKYISrvyqnplqgTAPRMTVAQNLslal 108
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD-----PELKISY-KPQYIK---------PDYDGTVEDLL---- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 109 rRGLKRGLKKGYTAEELeqfkalLTPLQLglEERLDAEIGLLSGGQRQAVSLLMATLRTPELLLLDEHTAALDPKtQRki 188
Cdd:PRK13409 422 -RSITDDLGSSYYKSEI------IKPLQL--ERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE-QR-- 489
|
170 180 190
....*....|....*....|....*....|....*
gi 260158848 189 MQLTKEI---IEEKELTALMITHN------LSDAL 214
Cdd:PRK13409 490 LAVAKAIrriAEEREATALVVDHDiymidyISDRL 524
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-230 |
2.06e-14 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 69.75 E-value: 2.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 2 DIRIENVHKTFYPNTNRshdALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGeaavehtaeyerAK 81
Cdd:cd03369 6 EIEVENLSVRYAPDLPP---VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEID------------GI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 82 YISRVyqnPLQGTAPRMT-VAQN---LSLALRRGLKRGLKkgYTAEELeqFKALLTplqlgleerldAEIGL-LSGGQRQ 156
Cdd:cd03369 71 DISTI---PLEDLRSSLTiIPQDptlFSGTIRSNLDPFDE--YSDEEI--YGALRV-----------SEGGLnLSQGQRQ 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 260158848 157 AVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEiiEEKELTALMITHNLSDALRYgNRLMMMHRGKIIQ 230
Cdd:cd03369 133 LLCLARALLKRPRVLVLDEATASIDYATDALIQKTIRE--EFTNSTILTIAHRLRTIIDY-DKILVMDAGEVKE 203
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-247 |
2.58e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 70.92 E-value: 2.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHkTFYPNTNRshdALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKY 82
Cdd:PRK13647 5 IEVEDLH-FRYKDGTK---ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 83 ISRVYQNPlQGTAPRMTVAQNLSLA-LRRGLKRglkkgytAEELEQFKALLTplQLGLEERLDAEIGLLSGGQRQAVSLL 161
Cdd:PRK13647 81 VGLVFQDP-DDQVFSSTVWDDVAFGpVNMGLDK-------DEVERRVEEALK--AVRMWDFRDKPPYHLSYGQKKRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 162 MATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKElTALMITHNLSDALRYGNRLMMMHRGKIIQvfeKEEKEALT 241
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGK-TVIVATHDVDLAAEWADQVIVLKEGRVLA---EGDKSLLT 226
|
....*.
gi 260158848 242 EEKLYQ 247
Cdd:PRK13647 227 DEDIVE 232
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
22-231 |
3.34e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 70.19 E-value: 3.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 22 ALIDINLTIHKGDFITIVGGNGAGKSTFLNAI------------SGSFPLDKGHIYMgeaavEHTAEYERAKYISRVYQN 89
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndlnpevtiTGSIVYNGHNIYS-----PRTDTVDLRKEIGMVFQQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 90 PlqGTAPrMTVAQNLSLALRRglkRGLKKGYTAEELEQFKALLTPLQLGLEERL-DAEIGLlSGGQRQAVSLLMATLRTP 168
Cdd:PRK14239 95 P--NPFP-MSIYENVVYGLRL---KGIKDKQVLDEAVEKSLKGASIWDEVKDRLhDSALGL-SGGQQQRVCIARVLATSP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 260158848 169 ELLLLDEHTAALDPKTQRKIMQLTKEIieEKELTALMITHNLSDALRYGNRLMMMHRGKIIQV 231
Cdd:PRK14239 168 KIILLDEPTSALDPISAGKIEETLLGL--KDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEY 228
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1-229 |
3.49e-14 |
|
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: 69.12 E-value: 3.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 1 MDIRIENVHKTFYPNTNRSHDALI-DINLTIHKGDFITIVGGNGAGKSTFLNAISGsfpLDKGHIYMGEAAVEHTAEYER 79
Cdd:cd03213 2 VTLSFRNLTVTVKSSPSKSGKQLLkNVSGKAKPGELTAIMGPSGAGKSTLLNALAG---RRTGLGVSGEVLINGRPLDKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 80 A--KYISRVYQNPLqgTAPRMTVAQNLSLAlrrglkrglkkgytaeeleqfkalltplqlgleerldAEIGLLSGGQRQA 157
Cdd:cd03213 79 SfrKIIGYVPQDDI--LHPTLTVRETLMFA-------------------------------------AKLRGLSGGERKR 119
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 260158848 158 VSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKElTALMITHNLSDAL-RYGNRLMMMHRGKII 229
Cdd:cd03213 120 VSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGR-TIICSIHQPSSEIfELFDKLLLLSQGRVI 191
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
26-236 |
3.58e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 70.93 E-value: 3.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 26 INLTIHKGDFITIVGGNGAGKSTFLNAISG--SFPldkGHIyMGEAA------VEHTAEYERAKYI----SRVYQNPLQG 93
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGliDYP---GRV-MAEKLefngqdLQRISEKERRNLVgaevAMIFQDPMTS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 94 TAPRMTVAQNLSLALR--RGLKRGLKKGYTAEeleqfkaLLTplQLGL---EERLDAEIGLLSGGQRQAVSLLMATLRTP 168
Cdd:PRK11022 102 LNPCYTVGFQIMEAIKvhQGGNKKTRRQRAID-------LLN--QVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 260158848 169 ELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKIIQVFEKEE 236
Cdd:PRK11022 173 KLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHD 240
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
22-208 |
3.63e-14 |
|
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: 68.92 E-value: 3.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 22 ALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYM-GEAAVEHTAEYERA-KYISRvyqnpLQGTAPRMT 99
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWnGTPLAEQRDEPHENiLYLGH-----LPGLKPELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 100 VAQNLSLalrrglkrgLKKGYTAEELEQFKALLtplQLGLEERLDAEIGLLSGGQRQAVSLLMATLRTPELLLLDEHTAA 179
Cdd:TIGR01189 90 ALENLHF---------WAAIHGGAQRTIEDALA---AVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
170 180
....*....|....*....|....*....
gi 260158848 180 LDPKTQRKIMQLTKEIIEEKELtALMITH 208
Cdd:TIGR01189 158 LDKAGVALLAGLLRAHLARGGI-VLLTTH 185
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-236 |
3.81e-14 |
|
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: 71.76 E-value: 3.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFypntnRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISG--SFPLDKGHIymgeaaVEHTAEYERA 80
Cdd:TIGR03269 1 IEVKNLTKKF-----DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRI------IYHVALCEKC 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 81 KYI---SRVYQN-PLQGTAPRMTVAQ--NLSLALRRGLKRGL-------------------------KKGYTAEELEQfK 129
Cdd:TIGR03269 70 GYVerpSKVGEPcPVCGGTLEPEEVDfwNLSDKLRRRIRKRIaimlqrtfalygddtvldnvlealeEIGYEGKEAVG-R 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 130 ALLTPLQLGLEERLDAEIGLLSGGQRQAVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITH- 208
Cdd:TIGR03269 149 AVDLIEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHw 228
|
250 260 270
....*....|....*....|....*....|...
gi 260158848 209 -----NLSDalrygnRLMMMHRGKIIQVFEKEE 236
Cdd:TIGR03269 229 pevieDLSD------KAIWLENGEIKEEGTPDE 255
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
21-236 |
4.94e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 71.42 E-value: 4.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 21 DALIDINLTIHKGDFITIVGGNGAGKSTFLNAI------------SGSFPLDKGHIYMGEAAVEHTAEYERAKY--ISRV 86
Cdd:PRK10261 30 AAVRNLSFSLQRGETLAIVGESGSGKSVTALALmrlleqagglvqCDKMLLRRRSRQVIELSEQSAAQMRHVRGadMAMI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 87 YQNPLQGTAPRMTVAQNLSLALRrgLKRGLKKgytAEELEQFKALLTPLQL-GLEERLDAEIGLLSGGQRQAVSLLMATL 165
Cdd:PRK10261 110 FQEPMTSLNPVFTVGEQIAESIR--LHQGASR---EEAMVEAKRMLDQVRIpEAQTILSRYPHQLSGGMRQRVMIAMALS 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 260158848 166 RTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKIIQVFEKEE 236
Cdd:PRK10261 185 CRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQ 255
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
25-229 |
6.52e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 69.83 E-value: 6.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 25 DINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKyISRVYQnpLQGTAPRMTVAQNL 104
Cdd:PRK13537 25 GLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQR-VGVVPQ--FDNLDPDFTVRENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 105 SLALRrglkrglkkgYTAEELEQFKALLTPLQ--LGLEERLDAEIGLLSGGQRQAVSLLMATLRTPELLLLDEHTAALDP 182
Cdd:PRK13537 102 LVFGR----------YFGLSAAAARALVPPLLefAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDP 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 260158848 183 KTQRKIMQLTKEIIEEKElTALMITHNLSDALRYGNRLMMMHRGKII 229
Cdd:PRK13537 172 QARHLMWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVIEEGRKI 217
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
26-239 |
7.73e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 70.77 E-value: 7.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 26 INLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKYISRVYQN-----PLQGtaprmtv 100
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDfhlfdQLLG------- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 101 aqnlslalrrglkrglKKGYTAEELEQFKALLTplqLGLEERLDAEIGL-----LSGGQRQAVSLLMATLRTPELLLLDE 175
Cdd:PRK10522 415 ----------------PEGKPANPALVEKWLER---LKMAHKLELEDGRisnlkLSKGQKKRLALLLALAEERDILLLDE 475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 260158848 176 HTAALDPKTQRKIMQLTKEIIEEKELTALMITHNlsDA-LRYGNRLMMMHRGKIIQVFEKEEKEA 239
Cdd:PRK10522 476 WAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD--DHyFIHADRLLEMRNGQLSELTGEERDAA 538
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
17-250 |
1.19e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 70.06 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 17 NRSHDALIDINLTIHKGDfitIVG-----GNgaGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKY-ISRVYQNP 90
Cdd:COG3845 268 DRGVPALKDVSLEVRAGE---ILGiagvaGN--GQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYIPEDR 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 91 L-QGTAPRMTVAQNLSL------ALRRG--LKRGLKKGYTAEELEQFKaLLTPlqlgleeRLDAEIGLLSGGQRQAVSLL 161
Cdd:COG3845 343 LgRGLVPDMSVAENLILgryrrpPFSRGgfLDRKAIRAFAEELIEEFD-VRTP-------GPDTPARSLSGGNQQKVILA 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 162 MATLRTPELLLLDEHTAALDPKTQRKIMQltkEIIEEKE--LTALMITHNLSDALRYGNRLMMMHRGKIIQVFEKEEkea 239
Cdd:COG3845 415 RELSRDPKLLIAAQPTRGLDVGAIEFIHQ---RLLELRDagAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAE--- 488
|
250
....*....|.
gi 260158848 240 LTEEKLYQLMA 250
Cdd:COG3845 489 ATREEIGLLMA 499
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
26-229 |
1.26e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 68.66 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 26 INLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEhtaEYERAKYISRVYQNPLQ-GTAPRMTVAQnl 104
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLE---SWSSKAFARKVAYLPQQlPAAEGMTVRE-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 105 SLALRRGLKRGLKKGYTAEELEQFKALLTPLQLG-LEERLdaeIGLLSGGQRQAVSLLMATLRTPELLLLDEHTAALDPK 183
Cdd:PRK10575 105 LVAIGRYPWHGALGRFGAADREKVEEAISLVGLKpLAHRL---VDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 260158848 184 TQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKII 229
Cdd:PRK10575 182 HQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMI 227
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
25-208 |
1.67e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 69.84 E-value: 1.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 25 DINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAavehtaeyERAKYISrvyQNP--LQGTaprmtvaq 102
Cdd:COG4178 381 DLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAG--------ARVLFLP---QRPylPLGT-------- 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 103 nlslaLRRGLKR-GLKKGYTAEELEQfkaLLTPLQLG-LEERLDAEIG---LLSGGQRQAVSLLMATLRTPELLLLDEHT 177
Cdd:COG4178 442 -----LREALLYpATAEAFSDAELRE---ALEAVGLGhLAERLDEEADwdqVLSLGEQQRLAFARLLLHKPDWLFLDEAT 513
|
170 180 190
....*....|....*....|....*....|.
gi 260158848 178 AALDPKTQRKIMQLTKEiiEEKELTALMITH 208
Cdd:COG4178 514 SALDEENEAALYQLLRE--ELPGTTVISVGH 542
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
20-210 |
2.36e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 69.35 E-value: 2.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 20 HDALIDINLTIHKGDFITIVGGNGAGKST----FLNAISGsfpldKGHIYMGEAAVEHTAEYERAKYISR---VYQNPLQ 92
Cdd:PRK15134 299 NVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQPLHNLNRRQLLPVRHRiqvVFQDPNS 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 93 GTAPRMTVAQNLSLALRRGlkrglKKGYTAEELEQfKALLTPLQLGLE----ERLDAEiglLSGGQRQAVSLLMATLRTP 168
Cdd:PRK15134 374 SLNPRLNVLQIIEEGLRVH-----QPTLSAAQREQ-QVIAVMEEVGLDpetrHRYPAE---FSGGQRQRIAIARALILKP 444
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 260158848 169 ELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNL 210
Cdd:PRK15134 445 SLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDL 486
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
16-245 |
2.79e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 69.04 E-value: 2.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 16 TNRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAK----YISRVYQNpl 91
Cdd:PRK09700 272 TSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKkgmaYITESRRD-- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 92 QGTAPRMTVAQNLSLAlrRGLKRGLKKGYTA---EELEQFKALLTPLQLGLE-ERLDAEIGLLSGGQRQAVSLLMATLRT 167
Cdd:PRK09700 350 NGFFPNFSIAQNMAIS--RSLKDGGYKGAMGlfhEVDEQRTAENQRELLALKcHSVNQNITELSGGNQQKVLISKWLCCC 427
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 260158848 168 PELLLLDEHTAALDPKTQRKIMQLTKEIIEEKElTALMITHNLSDALRYGNRLMMMHRGKIIQVFEKeeKEALTEEKL 245
Cdd:PRK09700 428 PEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGK-VILMVSSELPEIITVCDRIAVFCEGRLTQILTN--RDDMSEEEI 502
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
25-229 |
2.90e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 67.23 E-value: 2.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 25 DINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKY-ISRVYQNPlqGTAPRMTVAQN 103
Cdd:PRK10895 21 DVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgIGYLPQEA--SIFRRLSVYDN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 104 LS--LALRRGLKRGLKKGYTAEELEQFKALLTPLQLGLEerldaeiglLSGGQRQAVSLLMATLRTPELLLLDEHTAALD 181
Cdd:PRK10895 99 LMavLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQS---------LSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 260158848 182 PKTQRKImqltKEIIE---EKELTALMITHNLSDALRYGNRLMMMHRGKII 229
Cdd:PRK10895 170 PISVIDI----KRIIEhlrDSGLGVLITDHNVRETLAVCERAYIVSQGHLI 216
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-243 |
3.13e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 67.38 E-value: 3.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 23 LIDINLTIHKGDFITIVGGNGAGKSTFLNAIS-------GSFPLDKGHIYMGEAAVEHTAEYERaKYISRVYQNPlqGTA 95
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNrlieiydSKIKVDGKVLYFGKDIFQIDAIKLR-KEVGMVFQQP--NPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 96 PRMTVAQNLSLALRrglKRGLKKGYTAEELEQFKALLTPLQLGLEERLDAEIGLLSGGQRQAVSLLMATLRTPELLLLDE 175
Cdd:PRK14246 103 PHLSIYDNIAYPLK---SHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 260158848 176 HTAALDPKTQRKIMQLTKEIieEKELTALMITHNLSDALRYGNRLMMMHRGKIIQVFEKEE-----KEALTEE 243
Cdd:PRK14246 180 PTSMIDIVNSQAIEKLITEL--KNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEiftspKNELTEK 250
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-233 |
5.06e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 66.98 E-value: 5.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVhkTFYPNTNRshdALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDkghiymGEAAVEHTAE------ 76
Cdd:PRK14258 8 IKVNNL--SFYYDTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE------SEVRVEGRVEffnqni 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 77 YERAKYISRVYQN-----PLQGTAPrMTVAQNLSLALRR-GLKRGLKKGYTAEELEQFKALLTPLQLGLEER-LDaeigl 149
Cdd:PRK14258 77 YERRVNLNRLRRQvsmvhPKPNLFP-MSVYDNVAYGVKIvGWRPKLEIDDIVESALKDADLWDEIKHKIHKSaLD----- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 150 LSGGQRQAVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMH--RGK 227
Cdd:PRK14258 151 LSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKgnENR 230
|
....*.
gi 260158848 228 IIQVFE 233
Cdd:PRK14258 231 IGQLVE 236
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-228 |
5.09e-13 |
|
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: 68.82 E-value: 5.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 23 LIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKYISRVYQNPLQgtaprmtvaq 102
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVL---------- 1371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 103 nLSLALRRGL----KRGLKKGYTAEELEQFKALLTPLQLGLEERLdAEIGL-LSGGQRQAVSLLMATLRTPELLLLDEHT 177
Cdd:TIGR00957 1372 -FSGSLRMNLdpfsQYSDEEVWWALELAHLKTFVSALPDKLDHEC-AEGGEnLSVGQRQLVCLARALLRKTKILVLDEAT 1449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 260158848 178 AALDPKTQRKIMQLTKEIIEekELTALMITHNLSDALRYgNRLMMMHRGKI 228
Cdd:TIGR00957 1450 AAVDLETDNLIQSTIRTQFE--DCTVLTIAHRLNTIMDY-TRVIVLDKGEV 1497
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-210 |
5.27e-13 |
|
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: 68.27 E-value: 5.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 29 TIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMgEAAVEHTAEYERAKYisrvyqnplqgtapRMTVAQNlslaL 108
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDE-DLKISYKPQYISPDY--------------DGTVEEF----L 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 109 RRGLKRGLKKGYTAEEleqfkaLLTPlqLGLEERLDAEIGLLSGGQRQAVSLLMATLRTPELLLLDEHTAALDPKtQRki 188
Cdd:COG1245 423 RSANTDDFGSSYYKTE------IIKP--LGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE-QR-- 491
|
170 180
....*....|....*....|....*
gi 260158848 189 MQLTKEI---IEEKELTALMITHNL 210
Cdd:COG1245 492 LAVAKAIrrfAENRGKTAMVVDHDI 516
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
13-226 |
3.01e-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: 66.58 E-value: 3.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 13 YPNTnrSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTaeyerakyISRVYQNplQ 92
Cdd:TIGR01257 1947 YSGT--SSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTN--------ISDVHQN--M 2014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 93 GTAPRMTVAQNLSLALRRGLKRGLKKGYTAEELEQFkALLTPLQLGLEERLDAEIGLLSGGQRQAVSLLMATLRTPELLL 172
Cdd:TIGR01257 2015 GYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKV-ANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVL 2093
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 260158848 173 LDEHTAALDPKTQRKIMQLTKEIIEEkELTALMITHNLSDALRYGNRLMMMHRG 226
Cdd:TIGR01257 2094 LDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
20-223 |
4.22e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 64.52 E-value: 4.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 20 HDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKYISRvyQNPLQGTAPrmT 99
Cdd:PRK15056 20 HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQ--SEEVDWSFP--V 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 100 VAQNLSLALRRGlKRGLKKGYTAEELEQFKALLTplQLGLEERLDAEIGLLSGGQRQAVSLLMATLRTPELLLLDEHTAA 179
Cdd:PRK15056 96 LVEDVVMMGRYG-HMGWLRRAKKRDRQIVTAALA--RVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 260158848 180 LDPKTQRKIMQLTKEIIEEKElTALMITHNLSDALRYGNRLMMM 223
Cdd:PRK15056 173 VDVKTEARIISLLRELRDEGK-TMLVSTHNLGSVTEFCDYTVMV 215
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
3-236 |
4.66e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 65.77 E-value: 4.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFYPNTNrshDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKY 82
Cdd:PLN03232 1235 IKFEDVHLRYRPGLP---PVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRV 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 83 ISRVYQNPLQGTAprmTVAQNLSlALRRGLKRGLkkgYTAEELEQFKALLTPLQLGLEERLDAEIGLLSGGQRQAVSLLM 162
Cdd:PLN03232 1312 LSIIPQSPVLFSG---TVRFNID-PFSEHNDADL---WEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLAR 1384
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 260158848 163 ATLRTPELLLLDEHTAALDPKTQRKIMQLTKEiiEEKELTALMITHNLSDALRYgNRLMMMHRGKIIQVFEKEE 236
Cdd:PLN03232 1385 ALLRRSKILVLDEATASVDVRTDSLIQRTIRE--EFKSCTMLVIAHRLNTIIDC-DKILVLSSGQVLEYDSPQE 1455
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
3-208 |
5.16e-12 |
|
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: 61.70 E-value: 5.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFYpntnrSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIymgeaavehtaeyeraky 82
Cdd:cd03221 1 IELENLSKTYG-----GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV------------------ 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 83 isrvyqnplqgtaprmTVAQNLSLalrrglkrglkkGYtaeeLEQfkalltplqlgleerldaeiglLSGGQRQAVSLLM 162
Cdd:cd03221 58 ----------------TWGSTVKI------------GY----FEQ----------------------LSGGEKMRLALAK 83
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 260158848 163 ATLRTPELLLLDEHTAALDPKTqrkIMQLTkEIIEEKELTALMITH 208
Cdd:cd03221 84 LLLENPNLLLLDEPTNHLDLES---IEALE-EALKEYPGTVILVSH 125
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
25-186 |
5.81e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 62.97 E-value: 5.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 25 DINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKYISrvYQNPLQgtaPRMTVAQNL 104
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG--HRNAMK---PALTVAENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 105 SL--ALRRGLKRGLkkgytAEELEQFkalltplqlGLEERLDAEIGLLSGGQRQAVSL--LMATLRTpeLLLLDEHTAAL 180
Cdd:PRK13539 95 EFwaAFLGGEELDI-----AAALEAV---------GLAPLAHLPFGYLSAGQKRRVALarLLVSNRP--IWILDEPTAAL 158
|
....*.
gi 260158848 181 DPKTQR 186
Cdd:PRK13539 159 DAAAVA 164
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
3-210 |
6.52e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 63.59 E-value: 6.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFypntnRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIymgeaavehtaEYERAKY 82
Cdd:PRK09544 5 VSLENVSVSF-----GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRNGKLR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 83 ISRVYQN-PLQGTAPrMTVAQNLSLalrrglKRGLKKGYTAEELEQFKAlltplqlglEERLDAEIGLLSGGQRQAVSLL 161
Cdd:PRK09544 69 IGYVPQKlYLDTTLP-LTVNRFLRL------RPGTKKEDILPALKRVQA---------GHLIDAPMQKLSGGETQRVLLA 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 260158848 162 MATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNL 210
Cdd:PRK09544 133 RALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDL 181
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-226 |
1.15e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 64.04 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFYPNTnrshdALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKY 82
Cdd:PRK09700 6 ISMAGIGKSFGPVH-----ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 83 -ISRVYQNplQGTAPRMTVAQNLSLAlRRGLKRGLKKGYTAEELEQFKALLTPLQLGLEERLDAEIGLLSGGQRQAVSLL 161
Cdd:PRK09700 81 gIGIIYQE--LSVIDELTVLENLYIG-RHLTKKVCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 260158848 162 MATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIieEKELTALM-ITHNLSDALRYGNRLMMMHRG 226
Cdd:PRK09700 158 KTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQL--RKEGTAIVyISHKLAEIRRICDRYTVMKDG 221
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
20-194 |
1.22e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 62.27 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 20 HDALIDINLTIH--KGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHtaeyERAkyisrVYQNPLQGTAPR 97
Cdd:PRK13540 12 HDQPLLQQISFHlpAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK----DLC-----TYQKQLCFVGHR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 98 MTVaqNLSLALRRGLKRGLKKGYTAEELEQFKALLTplqlgLEERLDAEIGLLSGGQRQAVSLLMATLRTPELLLLDEHT 177
Cdd:PRK13540 83 SGI--NPYLTLRENCLYDIHFSPGAVGITELCRLFS-----LEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
170
....*....|....*..
gi 260158848 178 AALDPKTQRKIMQLTKE 194
Cdd:PRK13540 156 VALDELSLLTIITKIQE 172
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
3-223 |
1.39e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 64.28 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHktFYPNTNRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEA--AVEHTAEYERA 80
Cdd:PTZ00265 383 IQFKNVR--FHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShnLKDINLKWWRS 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 81 KyISRVYQNPL---------------------------------------QGTAPRMTVAQNLSLALRRGLKRGL---KK 118
Cdd:PTZ00265 461 K-IGVVSQDPLlfsnsiknnikyslyslkdlealsnyynedgndsqenknKRNSCRAKCAGDLNDMSNTTDSNELiemRK 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 119 GY-TAEELEQF----KALLTPLQLGLEERLDAEIGL----LSGGQRQAVSLLMATLRTPELLLLDEHTAALDPKTQRKIM 189
Cdd:PTZ00265 540 NYqTIKDSEVVdvskKVLIHDFVSALPDKYETLVGSnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQ 619
|
250 260 270
....*....|....*....|....*....|....
gi 260158848 190 QLTKEIIEEKELTALMITHNLSdALRYGNRLMMM 223
Cdd:PTZ00265 620 KTINNLKGNENRITIIIAHRLS-TIRYANTIFVL 652
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
18-229 |
2.24e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 62.54 E-value: 2.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 18 RSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFP---LDKGHIYMGEAAV--EHTAEYErAKYISRVYQNPLQ 92
Cdd:PRK13547 12 RHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggAPRGARVTGDVTLngEPLAAID-APRLARLRAVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 93 GTAPRMTVAQNLSLAL------RRGLKRGLKKGYTAEEleqfkalltPLQLGLEERLDA-EIGLLSGGQ--RQAVSLLMA 163
Cdd:PRK13547 91 AAQPAFAFSAREIVLLgryphaRRAGALTHRDGEIAWQ---------ALALAGATALVGrDVTTLSGGElaRVQFARVLA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 260158848 164 TL-------RTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKII 229
Cdd:PRK13547 162 QLwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIV 234
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
25-214 |
2.84e-11 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 62.09 E-value: 2.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 25 DINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYM-GE--AAVEHTAEYERAKYISRVYQNPLQGTapRMTVA 101
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFdGEniPAMSRSRLYTVRKRMSMLFQSGALFT--DMNVF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 102 QNLSLALRRGLKrglkkgyTAEELEQFKALLTPLQLGLEERLDAEIGLLSGGQRQAVSLLMATLRTPELLLLDEHTAALD 181
Cdd:PRK11831 103 DNVAYPLREHTQ-------LPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQD 175
|
170 180 190
....*....|....*....|....*....|...
gi 260158848 182 PKTQRKIMQLTKEIIEEKELTALMITHNLSDAL 214
Cdd:PRK11831 176 PITMGVLVKLISELNSALGVTCVVVSHDVPEVL 208
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
22-249 |
4.35e-11 |
|
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: 62.53 E-value: 4.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 22 ALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLD--KGHIYMGEAAVE--HTAEYERAKyISRVYQNPLqgTAPR 97
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKasNIRDTERAG-IVIIHQELT--LVPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 98 MTVAQNLSLALRRGLKRGLKKgyTAEELEQFKALLTPLQLGLEErLDAEIGLLSGGQRQAVSLLMATLRTPELLLLDEHT 177
Cdd:TIGR02633 93 LSVAENIFLGNEITLPGGRMA--YNAMYLRAKNLLRELQLDADN-VTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPS 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 260158848 178 AALDPKTQRKIMQLTKEiIEEKELTALMITHNLSDALRYGNRLMMMHRGKIIQVfekEEKEALTEEKLYQLM 249
Cdd:TIGR02633 170 SSLTEKETEILLDIIRD-LKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVAT---KDMSTMSEDDIITMM 237
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
22-249 |
5.99e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 62.11 E-value: 5.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 22 ALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPldkgH-------IYMGEAAVEHTAEYERAKYISRVYQNplQGT 94
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYP----HgsyegeiLFDGEVCRFKDIRDSEALGIVIIHQE--LAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 95 APRMTVAQNLSLALRRGlKRGLKKgyTAEELEQFKALLTplQLGLEERLDAEIGLLSGGQRQAVSLLMATLRTPELLLLD 174
Cdd:NF040905 90 IPYLSIAENIFLGNERA-KRGVID--WNETNRRARELLA--KVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILD 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 260158848 175 EHTAALDPKTQRKIMQLTKEiIEEKELTALMITHNLSDALRYGNRLMMMHRGKIIQVFEKeEKEALTEEKLYQLM 249
Cdd:NF040905 165 EPTAALNEEDSAALLDLLLE-LKAQGITSIIISHKLNEIRRVADSITVLRDGRTIETLDC-RADEVTEDRIIRGM 237
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
38-252 |
6.32e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 61.18 E-value: 6.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 38 IVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERA--KYISRVYQNPLQGTApRMTVAQNLSLALRR----- 110
Cdd:PRK13638 32 LVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLAlrQQVATVFQDPEQQIF-YTDIDSDIAFSLRNlgvpe 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 111 -GLKRGLKKGYTAEELEQFKAllTPLQLgleerldaeiglLSGGQRQAVSLLMATLRTPELLLLDEHTAALDPKTQRKIM 189
Cdd:PRK13638 111 aEITRRVDEALTLVDAQHFRH--QPIQC------------LSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMI 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 260158848 190 QLTKEIIEEKELTALM-----ITHNLSDA---LRYGNRLMMMHRGKIIQVFEKEEKEALTEEKLYQLMAEL 252
Cdd:PRK13638 177 AIIRRIVAQGNHVIISshdidLIYEISDAvyvLRQGQILTHGAPGEVFACTEAMEQAGLTQPWLVKLHTQL 247
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
23-229 |
9.37e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 61.60 E-value: 9.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 23 LIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPldKGHIYMGEAAVE-HTAEYERAKYISR-VYQNPLqgTAPRMTV 100
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSP--KGVKGSGSVLLNgMPIDAKEMRAISAyVQQDDL--FIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 101 AQNLSLALRRGLKRGLKKgytAEELEQFKALLTplQLGLEERLDAEIGL------LSGGQRQAVSLLMATLRTPELLLLD 174
Cdd:TIGR00955 117 REHLMFQAHLRMPRRVTK---KEKRERVDEVLQ--ALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCD 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 260158848 175 EHTAALDPKTQRKIMQLTKEiIEEKELTALMITHNLSDAL-RYGNRLMMMHRGKII 229
Cdd:TIGR00955 192 EPTSGLDSFMAYSVVQVLKG-LAQKGKTIICTIHQPSSELfELFDKIILMAEGRVA 246
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
3-229 |
1.15e-10 |
|
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: 61.37 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHktFypntnrSHDA----LIDINLTIHKGDFITIVGGNGAGKST-------FLNAISGSFPLDkGHiymgeaav 71
Cdd:COG5265 358 VRFENVS--F------GYDPerpiLKGVSFEVPAGKTVAIVGPSGAGKSTlarllfrFYDVTSGRILID-GQ-------- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 72 ehtaeyerakYISRVYQNPLQ---GTAPRMTVAQNLSLA--LRRGlkrglKKGYTAEELEQF--KALLTPLQLGLEERLD 144
Cdd:COG5265 421 ----------DIRDVTQASLRaaiGIVPQDTVLFNDTIAynIAYG-----RPDASEEEVEAAarAAQIHDFIESLPDGYD 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 145 AEIG---L-LSGGQRQAVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKelTALMITHNLS---DAlryg 217
Cdd:COG5265 486 TRVGergLkLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGR--TTLVIAHRLStivDA---- 559
|
250
....*....|..
gi 260158848 218 NRLMMMHRGKII 229
Cdd:COG5265 560 DEILVLEAGRIV 571
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
23-208 |
1.35e-10 |
|
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: 58.32 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 23 LIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMgeAAVEHTAeyerakYISrvyQNPL--QGTaprmtv 100
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM--PEGEDLL------FLP---QRPYlpLGT------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 101 aqnlslaLRRglkrglkkgytaeeleqfkALLTPLQLgleerldaeigLLSGGQRQAVSLLMATLRTPELLLLDEHTAAL 180
Cdd:cd03223 80 -------LRE-------------------QLIYPWDD-----------VLSGGEQQRLAFARLLLHKPKFVFLDEATSAL 122
|
170 180
....*....|....*....|....*...
gi 260158848 181 DPKTQRKIMQLtkeiIEEKELTALMITH 208
Cdd:cd03223 123 DEESEDRLYQL----LKELGITVISVGH 146
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
23-229 |
2.20e-10 |
|
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: 58.69 E-value: 2.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 23 LIDINLTIHKGDFITIVGGNGAGKSTFLNAISG--SFPLDKGHIYMGEAAVEHTAEYERAK---YISrvYQNPLQgtAPR 97
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGEDITDLPPEERARlgiFLA--FQYPPE--IPG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 98 MTVAQNLslalrrglkRGLKKGytaeeleqfkalltplqlgleerldaeiglLSGGQRQAVSLL-MATLRtPELLLLDEH 176
Cdd:cd03217 92 VKNADFL---------RYVNEG------------------------------FSGGEKKRNEILqLLLLE-PDLAILDEP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 260158848 177 TAALDPKTQRKIMQLTKEIIEEKElTALMITHN--LSDALRyGNRLMMMHRGKII 229
Cdd:cd03217 132 DSGLDIDALRLVAEVINKLREEGK-SVLIITHYqrLLDYIK-PDRVHVLYDGRIV 184
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
25-230 |
2.62e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 58.94 E-value: 2.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 25 DINLTIHKGDFITIVGGNGAGKSTFLNAISGSFP----LDKGHIYMGEAAVEhtAEYERAKYISRVYQNPLQGTAPRMTV 100
Cdd:PRK10418 21 GVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPagvrQTAGRVLLDGKPVA--PCALRGRKIATIMQNPRSAFNPLHTM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 101 AqnlSLALRRGLKRGlKKGYTAEELEQFKALltplqlGLEER---LDAEIGLLSGGQRQAVSLLMATLRTPELLLLDEHT 177
Cdd:PRK10418 99 H---THARETCLALG-KPADDATLTAALEAV------GLENAarvLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 260158848 178 AALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKIIQ 230
Cdd:PRK10418 169 TDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVE 221
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
25-230 |
3.58e-10 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 58.54 E-value: 3.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 25 DINLTIHKGDFITIVGGNGAGKSTFLNAISG--SFPLDKGHI-YMGEAAVEHTAEyERAKY-ISRVYQNPLQgtAPRMTV 100
Cdd:COG0396 18 GVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSIlLDGEDILELSPD-ERARAgIFLAFQYPVE--IPGVSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 101 AQNLSLALRrglKRGLKKGYTAEELEQFKALLTplQLGL-EERLDAEIGL-LSGGQRQAVSLLMATLRTPELLLLDEHTA 178
Cdd:COG0396 95 SNFLRTALN---ARRGEELSAREFLKLLKEKMK--ELGLdEDFLDRYVNEgFSGGEKKRNEILQMLLLEPKLAILDETDS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 260158848 179 ALDPKTQRKIMQLTKEIIEEkELTALMITHN--LsdaLRYGN--RLMMMHRGKIIQ 230
Cdd:COG0396 170 GLDIDALRIVAEGVNKLRSP-DRGILIITHYqrI---LDYIKpdFVHVLVDGRIVK 221
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
22-249 |
4.81e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 59.17 E-value: 4.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 22 ALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLD--KGHIYMGEAAVE--HTAEYERAKyISRVYQNPLqgTAPR 97
Cdd:PRK13549 20 ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELQasNIRDTERAG-IAIIHQELA--LVKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 98 MTVAQNLSLAlrRGLKRGLKKGYTAEELEQfKALLTplQLGLEERLDAEIGLLSGGQRQAVSLLMATLRTPELLLLDEHT 177
Cdd:PRK13549 97 LSVLENIFLG--NEITPGGIMDYDAMYLRA-QKLLA--QLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPT 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 260158848 178 AALDPKTQRKIMQLTKEiIEEKELTALMITHNLSDALRYGNRLMMMHRGKIIQVfekEEKEALTEEKLYQLM 249
Cdd:PRK13549 172 ASLTESETAVLLDIIRD-LKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGT---RPAAGMTEDDIITMM 239
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
3-239 |
5.87e-10 |
|
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: 59.04 E-value: 5.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFYPNTNRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVehTAEyERAKY 82
Cdd:COG4615 328 LELRGVTYRYPGEDGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV--TAD-NREAY 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 83 ---ISRVYQNP-----LQGTAPrmtvaqnlslalrrglkrglkkgytAEELEQFKALLTplQLGLEERLDAEIGL----- 149
Cdd:COG4615 405 rqlFSAVFSDFhlfdrLLGLDG-------------------------EADPARARELLE--RLELDHKVSVEDGRfsttd 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 150 LSGGQRQAVSLLMATLRTPELLLLDEHTAALDPkTQRKImqLTKEIIEE-KEL--TALMITHNlsDalRY---GNRLMMM 223
Cdd:COG4615 458 LSQGQRKRLALLVALLEDRPILVFDEWAADQDP-EFRRV--FYTELLPElKARgkTVIAISHD--D--RYfdlADRVLKM 530
|
250
....*....|....*.
gi 260158848 224 HRGKIIQVFEKEEKEA 239
Cdd:COG4615 531 DYGKLVELTGPAALAA 546
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
19-215 |
7.91e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 57.87 E-value: 7.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 19 SHDALIDINLTIHKGDFITIVGGNGAGKSTFL------NAISGSFPLDKGHIYMGEAAVE-HTAEYERAKYISRVYQNPl 91
Cdd:PRK14243 22 SFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlNDLIPGFRVEGKVTFHGKNLYApDVDPVEVRRRIGMVFQKP- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 92 qGTAPRmTVAQNLSLALR-RGLKRGLkkgytaEELEQFKALLTPLQLGLEERLDAEIGLLSGGQRQAVSLLMATLRTPEL 170
Cdd:PRK14243 101 -NPFPK-SIYDNIAYGARiNGYKGDM------DELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 260158848 171 LLLDEHTAALDPKTQRKIMQLTKEIIEekELTALMITHNLSDALR 215
Cdd:PRK14243 173 ILMDEPCSALDPISTLRIEELMHELKE--QYTIIIVTHNMQQAAR 215
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
5-229 |
9.13e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 57.34 E-value: 9.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 5 IENVHKTFypNTNrshDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISG--SFPLDKGHI-YMGEAAVEHTAEyERAK 81
Cdd:CHL00131 10 IKNLHASV--NEN---EILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDIlFKGESILDLEPE-ERAH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 82 Y-ISRVYQNPLqgTAPRMTVAQNLSLALRRGLK-RGLKKgytAEELEQFKALLTPLQL-GLEERL---DAEIGlLSGGQR 155
Cdd:CHL00131 84 LgIFLAFQYPI--EIPGVSNADFLRLAYNSKRKfQGLPE---LDPLEFLEIINEKLKLvGMDPSFlsrNVNEG-FSGGEK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 156 QAVSLLMATLRTPELLLLDEHTAALD-------PKTQRKIMQLTKEIIeekeltalMITH--NLSDALRyGNRLMMMHRG 226
Cdd:CHL00131 158 KRNEILQMALLDSELAILDETDSGLDidalkiiAEGINKLMTSENSII--------LITHyqRLLDYIK-PDYVHVMQNG 228
|
...
gi 260158848 227 KII 229
Cdd:CHL00131 229 KII 231
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
4-244 |
9.78e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 58.40 E-value: 9.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 4 RIENVhkTFYPNTNRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFP-LDKGHIYMG--EAAVEHTAEYERA 80
Cdd:PRK13549 261 EVRNL--TAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDgkPVKIRNPQQAIAQ 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 81 KyISRVYQN-PLQGTAPRMTVAQNLSLALrrgLKRGLKKGYTAEELEQFKALLTPLQLGLE-ERLDAEIGLLSGGQRQAV 158
Cdd:PRK13549 339 G-IAMVPEDrKRDGIVPVMGVGKNITLAA---LDRFTGGSRIDDAAELKTILESIQRLKVKtASPELAIARLSGGNQQKA 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 159 SLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKeLTALMITHNLSDALRYGNRLMMMHRGKIIQVFEKEEke 238
Cdd:PRK13549 415 VLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQG-VAIIVISSELPEVLGLSDRVLVMHEGKLKGDLINHN-- 491
|
....*.
gi 260158848 239 aLTEEK 244
Cdd:PRK13549 492 -LTQEQ 496
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
26-236 |
1.08e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.60 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 26 INLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKYISRVYQNPLQGTAprmTVAQNLS 105
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSG---TVRFNLD 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 106 -------LALRRGLKRGlkkgytaeeleQFKALLTPLQLGLeerlDAEIGL----LSGGQRQAVSLLMATLRTPELLLLD 174
Cdd:PLN03130 1335 pfnehndADLWESLERA-----------HLKDVIRRNSLGL----DAEVSEagenFSVGQRQLLSLARALLRRSKILVLD 1399
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 260158848 175 EHTAALDPKTQRKIMqltKEIIEE-KELTALMITHNLSDALRyGNRLMMMHRGKIIQVFEKEE 236
Cdd:PLN03130 1400 EATAAVDVRTDALIQ---KTIREEfKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPEN 1458
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
23-181 |
1.45e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 58.02 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 23 LIDINLTIHKGDFITIVGGNGAGKSTFLNAISGsfpLDKGhiYMGEAAVehtaeyerAKYISRVY--QNPLqgTAPRMTV 100
Cdd:TIGR03719 21 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG---VDKD--FNGEARP--------QPGIKVGYlpQEPQ--LDPTKTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 101 AQNLSLALRRglKRGLKKGYT------AEELEQFKALLTPlQLGLEERL------------------------DAEIGLL 150
Cdd:TIGR03719 86 RENVEEGVAE--IKDALDRFNeisakyAEPDADFDKLAAE-QAELQEIIdaadawdldsqleiamdalrcppwDADVTKL 162
|
170 180 190
....*....|....*....|....*....|.
gi 260158848 151 SGGQRQAVSLLMATLRTPELLLLDEHTAALD 181
Cdd:TIGR03719 163 SGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
25-181 |
1.57e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 56.35 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 25 DINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYM-GEAAVEHTAEYerakyisrvYQNPL-----QGTAPRM 98
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWqGEPIRRQRDEY---------HQDLLylghqPGIKTEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 99 TVAQNLSLALRrglkrgLKKGYTAEELEQfkALltpLQLGLEERLDAEIGLLSGGQRQAVSLLMATLRTPELLLLDEHTA 178
Cdd:PRK13538 90 TALENLRFYQR------LHGPGDDEALWE--AL---AQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFT 158
|
...
gi 260158848 179 ALD 181
Cdd:PRK13538 159 AID 161
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-231 |
3.60e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.79 E-value: 3.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 18 RSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERA---KYISRVYQNPLQGT 94
Cdd:PRK10261 335 REVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQalrRDIQFIFQDPYASL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 95 APRMTVAQNLSLALRrglKRGLKKGYTAEEleQFKALLTPLQLGLEE--RLDAEiglLSGGQRQAVSLLMATLRTPELLL 172
Cdd:PRK10261 415 DPRQTVGDSIMEPLR---VHGLLPGKAAAA--RVAWLLERVGLLPEHawRYPHE---FSGGQRQRICIARALALNPKVII 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 260158848 173 LDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKIIQV 231
Cdd:PRK10261 487 ADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEI 545
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
3-236 |
4.68e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 55.59 E-value: 4.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHK---TFYPNTNRSHDALI------------DINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIymg 67
Cdd:PRK13546 5 VNIKNVTKeyrIYRTNKERMKDALIpkhknktffaldDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 68 eaavehtaeyERAKYISRVYQNplQGTAPRMTVAQNLSLALrrglkrgLKKGYTAEELEQfkalLTP-----LQLGleER 142
Cdd:PRK13546 82 ----------DRNGEVSVIAIS--AGLSGQLTGIENIEFKM-------LCMGFKRKEIKA----MTPkiiefSELG--EF 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 143 LDAEIGLLSGGQRQAVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKElTALMITHNLSDALRYGNRLMM 222
Cdd:PRK13546 137 IYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEQNK-TIFFVSHNLGQVRQFCTKIAW 215
|
250
....*....|....
gi 260158848 223 MHRGKIIQVFEKEE 236
Cdd:PRK13546 216 IEGGKLKDYGELDD 229
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
10-229 |
8.58e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.89 E-value: 8.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 10 KTFYPNTNRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSfpLDKGHI-------YMGeaaveHT-AEYERAK 81
Cdd:TIGR00956 64 KLKKFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASN--TDGFHIgvegvitYDG-----ITpEEIKKHY 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 82 YISRVYQNPLQGTAPRMTVAQNLSLALRRGLKRGLKKGYTAEELEQFKALLTPLQLGLEERLDAEIGL-----LSGGQRQ 156
Cdd:TIGR00956 137 RGDVVYNAETDVHFPHLTVGETLDFAARCKTPQNRPDGVSREEYAKHIADVYMATYGLSHTRNTKVGNdfvrgVSGGERK 216
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 260158848 157 AVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLS-DALRYGNRLMMMHRGKII 229
Cdd:TIGR00956 217 RVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCSqDAYELFDKVIVLYEGYQI 290
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
98-215 |
1.03e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.81 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 98 MTVAQNLSL----ALRRGLKRGLKKGYTAEELEQfkalltplqlgLEERLDAEIG----LLSGGQRQAVSLLMATLRTPE 169
Cdd:PTZ00265 1310 MSIYENIKFgkedATREDVKRACKFAAIDEFIES-----------LPNKYDTNVGpygkSLSGGQKQRIAIARALLREPK 1378
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 260158848 170 LLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALR 215
Cdd:PTZ00265 1379 ILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR 1424
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
28-184 |
3.30e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.80 E-value: 3.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 28 LTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIymgeaavehtaEYERAKYISRVYQNP---LQGTAPRMTVA--Q 102
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRI-----------IYEQDLIVARLQQDPprnVEGTVYDFVAEgiE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 103 NLSLALRR--GLKRGLKKGYTAEELEQFKALLTPL-----------------QLGLEErlDAEIGLLSGGQRQAVSLLMA 163
Cdd:PRK11147 93 EQAEYLKRyhDISHLVETDPSEKNLNELAKLQEQLdhhnlwqlenrinevlaQLGLDP--DAALSSLSGGWLRKAALGRA 170
|
170 180
....*....|....*....|.
gi 260158848 164 TLRTPELLLLDEHTAALDPKT 184
Cdd:PRK11147 171 LVSNPDVLLLDEPTNHLDIET 191
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
26-191 |
3.57e-08 |
|
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: 52.11 E-value: 3.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 26 INLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYM-GEAAVEHTAEYERA-KYISrvYQNPLQGTaprMTVAQN 103
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLnGGPLDFQRDSIARGlLYLG--HAPGIKTT---LSVLEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 104 LslalrrglkRGLKKGYTAEELEQFKAlltplQLGLEERLDAEIGLLSGGQRQAVSLLMATLRTPELLLLDEHTAALDPK 183
Cdd:cd03231 94 L---------RFWHADHSDEQVEEALA-----RVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
....*...
gi 260158848 184 TQRKIMQL 191
Cdd:cd03231 160 GVARFAEA 167
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
33-190 |
4.20e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 53.73 E-value: 4.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 33 GDFITIVGGNGAGKSTFLNAISGSFpldKGHIYMGEAAVEHTAEYERA-KYISRVYQNPLqgTAPRMTVAQNLSLALRRG 111
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRI---QGNNFTGTILANNRKPTKQIlKRTGFVTQDDI--LYPHLTVRETLVFCSLLR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 112 LKRGLKKgytAEELEQFKALLTplQLGLEERLDAEIGL-----LSGGQRQAVSLLMATLRTPELLLLDEHTAALDPKTQR 186
Cdd:PLN03211 169 LPKSLTK---QEKILVAESVIS--ELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAY 243
|
....
gi 260158848 187 KIMQ 190
Cdd:PLN03211 244 RLVL 247
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
25-229 |
5.81e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.20 E-value: 5.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 25 DINLTIHKGDFITIVGGNGAGKST-------FLNAISGS---F--PLDKGHI-------YM-------GEaavehtaeye 78
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTtmkmltgLLPASEGEawlFgqPVDAGDIatrrrvgYMsqafslyGE---------- 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 79 rakyisrvyqnplqgtaprMTVAQNLSLALRR-GLKRGLKKGYTAEELEQFkalltplqlGLEERLDAEIGLLSGGQRQA 157
Cdd:NF033858 354 -------------------LTVRQNLELHARLfHLPAAEIAARVAEMLERF---------DLADVADALPDSLPLGIRQR 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 260158848 158 VSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYgNRLMMMHRGKII 229
Cdd:NF033858 406 LSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEAERC-DRISLMHAGRVL 476
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
23-210 |
6.88e-08 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 51.56 E-value: 6.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 23 LIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIY---MGEAAVEHTAEYERAKY-ISRVYQNPLQGTAprm 98
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnKNESEPSFEATRSRNRYsVAYAAQKPWLLNA--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 99 TVAQNLSLAlrrglkrglkkgyTAEELEQFKALLTPLQLGLEERL-----DAEIGL----LSGGQRQAVSLLMATLRTPE 169
Cdd:cd03290 94 TVEENITFG-------------SPFNKQRYKAVTDACSLQPDIDLlpfgdQTEIGErginLSGGQRQRICVARALYQNTN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 260158848 170 LLLLDEHTAALDPKTQRKIMQL-TKEIIEEKELTALMITHNL 210
Cdd:cd03290 161 IVFLDDPFSALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKL 202
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
26-228 |
7.02e-08 |
|
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: 53.03 E-value: 7.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 26 INLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYM-GEAAvehtaeyerakYIsrvyqnplqgtaPRMTVAQNL 104
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMkGSVA-----------YV------------PQQAWIQND 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 105 SLALRRGLKRGLKKGYTAEELEQFkALLTPLQLgLEERLDAEIGL----LSGGQRQAVSLLMATLRTPELLLLDEHTAAL 180
Cdd:TIGR00957 714 SLRENILFGKALNEKYYQQVLEAC-ALLPDLEI-LPSGDRTEIGEkgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAV 791
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 260158848 181 DPKTQRKIMQltkEIIEEKEL----TALMITHNLSdALRYGNRLMMMHRGKI 228
Cdd:TIGR00957 792 DAHVGKHIFE---HVIGPEGVlknkTRILVTHGIS-YLPQVDVIIVMSGGKI 839
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
3-254 |
7.86e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.06 E-value: 7.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHktFYPNTNRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPldkghiYMGEAAVEHTAEYERAKY 82
Cdd:PLN03232 615 ISIKNGY--FSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELS------HAETSSVVIRGSVAYVPQ 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 83 ISRVYQnplqgtaprMTVAQNLSLalrrglkrglkkGYTAEELEQFKAL-LTPLQLGLE---ERLDAEIGL----LSGGQ 154
Cdd:PLN03232 687 VSWIFN---------ATVRENILF------------GSDFESERYWRAIdVTALQHDLDllpGRDLTEIGErgvnISGGQ 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 155 RQAVSLLMATLRTPELLLLDEHTAALDPKTQRKIM-QLTKEIIEEKelTALMITHNLSdALRYGNRLMMMHRGKIIQ--V 231
Cdd:PLN03232 746 KQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFdSCMKDELKGK--TRVLVTNQLH-FLPLMDRIILVSEGMIKEegT 822
|
250 260
....*....|....*....|...
gi 260158848 232 FEKEEKEALTEEKLYQLMAELDE 254
Cdd:PLN03232 823 FAELSKSGSLFKKLMENAGKMDA 845
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
26-236 |
9.59e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 52.11 E-value: 9.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 26 INLTIHKGDFITIVGGNGAGKSTFLNAISG----SFPLDKGHIYMGEAAVEHTAEYERAKYI----SRVYQNPLQGTAPR 97
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAICGvtkdNWRVTADRMRFDDIDLLRLSPRERRKLVghnvSMIFQEPQSCLDPS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 98 MTVAQNLSLALRRGLKRGlkKGYTAEELEQFKALLTPLQLGLEERLDAEIGL---LSGGQRQAVSLLMATLRTPELLLLD 174
Cdd:PRK15093 106 ERVGRQLMQNIPGWTYKG--RWWQRFGWRKRRAIELLHRVGIKDHKDAMRSFpyeLTEGECQKVMIAIALANQPRLLIAD 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 260158848 175 EHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRGKIIQVFEKEE 236
Cdd:PRK15093 184 EPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKE 245
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
30-182 |
1.25e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 51.00 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 30 IHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIymgEAAVEHTAEYERAKYISrvYQNPLQGTAPRMTVAQNLSLAlr 109
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQI---QIDGKTATRGDRSRFMA--YLGHLPGLKADLSTLENLHFL-- 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 260158848 110 RGLkrglkKGYTAEELEQfKALLTplqLGLEERLDAEIGLLSGGQRQAVSLLMATLRTPELLLLDEHTAALDP 182
Cdd:PRK13543 107 CGL-----HGRRAKQMPG-SALAI---VGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-208 |
2.45e-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: 51.09 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFypntnrSHDALI-DINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVehtaeyerak 81
Cdd:TIGR03719 323 IEAENLTKAF------GDKLLIdDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVK---------- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 82 yISRVYQNPlQGTAPRMTVAQNLSLA---LRRGLKRGLKKGYTAeeLEQFKAlltplqlGLEERLdaeIGLLSGGQRQAV 158
Cdd:TIGR03719 387 -LAYVDQSR-DALDPNKTVWEEISGGldiIKLGKREIPSRAYVG--RFNFKG-------SDQQKK---VGQLSGGERNRV 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 260158848 159 SLLMaTLRTP-ELLLLDEHTAALDPKTQRKImqltKEIIEEKELTALMITH 208
Cdd:TIGR03719 453 HLAK-TLKSGgNVLLLDEPTNDLDVETLRAL----EEALLNFAGCAVVISH 498
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
23-181 |
2.70e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.89 E-value: 2.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 23 LIDINLTIHKGDFITIVGGNGAGKSTFLNAISGsfpLDKghIYMGEAAVehtaeyerAKYISRVY--QNPLQGtaPRMTV 100
Cdd:PRK11819 23 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG---VDK--EFEGEARP--------APGIKVGYlpQEPQLD--PEKTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 101 AQNLSLALrrGLKRGLKKGYT------AEELEQFKALLTPlQLGLEERL------------------------DAEIGLL 150
Cdd:PRK11819 88 RENVEEGV--AEVKAALDRFNeiyaayAEPDADFDALAAE-QGELQEIIdaadawdldsqleiamdalrcppwDAKVTKL 164
|
170 180 190
....*....|....*....|....*....|.
gi 260158848 151 SGGQRQAVSLLMATLRTPELLLLDEHTAALD 181
Cdd:PRK11819 165 SGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
27-191 |
3.90e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.40 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 27 NLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKYISRVYQ-NPLQGTAPR-----MTV 100
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDEWQrNNTDMLSPGeddtgRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 101 AQNLSLalrrglkrGLKKGYTAEELEQfkalltplQLGLEERLDAEIGLLSGGQRQAVSLLMATLRTPELLLLDEHTAAL 180
Cdd:PRK10938 103 AEIIQD--------EVKDPARCEQLAQ--------QFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGL 166
|
170
....*....|.
gi 260158848 181 DPKTQRKIMQL 191
Cdd:PRK10938 167 DVASRQQLAEL 177
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
2-231 |
4.32e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 49.19 E-value: 4.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 2 DIRIENVHKTFYPNTNRSHDALI------------------DINLTIHKGDFITIVGGNGAGKSTFLNAISGsfpLDKGH 63
Cdd:COG2401 7 FFVLMRVTKVYSSVLDLSERVAIvleafgvelrvveryvlrDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG---ALKGT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 64 IYMGEAAVEHTAEYERAKYISRVYQNPLQGTAPRMTVAQNLS---LALRRglkrglkkgytaeeleqFKALltplqlgle 140
Cdd:COG2401 84 PVAGCVDVPDNQFGREASLIDAIGRKGDFKDAVELLNAVGLSdavLWLRR-----------------FKEL--------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 141 erldaeigllSGGQRQAVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITH--NLSDALRyGN 218
Cdd:COG2401 138 ----------STGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHhyDVIDDLQ-PD 206
|
250
....*....|...
gi 260158848 219 RLMMMHRGKIIQV 231
Cdd:COG2401 207 LLIFVGYGGVPEE 219
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-211 |
5.10e-07 |
|
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: 49.29 E-value: 5.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 33 GDFITIVGGNGAGKSTFLNAISGSFPLDKGHiYMGEAAVEHTAEYERAKYISRVYQNPLQGTAPRMTVAQNLSL---ALR 109
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGK-FDDPPDWDEILDEFRGSELQNYFTKLLEGDVKVIVKPQYVDLipkAVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 110 RGLKRGLKKgytAEELEQFKALLTplQLGLEERLDAEIGLLSGGQRQAVSLLMATLRTPELLLLDEHTAALDPKTQRKIM 189
Cdd:cd03236 105 GKVGELLKK---KDERGKLDELVD--QLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAA 179
|
170 180
....*....|....*....|..
gi 260158848 190 QLTKEIIEEKElTALMITHNLS 211
Cdd:cd03236 180 RLIRELAEDDN-YVLVVEHDLA 200
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-249 |
6.31e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 50.00 E-value: 6.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVHKTFyPNTNrshdALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHI-YMGEAAVEHTAEYERAK 81
Cdd:PRK10762 5 LQLKGIDKAF-PGVK----ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSIlYLGKEVTFNGPKSSQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 82 YISRVYQ--NPLqgtaPRMTVAQNLSLAlrRGLKRGL-----KKGYtaeelEQFKALLTplQLGLEERLDAEIGLLSGGQ 154
Cdd:PRK10762 80 GIGIIHQelNLI----PQLTIAENIFLG--REFVNRFgridwKKMY-----AEADKLLA--RLNLRFSSDKLVGELSIGE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 155 RQAVSLLMATLRTPELLLLDEHTAALdpkTQRKIMQLTKEIieeKELTA-----LMITHNLSDALRYGNRLMMMHRGKII 229
Cdd:PRK10762 147 QQMVEIAKVLSFESKVIIMDEPTDAL---TDTETESLFRVI---RELKSqgrgiVYISHRLKEIFEICDDVTVFRDGQFI 220
|
250 260
....*....|....*....|
gi 260158848 230 QvfEKEEKEaLTEEKLYQLM 249
Cdd:PRK10762 221 A--EREVAD-LTEDSLIEMM 237
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
16-228 |
9.43e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 49.28 E-value: 9.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 16 TNRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKyISRVY------QN 89
Cdd:PRK15439 272 EDLTGEGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLA-RGLVYlpedrqSS 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 90 PLQGTAPrmtVAQNLSLALRRGLKRGLKKGYTAEELEQFKAlltplQLGLE-ERLDAEIGLLSGGQRQAVSLLMATLRTP 168
Cdd:PRK15439 351 GLYLDAP---LAWNVCALTHNRRGFWIKPARENAVLERYRR-----ALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASP 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 169 ELLLLDEHTAALDPKTQRKIMQLTKEIIEEkELTALMITHNLSDALRYGNRLMMMHRGKI 228
Cdd:PRK15439 423 QLLIVDEPTRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
23-226 |
1.51e-06 |
|
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: 49.14 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 23 LIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIymgeaavehtaeyeraKYISRVYQNPLQGTAPRMTVAQ 102
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI----------------KHSGRISFSPQTSWIMPGTIKD 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 103 NLSLALRRGLKRglkkgYT----AEELEQFKALL-----TPLQLGleerldaeiGL-LSGGQRQAVSLLMATLRTPELLL 172
Cdd:TIGR01271 506 NIIFGLSYDEYR-----YTsvikACQLEEDIALFpekdkTVLGEG---------GItLSGGQRARISLARAVYKDADLYL 571
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 260158848 173 LDEHTAALDPKTQRKIMQ--LTKEIIEEkelTALMITHNLsDALRYGNRLMMMHRG 226
Cdd:TIGR01271 572 LDSPFTHLDVVTEKEIFEscLCKLMSNK---TRILVTSKL-EHLKKADKILLLHEG 623
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
151-229 |
1.71e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 48.19 E-value: 1.71e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 260158848 151 SGGQRQAVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKElTALMITHNLSDALRYGNRLMMMHRGKII 229
Cdd:NF000106 146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGA-TVLLTTQYMEEAEQLAHELTVIDRGRVI 223
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-210 |
1.80e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 48.65 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 29 TIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGhIYMGEAAVEHTAEYERAK----YISRVYQNplqgtapRMTVAQN- 103
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNLG-DYEEEPSWDEVLKRFRGTelqnYFKKLYNG-------EIKVVHKp 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 104 -----LSLALRRGLKRGLKKgytAEELEQFKALLTplQLGLEERLDAEIGLLSGGQRQAVSLLMATLRTPELLLLDEHTA 178
Cdd:PRK13409 167 qyvdlIPKVFKGKVRELLKK---VDERGKLDEVVE--RLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTS 241
|
170 180 190
....*....|....*....|....*....|...
gi 260158848 179 ALDPKtQR-KIMQLTKEIIEEKelTALMITHNL 210
Cdd:PRK13409 242 YLDIR-QRlNVARLIRELAEGK--YVLVVEHDL 271
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
22-229 |
1.98e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 48.58 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 22 ALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIY-----MGEAAvehtaeyERAKYISRVYQNPlQGTA- 95
Cdd:NF033858 16 ALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvlggdMADAR-------HRRAVCPRIAYMP-QGLGk 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 96 ---PRMTVAQNLSLALR-RGLKRglkkgytAEELEQFKALLTplQLGLEERLDAEIGLLSGGQRQAVSLLMATLRTPELL 171
Cdd:NF033858 88 nlyPTLSVFENLDFFGRlFGQDA-------AERRRRIDELLR--ATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 260158848 172 LLDEHTAALDPKTQRKIMQLTKEIIEEKE-LTALMITHNLSDALRYgNRLMMMHRGKII 229
Cdd:NF033858 159 ILDEPTTGVDPLSRRQFWELIDRIRAERPgMSVLVATAYMEEAERF-DWLVAMDAGRVL 216
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
23-226 |
2.56e-06 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 47.54 E-value: 2.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 23 LIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIymgeaavEHTAeyerakyisrvyqnplqgtapRMTVAQ 102
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI-------KHSG---------------------RISFSS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 103 NLSLALRRGLKRGLKKGYTAEELeQFKALLTPLQlgLEERLD----------AEIGL-LSGGQRQAVSLLMATLRTPELL 171
Cdd:cd03291 105 QFSWIMPGTIKENIIFGVSYDEY-RYKSVVKACQ--LEEDITkfpekdntvlGEGGItLSGGQRARISLARAVYKDADLY 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 260158848 172 LLDEHTAALDPKTQRKIMQ-LTKEIIEEKelTALMITHNLsDALRYGNRLMMMHRG 226
Cdd:cd03291 182 LLDSPFGYLDVFTEKEIFEsCVCKLMANK--TRILVTSKM-EHLKKADKILILHEG 234
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
33-234 |
3.22e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.18 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 33 GDFITIVGGNGAGKSTFLNAISGSfpLDKGHIYMGEAAV---EHTAEYERAkyISRVYQNPLQgtAPRMTVAQNL--SLA 107
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLAER--VTTGVITGGDRLVngrPLDSSFQRS--IGYVQQQDLH--LPTSTVRESLrfSAY 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 108 LRRglkrglKKGYTAEELEQFKALLTPLqLGLEERLDAEIGL----LSGGQRQAVSLLMATLRTPELLL-LDEHTAALDP 182
Cdd:TIGR00956 863 LRQ------PKSVSKSEKMEYVEEVIKL-LEMESYADAVVGVpgegLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDS 935
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 260158848 183 KTQRKIMQLTKEIIEEKElTALMITHNLS-DALRYGNRLMMMHRG--------------KIIQVFEK 234
Cdd:TIGR00956 936 QTAWSICKLMRKLADHGQ-AILCTIHQPSaILFEEFDRLLLLQKGgqtvyfgdlgenshTIINYFEK 1001
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
150-235 |
3.35e-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: 46.41 E-value: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 150 LSGGQRQAVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLsdalrygnrLMMMHRGKII 229
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDL---------AVLDYLSDRI 142
|
....*.
gi 260158848 230 QVFEKE 235
Cdd:cd03222 143 HVFEGE 148
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
147-250 |
3.84e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.42 E-value: 3.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 147 IGLLSGGQRQAVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEiIEEKELTALMITHNLSDALRYGNRLMMMHRG 226
Cdd:PRK10982 389 IGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAE-LAKKDKGIIIISSEMPELLGITDRILVMSNG 467
|
90 100
....*....|....*....|....
gi 260158848 227 KIIQVFEKEEKealTEEKLYQLMA 250
Cdd:PRK10982 468 LVAGIVDTKTT---TQNEILRLAS 488
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-248 |
4.10e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.58 E-value: 4.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 20 HDALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYM-GEAAVehtaeyeraKYISRVYQNPLQGTaprm 98
Cdd:PRK13545 37 HYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIkGSAAL---------IAISSGLNGQLTGI---- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 99 tvaQNLSLalrrglkRGLKKGYTAEELEQfkalLTPLQLGLeerldAEIGLL--------SGGQRQAVSLLMATLRTPEL 170
Cdd:PRK13545 104 ---ENIEL-------KGLMMGLTKEKIKE----IIPEIIEF-----ADIGKFiyqpvktySSGMKSRLGFAISVHINPDI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 171 LLLDEHTAALDPKTQRKIMQLTKEiIEEKELTALMITHNLSDALRYGNRLMMMHRGKIIQV------------------- 231
Cdd:PRK13545 165 LVIDEALSVGDQTFTKKCLDKMNE-FKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYgdikevvdhydeflkkynq 243
|
250
....*....|....*..
gi 260158848 232 FEKEEKEALTEEKLYQL 248
Cdd:PRK13545 244 MSVEERKDFREEQISQF 260
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
25-208 |
4.57e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 47.25 E-value: 4.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 25 DINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMG---EAAV--EHTAEYErakyisrvyqnplqgtaPRMT 99
Cdd:PRK11147 337 DFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGtklEVAYfdQHRAELD-----------------PEKT 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 100 VAQNLSLALRRGLKRGLKK---GYTAEELEQFKALLTPLQlgleerldaeigLLSGGQRQavSLLMAT--LRTPELLLLD 174
Cdd:PRK11147 400 VMDNLAEGKQEVMVNGRPRhvlGYLQDFLFHPKRAMTPVK------------ALSGGERN--RLLLARlfLKPSNLLILD 465
|
170 180 190
....*....|....*....|....*....|....
gi 260158848 175 EHTAALDPKTqrkiMQLTKEIIEEKELTALMITH 208
Cdd:PRK11147 466 EPTNDLDVET----LELLEELLDSYQGTVLLVSH 495
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
25-208 |
1.13e-05 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 45.76 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 25 DINLTIHKgDFITIVGGNGAGKSTFLNAI------SGSFPLDKGHIYMGE--AAVEHTAEYERAKYISRVYQNPLQGTAP 96
Cdd:COG3593 16 DLSIELSD-DLTVLVGENNSGKSSILEALrlllgpSSSRKFDEEDFYLGDdpDLPEIEIELTFGSLLSRLLRLLLKEEDK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 97 rmtvaQNLSLALRRgLKRGLKKGYTA--EELEQF-------------------KALLTPLQLGLEERLDAEIGLLSGGQR 155
Cdd:COG3593 95 -----EELEEALEE-LNEELKEALKAlnELLSEYlkelldgldlelelsldelEDLLKSLSLRIEDGKELPLDRLGSGFQ 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 156 QAVSLLMATL-------RTPELLLLDEHTAALDPKTQRKIMQLTKEIIEEKeLTALMITH 208
Cdd:COG3593 169 RLILLALLSAlaelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKP-NQVIITTH 227
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
23-251 |
1.23e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 46.27 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 23 LIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGhiymGEAAVEHTAEY-ERAKYI--SRVYQNPLQGT---AP 96
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSD----ASVVIRGTVAYvPQVSWIfnATVRDNILFGSpfdPE 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 97 RMTVAQNLSlALRRGLkrglkkgytaeeleqfkALLTPLQLgleerldAEIGL----LSGGQRQAVSLLMATLRTPELLL 172
Cdd:PLN03130 709 RYERAIDVT-ALQHDL-----------------DLLPGGDL-------TEIGErgvnISGGQKQRVSMARAVYSNSDVYI 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 173 LDEHTAALDPKTQRKIMQltKEIIEE-KELTALMITHNLSdALRYGNRLMMMHRGKIiqvfeKEE---KEALTEEKLYQL 248
Cdd:PLN03130 764 FDDPLSALDAHVGRQVFD--KCIKDElRGKTRVLVTNQLH-FLSQVDRIILVHEGMI-----KEEgtyEELSNNGPLFQK 835
|
...
gi 260158848 249 MAE 251
Cdd:PLN03130 836 LME 838
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
26-248 |
2.31e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 45.29 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 26 INLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYM-GEA-AVEHTAEYERAKYISRVYQNPLQGTAPRMTVAQN 103
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLdGKPiDIRSPRDAIRAGIMLCPEDRKAEGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 104 LSLALRRGLKRG---LKKGYTAEELEQFKALL---TPlqlgleeRLDAEIGLLSGGQRQAVSL---LMATLRtpeLLLLD 174
Cdd:PRK11288 352 INISARRHHLRAgclINNRWEAENADRFIRSLnikTP-------SREQLIMNLSGGNQQKAILgrwLSEDMK---VILLD 421
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 260158848 175 EHTAALDPKTQRKIMQLTKEIIEEKeLTALMITHNLSDALRYGNRLMMMHRGKIIQVFEKEEKealTEEKLYQL 248
Cdd:PRK11288 422 EPTRGIDVGAKHEIYNVIYELAAQG-VAVLFVSSDLPEVLGVADRIVVMREGRIAGELAREQA---TERQALSL 491
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
3-195 |
2.78e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 43.85 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 3 IRIENVhktfypntnRSHDALIDINLTihkGDFITIVGGNGAGKSTFLNAI----------SGSFPLDKGHIYMGEAAVE 72
Cdd:COG0419 5 LRLENF---------RSYRDTETIDFD---DGLNLIVGPNGAGKSTILEAIryalygkarsRSKLRSDLINVGSEEASVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 73 HTAEYERAKY-ISRvyqnpLQGTAPRMTVAQnlSLALRRGLKRGLKkgytAEELEQFKALLTPLQLGLEERLDA------ 145
Cdd:COG0419 73 LEFEHGGKRYrIER-----RQGEFAEFLEAK--PSERKEALKRLLG----LEIYEELKERLKELEEALESALEElaelqk 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 260158848 146 -------------EIGLLSGGQRQAVSLLMAtLRtpelLLLDehTAALDPKTQRKIMQLTKEI 195
Cdd:COG0419 142 lkqeilaqlsgldPIETLSGGERLRLALADL-LS----LILD--FGSLDEERLERLLDALEEL 197
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-210 |
4.72e-05 |
|
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: 44.39 E-value: 4.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 32 KGDFITIVGGNGAGKSTFLNAISGSF---------PLDKghiymgEAAVEHTAEYERAKYISRVYQNPLQGT-------- 94
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELkpnlgdydeEPSW------DEVLKRFRGTELQDYFKKLANGEIKVAhkpqyvdl 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 95 APRM---TVAQNLSLALRRGLKRGLKKgytaeeleqfkalltplQLGLEERLDAEIGLLSGGQRQAVSLLMATLRTPELL 171
Cdd:COG1245 172 IPKVfkgTVRELLEKVDERGKLDELAE-----------------KLGLENILDRDISELSGGELQRVAIAAALLRDADFY 234
|
170 180 190
....*....|....*....|....*....|....*....
gi 260158848 172 LLDEHTAALDPKTQRKIMQLTKEIIEEKElTALMITHNL 210
Cdd:COG1245 235 FFDEPSSYLDIYQRLNVARLIRELAEEGK-YVLVVEHDL 272
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-68 |
5.24e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 43.95 E-value: 5.24e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 260158848 3 IRIENVHKTFYPNTnrshdaLID-INLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGE 68
Cdd:PRK11819 325 IEAENLSKSFGDRL------LIDdLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGE 385
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
26-254 |
6.36e-05 |
|
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: 43.36 E-value: 6.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 26 INLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKYISRVYQNPLqgtaprmTVAQNLS 105
Cdd:cd03288 40 VKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPI-------LFSGSIR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 106 LALRRGLKRGLKKGYTAEELEQFKALLTPLQLGLEERLDAEIGLLSGGQRQAVSLLMATLRTPELLLLDEHTAALDPKTQ 185
Cdd:cd03288 113 FNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 260158848 186 RKIMQLTKEIIEEKelTALMITHNLSDALRyGNRLMMMHRGKIIQvFEKEEKEALTEEKLYQLMAELDE 254
Cdd:cd03288 193 NILQKVVMTAFADR--TVVTIAHRVSTILD-ADLVLVLSRGILVE-CDTPENLLAQEDGVFASLVRTDK 257
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
25-78 |
7.66e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 43.73 E-value: 7.66e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 25 DINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAV------EHTAEYE 78
Cdd:PRK15064 337 NLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANigyyaqDHAYDFE 396
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
5-249 |
7.86e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.56 E-value: 7.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 5 IENVHKTFyPNTNrshdALIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSFPLDKGHI-YMGEAAVEHTAEYERAKYI 83
Cdd:PRK10982 1 MSNISKSF-PGVK----ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSIlFQGKEIDFKSSKEALENGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 84 SRVYQNpLQGTAPRmTVAQNLSLAlrrglkRGLKKGYTAEELEQF---KALLTPLQLGLEERldAEIGLLSGGQRQAVSL 160
Cdd:PRK10982 76 SMVHQE-LNLVLQR-SVMDNMWLG------RYPTKGMFVDQDKMYrdtKAIFDELDIDIDPR--AKVATLSVSQMQMIEI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 161 LMATLRTPELLLLDEHTAALdpkTQRKIMQLTKEI--IEEKELTALMITHNLSDALRYGNRLMMMHRGKIIQVfekEEKE 238
Cdd:PRK10982 146 AKAFSYNAKIVIMDEPTSSL---TEKEVNHLFTIIrkLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIAT---QPLA 219
|
250
....*....|.
gi 260158848 239 ALTEEKLYQLM 249
Cdd:PRK10982 220 GLTMDKIIAMM 230
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
19-211 |
8.50e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 41.92 E-value: 8.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 19 SHDALIDINLTIHKGDFITIVGGNGAGKSTFLNAIsgsfpldkghiymgeaaVEHTAEYERAKYISRVYQNPLqgtaprM 98
Cdd:cd03238 7 NVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG-----------------LYASGKARLISFLPKFSRNKL------I 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 99 TVAQnlslaLRRGLKRGLkkGYTaeeleqfkalltplqlgleeRLDAEIGLLSGGQRQAVSLL--MATLRTPELLLLDEH 176
Cdd:cd03238 64 FIDQ-----LQFLIDVGL--GYL--------------------TLGQKLSTLSGGELQRVKLAseLFSEPPGTLFILDEP 116
|
170 180 190
....*....|....*....|....*....|....*
gi 260158848 177 TAALDPKTQRKIMQLTKEIIEEKElTALMITHNLS 211
Cdd:cd03238 117 STGLHQQDINQLLEVIKGLIDLGN-TVILIEHNLD 150
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
4-211 |
1.06e-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: 42.76 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 4 RIENVHKTFYPNTNRSHDALIDINLTIHKGDFITIVGGNGAGKSTFLNA----ISGSFPLDKGHIYMGEAAVEHTAEYER 79
Cdd:pfam13304 86 KLSSKPTLLEKRLLLREDSEEREPKFPPEAEELRLGLDVEERIELSLSElsdlISGLLLLSIISPLSFLLLLDEGLLLED 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 80 AKYISRVyqNPLQGTAPRMTVAQNLSLALRRGLKRGLKKGYTAEE-LEQFKALLTPLQLGLEERLDAEI--GLLSGGQRQ 156
Cdd:pfam13304 166 WAVLDLA--ADLALFPDLKELLQRLVRGLKLADLNLSDLGEGIEKsLLVDDRLRERGLILLENGGGGELpaFELSDGTKR 243
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 260158848 157 A---VSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEiIEEKELTALMITHNLS 211
Cdd:pfam13304 244 LlalLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKE-LSRNGAQLILTTHSPL 300
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
23-181 |
1.46e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.85 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 23 LIDINLTIHKGDFITIVGGNGAGKSTF-------LNAISGSFPLDKGhIYMGEAAvEHTAEYERAKyisrvyQNPLQG-- 93
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLikllageLAPVSGEIGLAKG-IKLGYFA-QHQLEFLRAD------ESPLQHla 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 94 -TAPRMTVAQnlslaLRRGLKR-GLKKGYTAEELEQFkalltplqlgleerldaeigllSGGQRQAVSLLMATLRTPELL 171
Cdd:PRK10636 400 rLAPQELEQK-----LRDYLGGfGFQGDKVTEETRRF----------------------SGGEKARLVLALIVWQRPNLL 452
|
170
....*....|
gi 260158848 172 LLDEHTAALD 181
Cdd:PRK10636 453 LLDEPTNHLD 462
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
138-194 |
1.68e-04 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 39.53 E-value: 1.68e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 138 GLEERLDAEIGLLSGGQRQ---AVSLLMA----------TLRTPELLLLDEHTAALDPKTQRKIMQLTKE 194
Cdd:pfam13558 21 GSEVETYRRSGGLSGGEKQllaYLPLAAAlaaqygsaegRPPAPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
23-210 |
1.96e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 40.81 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 23 LIDINLTIHKGDFITIVGGNGAGKSTFLNAIsgsfpldkGHIYMGEAAVEHTAEYERAKYISrvyqnplqgtaprmtvaq 102
Cdd:cd03227 11 FVPNDVTFGEGSLTIITGPNGSGKSTILDAI--------GLALGGAQSATRRRSGVKAGCIV------------------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 103 nlslalrrglkrglkkgyTAEELEqfkALLTPLQLgleerldaeigllSGGQRQAVSL-----LMATLRTPeLLLLDEHT 177
Cdd:cd03227 65 ------------------AAVSAE---LIFTRLQL-------------SGGEKELSALalilaLASLKPRP-LYILDEID 109
|
170 180 190
....*....|....*....|....*....|...
gi 260158848 178 AALDPKTQRKIMQLTKEIIEEKeLTALMITHNL 210
Cdd:cd03227 110 RGLDPRDGQALAEAILEHLVKG-AQVIVITHLP 141
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
147-231 |
4.42e-04 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 40.14 E-value: 4.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 147 IGLLSGGQRQ--AVSLLMATLRT---PeLLLLDEHTAALDPKTQRKIMQLTKEIIEEKELtaLMITHnlsdalrygNRLM 221
Cdd:cd03278 111 LSLLSGGEKAltALALLFAIFRVrpsP-FCVLDEVDAALDDANVERFARLLKEFSKETQF--IVITH---------RKGT 178
|
90
....*....|
gi 260158848 222 MMHRGKIIQV 231
Cdd:cd03278 179 MEAADRLYGV 188
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
38-194 |
1.30e-03 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 38.83 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 38 IVGGNGAGKSTFLNAISgsFPLDkghiymgeaavehtaeyERAKYISRvyqnplqgtaprmtvAQNLSLAlRRGLKRGLK 117
Cdd:cd03239 27 IVGPNGSGKSNIVDAIC--FVLG-----------------GKAAKLRR---------------GSLLFLA-GGGVKAGIN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 118 KGYTAEELEQFKALLtplqlgLEERLDAeigLLSGGQRQ--AVSLLMATL---RTPeLLLLDEHTAALDPKTQRKIMQLT 192
Cdd:cd03239 72 SASVEITFDKSYFLV------LQGKVEQ---ILSGGEKSlsALALIFALQeikPSP-FYVLDEIDAALDPTNRRRVSDMI 141
|
..
gi 260158848 193 KE 194
Cdd:cd03239 142 KE 143
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
23-233 |
2.26e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 39.44 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 23 LIDINLTIHKGDFITIVGGNGAGKSTFLNAISGSfpLDKGHIymgEAAVEHTAEYERAKYISRVY----QNPLQgtAPRM 98
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGR--KTGGYI---EGDIRISGFPKKQETFARISgyceQNDIH--SPQV 968
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 99 TVAQNL--SLALRrglkrgLKKGYTAEELEQFKALLTPLqLGLEERLDAEIGL-----LSGGQRQAVSLLMATLRTPELL 171
Cdd:PLN03140 969 TVRESLiySAFLR------LPKEVSKEEKMMFVDEVMEL-VELDNLKDAIVGLpgvtgLSTEQRKRLTIAVELVANPSII 1041
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 260158848 172 LLDEHTAALDPKTQRKIMQLTKEIIEEKELTALMITHNLSDALRYGNRLMMMHRG--------------KIIQVFE 233
Cdd:PLN03140 1042 FMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMKRGgqviysgplgrnshKIIEYFE 1117
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
25-195 |
2.56e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 38.44 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 25 DINLTIHKGDFIT-IVGGNGAGKSTFLNAIS---GSFPLDKGHIYMGEAAVEHTAEYERAKYIS------RVYQNPLQGT 94
Cdd:COG3950 16 DLEIDFDNPPRLTvLVGENGSGKTTLLEAIAlalSGLLSRLDDVKFRKLLIRNGEFGDSAKLILyygtsrLLLDGPLKKL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 95 APRMTVAQNLSLALRRGLKRG----------------LKKGYTAEELEQFKAL-----------------LTPLQLGLEE 141
Cdd:COG3950 96 ERLKEEYFSRLDGYDSLLDEDsnlreflewlreyledLENKLSDELDEKLEAVrealnkllpdfkdiridRDPGRLVILD 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 260158848 142 RLDAEIGL--LSGGQRQAVSLLM--------------ATLRTPELLLLDE---HtaaLDPKTQRKIMQLTKEI 195
Cdd:COG3950 176 KNGEELPLnqLSDGERSLLALVGdlarrlaelnpaleNPLEGEGIVLIDEidlH---LHPKWQRRILPDLRKI 245
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-112 |
3.57e-03 |
|
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: 36.97 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 32 KGDFITIVGGNGAGKSTFLNAISGSFPLDKGHIYMGEAAVEHTAEYERAKYISRVYQNPLQGTAPRMTVAQNLSLALRRG 111
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPD 80
|
.
gi 260158848 112 L 112
Cdd:smart00382 81 V 81
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
149-230 |
9.11e-03 |
|
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: 36.76 E-value: 9.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260158848 149 LLSGGQRQAVSLLMATLRTPELLLLDEHTAALDPKTQRKIMQLTKEIIeeKELTALMITHNLsDALRYGNRLMMMHRGKI 228
Cdd:cd03289 138 VLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAF--ADCTVILSEHRI-EAMLECQRFLVIEENKV 214
|
..
gi 260158848 229 IQ 230
Cdd:cd03289 215 RQ 216
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