|
Name |
Accession |
Description |
Interval |
E-value |
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
9-249 |
3.31e-144 |
|
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: 403.98 E-value: 3.31e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 9 STQSLIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELFAA 88
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 89 RARMGMLFQSGALFTDMSVYENVAFPIRAHTKLSENLIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDP 168
Cdd:COG1127 81 RRRIGMLFQGGALFDSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 169 DLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELQAYASPFVKQF 248
Cdd:COG1127 161 EILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASDDPWVRQF 240
|
.
7D06_B 249 L 249
Cdd:COG1127 241 L 241
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
14-248 |
2.73e-141 |
|
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: 396.49 E-value: 2.73e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELFAARARMG 93
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 94 MLFQSGALFTDMSVYENVAFPIRAHTKLSENLIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPDLIMY 173
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
7D06_B 174 DEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELQAYASPFVKQF 248
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASDDPLVRQF 235
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
9-268 |
5.94e-137 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 386.81 E-value: 5.94e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 9 STQSLIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELFAA 88
Cdd:PRK11831 3 SVANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 89 RARMGMLFQSGALFTDMSVYENVAFPIRAHTKLSENLIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDP 168
Cdd:PRK11831 83 RKRMSMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 169 DLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELQAYASPFVKQF 248
Cdd:PRK11831 163 DLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPRVRQF 242
|
250 260
....*....|....*....|
7D06_B 249 LTGSAEGPVEYQFSHQAYLD 268
Cdd:PRK11831 243 LDGIADGPVPFRYPAGDYHA 262
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
10-249 |
4.14e-74 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 229.98 E-value: 4.14e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 10 TQSLIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSrqelfAAR 89
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLP-----PEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 90 ARMGMLFQSGALFTDMSVYENVAFPIRAHtKLSENLIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPD 169
Cdd:COG3842 77 RNVGMVFQDYALFPHLTVAENVAFGLRMR-GVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 170 LIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELqaY---ASPFVK 246
Cdd:COG3842 156 VLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEI--YerpATRFVA 233
|
...
7D06_B 247 QFL 249
Cdd:COG3842 234 DFI 236
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
14-229 |
8.14e-72 |
|
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: 219.31 E-value: 8.14e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSrqelfAARARMG 93
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVP-----PERRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 94 MLFQSGALFTDMSVYENVAFPIRAHtKLSENLIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPDLIMY 173
Cdd:cd03259 76 MVFQDYALFPHLTVAENIAFGLKLR-GVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
7D06_B 174 DEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQ 229
Cdd:cd03259 155 DEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
14-249 |
5.72e-68 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 214.24 E-value: 5.72e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDiaqmsrqeLFAARA--- 90
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRD--------LFTNLPpre 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 91 -RMGMLFQSGALFTDMSVYENVAFPIRaHTKLSENLIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPD 169
Cdd:COG1118 75 rRVGFVFQHYALFPHMTVAENIAFGLR-VRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 170 LIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELQAY-ASPFVKQF 248
Cdd:COG1118 154 VLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRpATPFVARF 233
|
.
7D06_B 249 L 249
Cdd:COG1118 234 L 234
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
14-249 |
1.11e-65 |
|
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: 204.88 E-value: 1.11e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQElfaarARMG 93
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE-----RNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 94 MLFQSGALFTDMSVYENVAFPIR---AHTKLSENLIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPDL 170
Cdd:cd03296 78 FVFQHYALFRHMTVFDNVAFGLRvkpRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 171 IMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEEL-QAYASPFVKQFL 249
Cdd:cd03296 158 LLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVyDHPASPFVYSFL 237
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-243 |
1.40e-65 |
|
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: 212.84 E-value: 1.40e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 5 KTPLSTQSLIEVKNLSF-----NRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQ 79
Cdd:COG1123 252 PAAAAAEPLLEVRNLSKrypvrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTK 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 80 MSRQELFAARARMGMLFQ--SGALFTDMSVYENVAFPIRAHTKLSENLIAELVALKLESVGL-RGTEQLMPTELSGGMNR 156
Cdd:COG1123 332 LSRRSLRELRRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQ 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 157 RVALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEE 236
Cdd:COG1123 412 RVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEE 491
|
....*..
7D06_B 237 LqaYASP 243
Cdd:COG1123 492 V--FANP 496
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
9-231 |
3.23e-65 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 204.17 E-value: 3.23e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 9 STQSLIEVKNLSF----NRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAqmsrqe 84
Cdd:COG1116 3 AAAPALELRGVSKrfptGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 85 lfAARARMGMLFQSGALFTDMSVYENVAFPIRAHtKLSENLIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAI 164
Cdd:COG1116 77 --GPGPDRGVVFQEPALLPWLTVLDNVALGLELR-GVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
7D06_B 165 ALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAE--GKIQGE 231
Cdd:COG1116 154 ANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVEE 222
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
14-249 |
1.37e-64 |
|
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: 201.70 E-value: 1.37e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQmsrqeLFAARARMG 93
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN-----LPPHKRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 94 MLFQSGALFTDMSVYENVAFPIRAhTKLSENLIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPDLIMY 173
Cdd:cd03300 76 TVFQNYALFPHLTVFENIAFGLRL-KKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
7D06_B 174 DEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELqaYASP---FVKQFL 249
Cdd:cd03300 155 DEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEI--YEEPanrFVADFI 231
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
14-237 |
3.27e-64 |
|
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: 200.48 E-value: 3.27e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGG-----QLVPDQGEVLLDGKDIAQMSRQELfAA 88
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKDIYDLDVDVL-EL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 89 RARMGMLFQSGALFtDMSVYENVAFPIRAHTKLSENLIAELVALKLESVGL--RGTEQLMPTELSGGMNRRVALARAIAL 166
Cdd:cd03260 80 RRRVGMVFQKPNPF-PGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALwdEVKDRLHALGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
7D06_B 167 DPDLIMYDEPFAGQDPIVKGVLTRLIRSLREalDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEEL 237
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKK--EYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
14-237 |
7.42e-64 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 199.87 E-value: 7.42e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFN-RGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELfaaRARM 92
Cdd:COG1122 1 IELENLSFSyPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLREL---RRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 93 GMLFQ-SGALFTDMSVYENVAFPIRaHTKLSENLIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPDLI 171
Cdd:COG1122 78 GLVFQnPDDQLFAPTVEEDVAFGPE-NLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
7D06_B 172 MYDEPFAGQDPIVKGVLTRLIRSLREAlDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEEL 237
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
14-231 |
4.71e-63 |
|
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: 197.31 E-value: 4.71e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSF----NRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQmsrqelfaAR 89
Cdd:cd03293 1 LEVRNVSKtyggGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG--------PG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 90 ARMGMLFQSGALFTDMSVYENVAFPIRAHtKLSENLIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPD 169
Cdd:cd03293 73 PDRGYVFQQDALLPWLTVLDNVALGLELQ-GVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
7D06_B 170 LIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAE--GKIQGE 231
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAE 215
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
31-251 |
2.69e-62 |
|
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: 197.10 E-value: 2.69e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 31 NISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELFAARA-RMGMLFQSGALFTDMSVYE 109
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRkKISMVFQSFALLPHRTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 110 NVAFPIR-AHTKLSENLIAELVALKLesVGLRGTEQLMPTELSGGMNRRVALARAIALDPDLIMYDEPFAGQDPIVKGVL 188
Cdd:cd03294 122 NVAFGLEvQGVPRAEREERAAEALEL--VGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREM 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
7D06_B 189 TRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEE-LQAYASPFVKQFLTG 251
Cdd:cd03294 200 QDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEiLTNPANDYVREFFRG 263
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
14-227 |
4.18e-62 |
|
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: 193.56 E-value: 4.18e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELfAARARMG 93
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELP-PLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 94 MLFQSGALFTDMSVYENVAFPirahtklsenliaelvalklesvglrgteqlmpteLSGGMNRRVALARAIALDPDLIMY 173
Cdd:cd03229 80 MVFQDFALFPHLTVLENIALG-----------------------------------LSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
7D06_B 174 DEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGK 227
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
14-228 |
6.18e-62 |
|
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: 194.25 E-value: 6.18e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLS--FNRG--ERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELFAAR 89
Cdd:cd03255 1 IELKNLSktYGGGgeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 90 AR-MGMLFQSGALFTDMSVYENVAFPIRAHTKLSENliAELVALK-LESVGLRGTEQLMPTELSGGMNRRVALARAIALD 167
Cdd:cd03255 81 RRhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKE--RRERAEElLERVGLGDRLNHYPSELSGGQQQRVAIARALAND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
7D06_B 168 PDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDvPETLSIADYIYVVAEGKI 228
Cdd:cd03255 159 PKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
14-252 |
4.86e-61 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 196.45 E-value: 4.86e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMsrqelfAARAR-M 92
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDL------PPKDRnI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 93 GMLFQSGALFTDMSVYENVAFPIRAHtKLSENLIAELVALKLESVGLrgTEQL--MPTELSGGMNRRVALARAIALDPDL 170
Cdd:COG3839 78 AMVFQSYALYPHMTVYENIAFPLKLR-KVPKAEIDRRVREAAELLGL--EDLLdrKPKQLSGGQRQRVALGRALVREPKV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 171 IMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELqaYASP---FVKQ 247
Cdd:COG3839 155 FLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEEL--YDRPanlFVAG 232
|
....*
7D06_B 248 FLtGS 252
Cdd:COG3839 233 FI-GS 236
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
14-239 |
9.41e-61 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 191.82 E-value: 9.41e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRqelfAARARMG 93
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPA----EVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 94 MLFQSGALFTDMSVYENVAFPIRAHtKLSENLIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPDLIMY 173
Cdd:COG1131 77 YVPQEPALYPDLTVRENLRFFARLY-GLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLIL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
7D06_B 174 DEPFAGQDPIVKGVLTRLIRSLREAlDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELQA 239
Cdd:COG1131 156 DEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKA 220
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
13-232 |
1.58e-60 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 191.18 E-value: 1.58e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 13 LIEVKNLS----FNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELFAA 88
Cdd:cd03257 1 LLEVKNLSvsfpTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 89 RARMGMLFQ--SGALFTDMSVYENVAFPIRAHTKLS-ENLIAELVALKLESVGLRgtEQLM---PTELSGGMNRRVALAR 162
Cdd:cd03257 81 RKEIQMVFQdpMSSLNPRMTIGEQIAEPLRIHGKLSkKEARKEAVLLLLVGVGLP--EEVLnryPHELSGGQRQRVAIAR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 163 AIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEG 232
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
10-239 |
5.58e-60 |
|
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: 190.63 E-value: 5.58e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 10 TQSLIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQElfaaR 89
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHR----I 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 90 ARMGML--FQSGALFTDMSVYENVAFPIRAHTKlsENLIAELVALK----------------LESVGLRGTEQLMPTELS 151
Cdd:COG0411 77 ARLGIArtFQNPRLFPELTVLENVLVAAHARLG--RGLLAALLRLPrarreereareraeelLERVGLADRADEPAGNLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 152 GGMNRRVALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGE 231
Cdd:COG0411 155 YGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAE 234
|
....*...
7D06_B 232 GTPEELQA 239
Cdd:COG0411 235 GTPAEVRA 242
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
11-231 |
2.25e-59 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 188.33 E-value: 2.25e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 11 QSLIEVKNLS--FNRGERVIY--DNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELF 86
Cdd:COG1136 2 SPLLELRNLTksYGTGEGEVTalRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 87 AARAR-MGMLFQSGALFTDMSVYENVAFPIR---AHTKLSENLIAELvalkLESVGLRGTEQLMPTELSGGMNRRVALAR 162
Cdd:COG1136 82 RLRRRhIGFVFQFFNLLPELTALENVALPLLlagVSRKERRERAREL----LERVGLGDRLDHRPSQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
7D06_B 163 AIALDPDLIMYDEPFA------GQDpivkgVLtRLIRSLREALDLTTIIVSHDvPETLSIADYIYVVAEGKIQGE 231
Cdd:COG1136 158 ALVNRPKLILADEPTGnldsktGEE-----VL-ELLRELNRELGTTIVMVTHD-PELAARADRVIRLRDGRIVSD 225
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
15-227 |
1.45e-58 |
|
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: 185.75 E-value: 1.45e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 15 EVKNLSF--NRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELfaaRARM 92
Cdd:cd03225 1 ELKNLSFsyPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKEL---RRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 93 GMLFQ--SGALFTDmSVYENVAFPIRaHTKLSENLIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPDL 170
Cdd:cd03225 78 GLVFQnpDDQFFGP-TVEEEVAFGLE-NLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
7D06_B 171 IMYDEPFAGQDPIVKGVLTRLIRSLREAlDLTTIIVSHDVPETLSIADYIYVVAEGK 227
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
14-273 |
2.34e-57 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 187.21 E-value: 2.34e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSrqelfaARAR-M 92
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLH------ARDRkV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 93 GMLFQSGALFTDMSVYENVAFPIRA---HTKLSENLIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPD 169
Cdd:PRK10851 77 GFVFQHYALFRHMTVFDNIAFGLTVlprRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 170 LIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELQAY-ASPFV--- 245
Cdd:PRK10851 157 ILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREpATRFVlef 236
|
250 260 270 280
....*....|....*....|....*....|....*....|.
7D06_B 246 -------------KQFLTGSAEGPVEYQFSHQAYLDNEVRP 273
Cdd:PRK10851 237 mgevnrlqgtirgGQFHVGAHRWPLGYTPAYQGPVDLFLRP 277
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
13-249 |
5.94e-57 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 182.50 E-value: 5.94e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 13 LIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAqMSRQELFAARARM 92
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKLRRKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 93 GMLFQSGALFTDMSVYENVAF-PIRAHtKLSENlIAELVALK-LESVGLRGTEQLMPTELSGGMNRRVALARAIALDPDL 170
Cdd:COG1126 80 GMVFQQFNLFPHLTVLENVTLaPIKVK-KMSKA-EAEERAMElLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 171 IMYDEPFAGQDP-IVKGVLtRLIRSLREAlDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEEL-QAYASPFVKQF 248
Cdd:COG1126 158 MLFDEPTSALDPeLVGEVL-DVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFfENPQHERTRAF 235
|
.
7D06_B 249 L 249
Cdd:COG1126 236 L 236
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
13-237 |
6.42e-57 |
|
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: 182.94 E-value: 6.42e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 13 LIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELfaARaRM 92
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRREL--AR-RI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 93 GMLFQSGALFTDMSVYENVAFPIRAHTKLSENLIAE---LVALKLESVGLRG-TEQLMpTELSGGMNRRVALARAIALDP 168
Cdd:COG1120 78 AYVPQEPPAPFGLTVRELVALGRYPHLGLFGRPSAEdreAVEEALERTGLEHlADRPV-DELSGGERQRVLIARALAQEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
7D06_B 169 DLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEEL 237
Cdd:COG1120 157 PLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
14-249 |
1.75e-56 |
|
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: 181.34 E-value: 1.75e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRGE-RVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELfaaRARM 92
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVEL---RRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 93 GMLFQSGALFTDMSVYENVAFpIRAHTKLSENLIAELVALKLESVGLrGTEQLM---PTELSGGMNRRVALARAIALDPD 169
Cdd:cd03295 78 GYVIQQIGLFPHMTVEENIAL-VPKLLKWPKEKIRERADELLALVGL-DPAEFAdryPHELSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 170 LIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELQAY-ASPFVKQF 248
Cdd:cd03295 156 LLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSpANDFVAEF 235
|
.
7D06_B 249 L 249
Cdd:cd03295 236 V 236
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
13-237 |
2.60e-56 |
|
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: 180.47 E-value: 2.60e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 13 LIEVKNLS--F--NRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELFAA 88
Cdd:cd03258 1 MIELKNVSkvFgdTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 89 RARMGMLFQSGALFTDMSVYENVAFPIR-AHTKLSEnlIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALD 167
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEiAGVPKAE--IEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
7D06_B 168 PDLIMYDEPFAGQDP-IVKGVLTrLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEEL 237
Cdd:cd03258 159 PKVLLCDEATSALDPeTTQSILA-LLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
14-239 |
2.82e-56 |
|
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: 180.71 E-value: 2.82e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQElfaaRARMG 93
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHE----IARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 94 ML--FQSGALFTDMSVYENVAFPIRAHTKLSENLIAELVALK---------LESVGLRGTEQLMPTELSGGMNRRVALAR 162
Cdd:cd03219 77 IGrtFQIPRLFPELTVLENVMVAAQARTGSGLLLARARREEReareraeelLERVGLADLADRPAGELSYGQQRRLEIAR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
7D06_B 163 AIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREAlDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELQA 239
Cdd:cd03219 157 ALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
13-239 |
1.10e-55 |
|
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: 179.28 E-value: 1.10e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 13 LIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRqelfAARARM 92
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR----EARRQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 93 GMLFQSGALFTDMSVYENVAFPIRAHtKLSENLIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPDLIM 172
Cdd:COG4555 77 GVLPDERGLYDRLTVRENIRYFAELY-GLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
7D06_B 173 YDEPFAGQDPIVKGVLTRLIRSLREaLDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELQA 239
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRALKK-EGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELRE 221
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
14-241 |
6.18e-55 |
|
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: 177.37 E-value: 6.18e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLS--FNRGERVIyDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELFAARAR 91
Cdd:cd03256 1 IEVENLSktYPNGKKAL-KDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 92 MGMLFQSGALFTDMSVYENVAFPIRAHTKLSENL------IAELVALK-LESVGLRGTEQLMPTELSGGMNRRVALARAI 164
Cdd:cd03256 80 IGMIFQQFNLIERLSVLENVLSGRLGRRSTWRSLfglfpkEEKQRALAaLERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
7D06_B 165 ALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELQAYA 241
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEV 236
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
14-243 |
1.21e-54 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 176.10 E-value: 1.21e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRGERVIydNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSrqelfAARARMG 93
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP-----PAERPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 94 MLFQSGALFTDMSVYENVAFPIRAHTKLSENLIAELVALkLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPDLIMY 173
Cdd:COG3840 75 MLFQENNLFPHLTVAQNIGLGLRPGLKLTAEQRAQVEQA-LERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 174 DEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELQAYASP 243
Cdd:COG3840 154 DEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPP 223
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
14-209 |
6.44e-54 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 174.09 E-value: 6.44e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFN-RGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELFAARARM 92
Cdd:COG2884 2 IRFENVSKRyPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 93 GMLFQSGALFTDMSVYENVAFPIRAhTKLSENLIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPDLIM 172
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVALPLRV-TGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190
....*....|....*....|....*....|....*..
7D06_B 173 YDEPFAGQDPIVKGVLTRLIRSLReALDLTTIIVSHD 209
Cdd:COG2884 161 ADEPTGNLDPETSWEIMELLEEIN-RRGTTVLIATHD 196
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
14-247 |
1.51e-53 |
|
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: 173.50 E-value: 1.51e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQElfaaRARMG 93
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK----RARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 94 M--LFQSGALFTDMSVYENVAFPIRAHTKLSENLIAELVALkLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPDLI 171
Cdd:cd03218 77 IgyLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEEL-LEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
7D06_B 172 MYDEPFAGQDPIVKGVLTRLIRSLREaLDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELqaYASPFVKQ 247
Cdd:cd03218 156 LLDEPFAGVDPIAVQDIQKIIKILKD-RGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEI--AANELVRK 228
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
14-237 |
4.68e-53 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 175.65 E-value: 4.68e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLS--FNRGERVIY--DNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELFAAR 89
Cdd:COG1135 2 IELENLSktFPTKGGPVTalDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 90 ARMGMLFQSGALFTDMSVYENVAFPIRaHTKLSENLIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPD 169
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPLE-IAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
7D06_B 170 LIMYDEPFAGQDP-IVKGVLTrLIRSLREALDLTTIIVSH--DVPEtlSIADYIYVVAEGKIQGEGTPEEL 237
Cdd:COG1135 161 VLLCDEATSALDPeTTRSILD-LLKDINRELGLTIVLITHemDVVR--RICDRVAVLENGRIVEQGPVLDV 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
13-252 |
8.49e-53 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 171.91 E-value: 8.49e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 13 LIEVKNLS----FNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELfaa 88
Cdd:COG1124 1 MLEVRNLSvsygQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAF--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 89 RARMGMLFQS--GALFTDMSVYENVAFPIRAHTKL-SENLIAELvalkLESVGLrgTEQLM---PTELSGGMNRRVALAR 162
Cdd:COG1124 78 RRRVQMVFQDpyASLHPRHTVDRILAEPLRIHGLPdREERIAEL----LEQVGL--PPSFLdryPHQLSGGQRQRVAIAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 163 AIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELQAYA- 241
Cdd:COG1124 152 ALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPk 231
|
250
....*....|.
7D06_B 242 SPFVKQFLTGS 252
Cdd:COG1124 232 HPYTRELLAAS 242
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
14-237 |
2.02e-52 |
|
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: 171.87 E-value: 2.02e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSF--NRG---ERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELFAA 88
Cdd:TIGR04521 1 IKLKNVSYiyQPGtpfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 89 RARMGMLFQSGA--LFTDmSVYENVAF-PIRahTKLSENLIAELVALKLESVGLrgTEQLM---PTELSGGMNRRVALAR 162
Cdd:TIGR04521 81 RKKVGLVFQFPEhqLFEE-TVYKDIAFgPKN--LGLSEEEAEERVKEALELVGL--DEEYLersPFELSGGQMRRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
7D06_B 163 AIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEEL 237
Cdd:TIGR04521 156 VLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREV 230
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
14-228 |
2.82e-52 |
|
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: 168.34 E-value: 2.82e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIaqmsRQELFAARARMG 93
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI----KKEPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 94 MLFQSGALFTDMSVYENVafpirahtklsenliaelvalklesvglrgteqlmptELSGGMNRRVALARAIALDPDLIMY 173
Cdd:cd03230 77 YLPEEPSLYENLTVRENL-------------------------------------KLSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
7D06_B 174 DEPFAGQDPIVKGVLTRLIRSLREAlDLTTIIVSHDVPETLSIADYIYVVAEGKI 228
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-248 |
3.52e-52 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 174.37 E-value: 3.52e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 2 MNNKTPLSTQSLIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMS 81
Cdd:PRK09452 3 KLNKQPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 82 rqelfAARARMGMLFQSGALFTDMSVYENVAFPIRAHtKLSENLIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALA 161
Cdd:PRK09452 83 -----AENRHVNTVFQSYALFPHMTVFENVAFGLRMQ-KTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 162 RAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELqaYA 241
Cdd:PRK09452 157 RAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI--YE 234
|
250
....*....|
7D06_B 242 SP---FVKQF 248
Cdd:PRK09452 235 EPknlFVARF 244
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
12-248 |
2.48e-51 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 167.90 E-value: 2.48e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 12 SLIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQ--MSRqelfaaR 89
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHlpMHK------R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 90 ARMGM--LFQSGALFTDMSVYENvafpIRA---HTKLS--------ENLIAELvalKLEsvGLRGTeqlMPTELSGGMNR 156
Cdd:COG1137 76 ARLGIgyLPQEASIFRKLTVEDN----ILAvleLRKLSkkereerlEELLEEF---GIT--HLRKS---KAYSLSGGERR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 157 RVALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREAlDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEE 236
Cdd:COG1137 144 RVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKER-GIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEE 222
|
250
....*....|..
7D06_B 237 LqaYASPFVKQF 248
Cdd:COG1137 223 I--LNNPLVRKV 232
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
14-249 |
1.96e-50 |
|
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: 165.59 E-value: 1.96e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRGERVIYdNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQelfaaRARMG 93
Cdd:cd03299 1 LKVENLSKDWKEFKLK-NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE-----KRDIS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 94 MLFQSGALFTDMSVYENVAFPIRaHTKLSENLIAELValkLESVGLRGTEQLM---PTELSGGMNRRVALARAIALDPDL 170
Cdd:cd03299 75 YVPQNYALFPHMTVYKNIAYGLK-KRKVDKKEIERKV---LEIAEMLGIDHLLnrkPETLSGGEQQRVAIARALVVNPKI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 171 IMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELQAYASP-FVKQFL 249
Cdd:cd03299 151 LLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNeFVAEFL 230
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
14-228 |
2.82e-50 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 164.22 E-value: 2.82e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELfaaRARMG 93
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEW---RRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 94 MLFQSGALFtDMSVYENVAFPIR-AHTKLSENLIAELvalkLESVGLrgTEQLM---PTELSGGMNRRVALARAIALDPD 169
Cdd:COG4619 78 YVPQEPALW-GGTVRDNLPFPFQlRERKFDRERALEL----LERLGL--PPDILdkpVERLSGGERQRLALIRALLLQPD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
7D06_B 170 LIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKI 228
Cdd:COG4619 151 VLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
11-237 |
2.92e-50 |
|
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: 172.40 E-value: 2.92e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 11 QSLIEVKNLS--FNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGqLVPD----QGEVLLDGKDIAQMSRQE 84
Cdd:COG1123 2 TPLLEVRDLSvrYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMG-LLPHggriSGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 85 LfaaRARMGMLFQS-GALFTDMSVYENVAFPIRAHtKLSENLIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARA 163
Cdd:COG1123 81 R---GRRIGMVFQDpMTQLNPVTVGDQIAEALENL-GLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
7D06_B 164 IALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEEL 237
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
16-247 |
5.51e-50 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 164.75 E-value: 5.51e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 16 VKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQElfaaRARMGM- 94
Cdd:TIGR04406 4 AENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHE----RARLGIg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 95 -LFQSGALFTDMSVYENVAFPIRAHTKLSENLIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPDLIMY 173
Cdd:TIGR04406 80 yLPQEASIFRKLTVEENIMAVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
7D06_B 174 DEPFAGQDPIVKGVLTRLIRSLREAlDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELqaYASPFVKQ 247
Cdd:TIGR04406 160 DEPFAGVDPIAVGDIKKIIKHLKER-GIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEI--VANEKVRR 230
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-219 |
5.92e-50 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 165.21 E-value: 5.92e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 4 NKTPLSTQSLIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLR-------LIGGQLVpdQGEVLLDGKD 76
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGARV--EGEILLDGED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 77 I--AQMSRQELfaaRARMGMLFQSGALFTdMSVYENVAFPIRAHTKLSENLIAELVALKLESVGL----------RGteq 144
Cdd:COG1117 80 IydPDVDVVEL---RRRVGMVFQKPNPFP-KSIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALwdevkdrlkkSA--- 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
7D06_B 145 lmpTELSGGMNRRVALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREalDLTTIIVSHDVPETLSIADY 219
Cdd:COG1117 153 ---LGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKK--DYTIVIVTHNMQQAARVSDY 222
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
14-228 |
1.06e-49 |
|
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: 163.08 E-value: 1.06e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQmSRQELFAARARMG 93
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 94 MLFQSGALFTDMSVYENVAFPIRAHTKLSENLiAELVALK-LESVGLRGTEQLMPTELSGGMNRRVALARAIALDPDLIM 172
Cdd:cd03262 80 MVFQQFNLFPHLTVLENITLAPIKVKGMSKAE-AEERALElLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
7D06_B 173 YDEPFAGQDP-IVKGVLtRLIRSLREAlDLTTIIVSHDVPETLSIADYIYVVAEGKI 228
Cdd:cd03262 159 FDEPTSALDPeLVGEVL-DVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
8-249 |
1.69e-49 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 166.82 E-value: 1.69e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 8 LSTQSLIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQElfa 87
Cdd:PRK11432 1 MTQKNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 88 arARMGMLFQSGALFTDMSVYENVAFPIRAHtKLSENLIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALD 167
Cdd:PRK11432 78 --RDICMVFQSYALFPHMSLGENVGYGLKML-GVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 168 PDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEEL-QAYASPFVK 246
Cdd:PRK11432 155 PKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELyRQPASRFMA 234
|
...
7D06_B 247 QFL 249
Cdd:PRK11432 235 SFM 237
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
13-219 |
5.64e-48 |
|
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: 158.41 E-value: 5.64e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 13 LIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIaqmsRQELFAARARM 92
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI----RDAREDYRRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 93 GMLFQSGALFTDMSVYENVAFPIRAH-TKLSENLIAELvalkLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPDLI 171
Cdd:COG4133 78 AYLGHADGLKPELTVRENLRFWAALYgLRADREAIDEA----LEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLW 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
7D06_B 172 MYDEPFAGQDPIVKGVLTRLIRSLREAlDLTTIIVSHD-----VPETLSIADY 219
Cdd:COG4133 154 LLDEPFTALDAAGVALLAELIAAHLAR-GGAVLLTTHQplelaAARVLDLGDF 205
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
14-239 |
6.32e-48 |
|
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: 169.24 E-value: 6.32e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSF--NRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELfaaRAR 91
Cdd:COG2274 474 IELENVSFryPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASL---RRQ 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 92 MGMLFQSGALFTDmSVYENVAFpirAHTKLSENLIAElvALKLesVGLRGTEQLMP-----------TELSGGMNRRVAL 160
Cdd:COG2274 551 IGVVLQDVFLFSG-TIRENITL---GDPDATDEEIIE--AARL--AGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAI 622
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
7D06_B 161 ARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREalDLTTIIVSHDvPETLSIADYIYVVAEGKIQGEGTPEELQA 239
Cdd:COG2274 623 ARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEELLA 698
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
14-229 |
7.78e-48 |
|
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: 158.19 E-value: 7.78e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAqmsrqELFAARARMG 93
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT-----DLPPKDRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 94 MLFQSGALFTDMSVYENVAFPIRAHtKLSENLIAELValkLESVGLRGTEQLM---PTELSGGMNRRVALARAIALDPDL 170
Cdd:cd03301 76 MVFQNYALYPHMTVYDNIAFGLKLR-KVPKDEIDERV---REVAELLQIEHLLdrkPKQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
7D06_B 171 IMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQ 229
Cdd:cd03301 152 FLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
13-243 |
7.05e-47 |
|
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: 159.06 E-value: 7.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 13 LIEVKNLS--FNRGERVIY--DNISLNIRRGQITAIMGPSGTGKTTLLRLIGGqLVP----DQGEVLLDGKDIAQMSRQE 84
Cdd:COG0444 1 LLEVRNLKvyFPTRRGVVKavDGVSFDVRRGETLGLVGESGSGKSTLARAILG-LLPppgiTSGEILFDGEDLLKLSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 85 LFAARAR-MGMLFQS--GALftD--MSVYENVAFPIRAHTKLSENLIAELVALKLESVGLRGTEQLM---PTELSGGMNR 156
Cdd:COG0444 80 LRKIRGReIQMIFQDpmTSL--NpvMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLdryPHELSGGMRQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 157 RVALARAIALDPDLIMYDEPFAGQDPIV-KGVLtRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPE 235
Cdd:COG0444 158 RVMIARALALEPKLLIADEPTTALDVTIqAQIL-NLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVE 236
|
....*...
7D06_B 236 ELqaYASP 243
Cdd:COG0444 237 EL--FENP 242
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
14-237 |
8.31e-47 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 155.74 E-value: 8.31e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLS--FNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIaqmsRQELFAARAR 91
Cdd:cd03263 1 LQIRNLTktYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI----RTDRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 92 MGMLFQSGALFTDMSVYENVAF--PIRAHTKLSENLIAELValkLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPD 169
Cdd:cd03263 77 LGYCPQFDALFDELTVREHLRFyaRLKGLPKSEIKEEVELL---LRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
7D06_B 170 LIMYDEPFAGQDPIVKGVLTRLIRSLREalDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEEL 237
Cdd:cd03263 154 VLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
14-227 |
2.54e-46 |
|
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: 152.92 E-value: 2.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRGER--VIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELfaaRAR 91
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESL---RKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 92 MGMLFQSGALFtDMSVYENVafpirahtklsenliaelvalklesvglrgteqlmpteLSGGMNRRVALARAIALDPDLI 171
Cdd:cd03228 78 IAYVPQDPFLF-SGTIRENI--------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
7D06_B 172 MYDEPFAGQDPIVKGVLTRLIRSLREalDLTTIIVSHDvPETLSIADYIYVVAEGK 227
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAK--GKTVIVIAHR-LSTIRDADRIIVLDDGR 171
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
14-237 |
3.85e-46 |
|
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: 155.67 E-value: 3.85e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFN--RGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIaqMSRQELFAARAR 91
Cdd:TIGR04520 1 IEVENVSFSypESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDT--LDEENLWEIRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 92 MGMLFQS------GALftdmsVYENVAF-PirahtklsENL------IAELVALKLESVGLRGTEQLMPTELSGGMNRRV 158
Cdd:TIGR04520 79 VGMVFQNpdnqfvGAT-----VEDDVAFgL--------ENLgvpreeMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
7D06_B 159 ALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSiADYIYVVAEGKIQGEGTPEEL 237
Cdd:TIGR04520 146 AIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREI 223
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
9-236 |
6.22e-46 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 154.09 E-value: 6.22e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 9 STQSLIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQmsrqelfaA 88
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR--------A 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 89 RARMGMLFQSGALFTD--MSVYENVAFPIRAHTKLSENLIA---ELVALKLESVGLRGTEQLMPTELSGGMNRRVALARA 163
Cdd:COG1121 74 RRRIGYVPQRAEVDWDfpITVRDVVLMGRYGRRGLFRRPSRadrEAVDEALERVGLEDLADRPIGELSGGQQQRVLLARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
7D06_B 164 IALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREAlDLTTIIVSHDVPETLSIADYIYVVAEGKIqGEGTPEE 236
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLV-AHGPPEE 224
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
15-227 |
6.92e-46 |
|
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: 151.24 E-value: 6.92e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 15 EVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELfaaRARMGM 94
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL---RRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 95 LFQsgalftdmsvyenvafpirahtklsenliaelvalklesvglrgteqlmpteLSGGMNRRVALARAIALDPDLIMYD 174
Cdd:cd00267 78 VPQ----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
7D06_B 175 EPFAGQDPIVKGVLTRLIRSLREAlDLTTIIVSHDVPETLSIADYIYVVAEGK 227
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-239 |
7.23e-45 |
|
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: 158.77 E-value: 7.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 3 NNKTPLSTQSLIEVKNLSFNR-GERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMS 81
Cdd:COG4988 326 TAPLPAAGPPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLD 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 82 RQELfaaRARMGMLFQSGALFTDmSVYENVAFpirAHTKLSEnliAELVALkLESVGLRGTEQLMP----TE-------L 150
Cdd:COG4988 406 PASW---RRQIAWVPQNPYLFAG-TIRENLRL---GRPDASD---EELEAA-LEAAGLDEFVAALPdgldTPlgeggrgL 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 151 SGGMNRRVALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREalDLTTIIVSHDvPETLSIADYIYVVAEGKIQG 230
Cdd:COG4988 475 SGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHR-LALLAQADRILVLDDGRIVE 551
|
....*....
7D06_B 231 EGTPEELQA 239
Cdd:COG4988 552 QGTHEELLA 560
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
15-232 |
3.23e-44 |
|
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: 147.58 E-value: 3.23e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 15 EVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELfaARaRMGM 94
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL--AR-KIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 95 LFQSgalftdmsvyenvafpirahtklsenliaelvalkLESVGLRG-TEQLMpTELSGGMNRRVALARAIALDPDLIMY 173
Cdd:cd03214 78 VPQA-----------------------------------LELLGLAHlADRPF-NELSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
7D06_B 174 DEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEG 232
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
13-249 |
3.57e-44 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 149.47 E-value: 3.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 13 LIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELfAARARM 92
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDER-LIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 93 GMLFQSGALFTDMSVYENVAF-PIR---AHTKLSENLIAELvalkLESVGLRGTEQLMPTELSGGMNRRVALARAIALDP 168
Cdd:PRK09493 80 GMVFQQFYLFPHLTALENVMFgPLRvrgASKEEAEKQAREL----LAKVGLAERAHHYPSELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 169 DLIMYDEPFAGQDPIVKGVLTRLIRSLREAlDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEEL-QAYASPFVKQ 247
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLiKNPPSQRLQE 234
|
..
7D06_B 248 FL 249
Cdd:PRK09493 235 FL 236
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
9-243 |
5.07e-44 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 151.81 E-value: 5.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 9 STQSLIEVKNLS---------FNRGERVIY--DNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDI 77
Cdd:COG4608 3 MAEPLLEVRDLKkhfpvrgglFGRTVGVVKavDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 78 AQMSRQELFAARARMGMLFQ--SGALFTDMSVYENVAFPIRAHTKLSENLIAELVALKLESVGLRgTEQLM--PTELSGG 153
Cdd:COG4608 83 TGLSGRELRPLRRRMQMVFQdpYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLR-PEHADryPHEFSGG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 154 MNRRVALARAIALDPDLIMYDEPFAGQD-PIVKGVLTrLIRSLREALDLTTIIVSHDvpetLS----IADYIYVVAEGKI 228
Cdd:COG4608 162 QRQRIGIARALALNPKLIVCDEPVSALDvSIQAQVLN-LLEDLQDELGLTYLFISHD----LSvvrhISDRVAVMYLGKI 236
|
250
....*....|....*
7D06_B 229 QGEGTPEELqaYASP 243
Cdd:COG4608 237 VEIAPRDEL--YARP 249
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
15-228 |
6.55e-44 |
|
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: 148.07 E-value: 6.55e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 15 EVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMsrqelfaaRARMGM 94
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE--------RKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 95 LFQSGALFTDM--SVYENVAFPIRAHTKLSENLIAE---LVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPD 169
Cdd:cd03235 73 VPQRRSIDRDFpiSVRDVVLMGLYGHKGLFRRLSKAdkaKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
7D06_B 170 LIMYDEPFAGQDPIVKGVLTRLIRSLReALDLTTIIVSHDVPETLSIADYIYVVAEGKI 228
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLRELR-REGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
39-232 |
1.31e-43 |
|
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: 147.44 E-value: 1.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 39 GQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKdIAQMSRQELF--AARARMGMLFQSGALFTDMSVYENVAFPIR 116
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGT-VLFDSRKKINlpPQQRKIGLVFQQYALFPHLNVRENLAFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 117 AHtklSENLIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLR 196
Cdd:cd03297 102 RK---RNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIK 178
|
170 180 190
....*....|....*....|....*....|....*.
7D06_B 197 EALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEG 232
Cdd:cd03297 179 KNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
6-239 |
2.01e-43 |
|
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: 154.92 E-value: 2.01e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 6 TPLSTQSLIEVKNLSF--NRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQ 83
Cdd:COG4987 326 APAPGGPSLELEDVSFryPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDED 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 84 ELfaaRARMGMLFQSGALFtDMSVYENVAFpirAHTKLSEnliAELVALkLESVGLRGTEQLMP-----------TELSG 152
Cdd:COG4987 406 DL---RRRIAVVPQRPHLF-DTTLRENLRL---ARPDATD---EELWAA-LERVGLGDWLAALPdgldtwlgeggRRLSG 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 153 GMNRRVALARAIALDPDLIMYDEPFAGQDPIvkgvlT--RLIRSLREAL-DLTTIIVSHDvPETLSIADYIYVVAEGKIQ 229
Cdd:COG4987 475 GERRRLALARALLRDAPILLLDEPTEGLDAA-----TeqALLADLLEALaGRTVLLITHR-LAGLERMDRILVLEDGRIV 548
|
250
....*....|
7D06_B 230 GEGTPEELQA 239
Cdd:COG4987 549 EQGTHEELLA 558
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
13-236 |
2.16e-43 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 147.95 E-value: 2.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 13 LIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELfaARARm 92
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWEL--ARRR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 93 GMLFQSGALFTDMSVYENVAFPIRAHTKLSENlIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIA------- 165
Cdd:COG4559 78 AVLPQHSSLAFPFTVEEVVALGRAPHGSSAAQ-DRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvd 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
7D06_B 166 LDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREAlDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEE 236
Cdd:COG4559 157 GGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
9-237 |
2.94e-43 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 147.83 E-value: 2.94e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 9 STQSLIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELfaa 88
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQI--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 89 rARMGML--FQSGALFTDMSVYEN--VAfpirAHTKLSENLIAELVALK----------------LESVGLRGTEQLMPT 148
Cdd:PRK11300 78 -ARMGVVrtFQHVRLFREMTVIENllVA----QHQQLKTGLFSGLLKTPafrraesealdraatwLERVGLLEHANRQAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 149 ELSGGMNRRVALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKI 228
Cdd:PRK11300 153 NLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTP 232
|
....*....
7D06_B 229 QGEGTPEEL 237
Cdd:PRK11300 233 LANGTPEEI 241
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-243 |
2.36e-42 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 148.83 E-value: 2.36e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 4 NKTPLSTQSLIEVKNL--SFNrGERVIyDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMS 81
Cdd:PRK11607 10 AKTRKALTPLLEIRNLtkSFD-GQHAV-DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 82 rqelfAARARMGMLFQSGALFTDMSVYENVAFPIRaHTKLSENLIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALA 161
Cdd:PRK11607 88 -----PYQRPINMMFQSYALFPHMTVEQNIAFGLK-QDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 162 RAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELqaYA 241
Cdd:PRK11607 162 RSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI--YE 239
|
..
7D06_B 242 SP 243
Cdd:PRK11607 240 HP 241
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
13-236 |
4.07e-42 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 144.91 E-value: 4.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 13 LIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELfaARARm 92
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAEL--ARRR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 93 GMLFQSGALFTDMSVYENVAF---PIRAHTKLSENLIAElvalKLESVGLRGTEQLMPTELSGGMNRRVALARAIA---- 165
Cdd:PRK13548 79 AVLPQHSSLSFPFTVEEVVAMgraPHGLSRAEDDALVAA----ALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwe 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
7D06_B 166 --LDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEE 236
Cdd:PRK13548 155 pdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
14-239 |
1.03e-41 |
|
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: 142.57 E-value: 1.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQElfaaRARMG 93
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHE----RARAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 94 MLF--QSGALFTDMSVYEN--VAFPIRAHTKLSENlIAELVAL------KLESVGlrGTeqlmpteLSGGMNRRVALARA 163
Cdd:cd03224 77 IGYvpEGRRIFPELTVEENllLGAYARRRAKRKAR-LERVYELfprlkeRRKQLA--GT-------LSGGEQQMLAIARA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
7D06_B 164 IALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREaLDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELQA 239
Cdd:cd03224 147 LMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRD-EGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
13-237 |
3.98e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 142.91 E-value: 3.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 13 LIEVKNLSFNRGE-RVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIaQMSRQELFAARAR 91
Cdd:PRK13639 1 ILETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 92 MGMLFQS--GALFTDmSVYENVAF-PIraHTKLSENLIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDP 168
Cdd:PRK13639 80 VGIVFQNpdDQLFAP-TVEEDVAFgPL--NLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
7D06_B 169 DLIMYDEPFAGQDPIVKGVLTRLIRSLREAlDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEEL 237
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
33-232 |
6.24e-41 |
|
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: 140.32 E-value: 6.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 33 SLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSrqelfAARARMGMLFQSGALFTDMSVYENVA 112
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAP-----PADRPVSMLFQENNLFAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 113 FPIRAHTKLSEnLIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLI 192
Cdd:cd03298 93 LGLSPGLKLTA-EDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
7D06_B 193 RSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEG 232
Cdd:cd03298 172 LDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
14-237 |
6.94e-41 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 148.39 E-value: 6.94e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFN-RGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELfaaRARM 92
Cdd:COG1132 340 IEFENVSFSyPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESL---RRQI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 93 GMLFQSGALFTDmSVYENVAFP--------IRAHTKLSEnlIAELVAlKLES-----VGLRGteqlmpTELSGGMNRRVA 159
Cdd:COG1132 417 GVVPQDTFLFSG-TIRENIRYGrpdatdeeVEEAAKAAQ--AHEFIE-ALPDgydtvVGERG------VNLSGGQRQRIA 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
7D06_B 160 LARAIALDPDLIMYDEPFAGQDPIVKgvlTRLIRSLREAL-DLTTIIVSHDVpETLSIADYIYVVAEGKIQGEGTPEEL 237
Cdd:COG1132 487 IARALLKDPPILILDEATSALDTETE---ALIQEALERLMkGRTTIVIAHRL-STIRNADRILVLDDGRIVEQGTHEEL 561
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
7-211 |
1.06e-40 |
|
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: 140.26 E-value: 1.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 7 PLSTQSLIEVKNLSF----NRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSR 82
Cdd:COG4181 2 SSSSAPIIELRGLTKtvgtGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 83 QELFAARAR-MGMLFQSGALFTDMSVYENVAFPirahtklsenliAELVALK---------LESVGLRGTEQLMPTELSG 152
Cdd:COG4181 82 DARARLRARhVGFVFQSFQLLPTLTALENVMLP------------LELAGRRdarararalLERVGLGHRLDHYPAQLSG 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
7D06_B 153 GMNRRVALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVP 211
Cdd:COG4181 150 GEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPA 208
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
29-178 |
1.50e-40 |
|
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: 137.39 E-value: 1.50e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 29 YDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELfaaRARMGMLFQSGALFTDMSVY 108
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSL---RKEIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
7D06_B 109 ENVAFP--IRAHTKLSENLIAELVALKLESVGLRGTEQLM-PTELSGGMNRRVALARAIALDPDLIMYDEPFA 178
Cdd:pfam00005 78 ENLRLGllLKGLSKREKDARAEEALEKLGLGDLADRPVGErPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
15-210 |
2.07e-40 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 139.15 E-value: 2.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 15 EVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPD---QGEVLLDGKDIAqmsrqELFAARAR 91
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLT-----ALPAEQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 92 MGMLFQSGALFTDMSVYENVAFPIRAHTKLSENliAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPDLI 171
Cdd:COG4136 78 IGILFQDDLLFPHLSVGENLAFALPPTIGRAQR--RARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRAL 155
|
170 180 190
....*....|....*....|....*....|....*....
7D06_B 172 MYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDV 210
Cdd:COG4136 156 LLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDE 194
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
12-239 |
3.67e-40 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 138.96 E-value: 3.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 12 SLIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQElfaaRAR 91
Cdd:COG0410 2 PMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHR----IAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 92 MGMLF--QSGALFTDMSVYEN---VAFPIRAHTKLSENLiAELVAL------KLESVGlrGTeqlmpteLSGG---Mnrr 157
Cdd:COG0410 78 LGIGYvpEGRRIFPSLTVEENlllGAYARRDRAEVRADL-ERVYELfprlkeRRRQRA--GT-------LSGGeqqM--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 158 VALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREAlDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEEL 237
Cdd:COG0410 145 LAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL 223
|
..
7D06_B 238 QA 239
Cdd:COG0410 224 LA 225
|
|
| ABC_choXWV_ATP |
TIGR03415 |
choline ABC transporter, ATP-binding protein; Members of this protein family are the ... |
31-248 |
5.85e-40 |
|
choline ABC transporter, ATP-binding protein; Members of this protein family are the ATP-binding subunit of a three-protein transporter. This family belongs, more broadly, to the family of proline and glycine-betaine transporters, but members have been identified by direct characterization and by bioinformatic means as choline transporters. Many species have several closely-related members of this family, probably with variable abilities to act additionally on related quaternary amines. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 188317 [Multi-domain] Cd Length: 382 Bit Score: 142.61 E-value: 5.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 31 NISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLL-DGK---DIAQMSRQELFAARA-RMGMLFQSGALFTDM 105
Cdd:TIGR03415 42 NASLDIEEGEICVLMGLSGSGKSTLLRAVNGLNPVSRGSVLVkDGDgsvDVANCDAATLRRLRThRVSMVFQQFALLPWR 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 106 SVYENVAFPIRAhTKLSENLIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPDLIMYDEPFAGQDPIVK 185
Cdd:TIGR03415 122 TVEENVAFGLEM-QGMPKAERRKRVDEQLELVGLAQWADRKPGELSGGMQQRVGLARAFATEAPILLMDEPFSALDPLIR 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
7D06_B 186 GVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELQAY-ASPFVKQF 248
Cdd:TIGR03415 201 TQLQDELLELQSKLKKTIVFVSHDLDEALKIGNRIAIMEGGRIIQHGTPEEIVLNpANDYVADF 264
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
30-209 |
8.58e-40 |
|
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: 137.54 E-value: 8.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 30 DNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELFAARARMGMLFQSGALFTDMSVYE 109
Cdd:cd03292 18 DGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKIGVVFQDFRLLPDRNVYE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 110 NVAFPIRAhTKLSENLIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPDLIMYDEPFAGQDPIVKGVLT 189
Cdd:cd03292 98 NVAFALEV-TGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIM 176
|
170 180
....*....|....*....|.
7D06_B 190 RLIRSLREAldLTTIIVS-HD 209
Cdd:cd03292 177 NLLKKINKA--GTTVVVAtHA 195
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
8-251 |
3.38e-39 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 140.94 E-value: 3.38e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 8 LSTQSLIEVKNLSFNrgerviYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELFA 87
Cdd:PRK10070 29 LSKEQILEKTGLSLG------VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 88 AR-ARMGMLFQSGALFTDMSVYENVAFPIR-AHTKLSENLIAELVALKleSVGLRGTEQLMPTELSGGMNRRVALARAIA 165
Cdd:PRK10070 103 VRrKKIAMVFQSFALMPHMTVLDNTAFGMElAGINAEERREKALDALR--QVGLENYAHSYPDELSGGMRQRVGLARALA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 166 LDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEE-LQAYASPF 244
Cdd:PRK10070 181 INPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEiLNNPANDY 260
|
....*..
7D06_B 245 VKQFLTG 251
Cdd:PRK10070 261 VRTFFRG 267
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
11-237 |
6.63e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 137.04 E-value: 6.63e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 11 QSLIEVKNLSF--NRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIaqmSRQELFAA 88
Cdd:PRK13632 5 SVMIKVENVSFsyPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI---SKENLKEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 89 RARMGMLFQS-GALFTDMSVYENVAFPIRaHTKLSENLIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALD 167
Cdd:PRK13632 82 RKKIGIIFQNpDNQFIGATVEDDIAFGLE-NKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 168 PDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLsIADYIYVVAEGKIQGEGTPEEL 237
Cdd:PRK13632 161 PEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEI 229
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
14-236 |
1.01e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 136.72 E-value: 1.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSF--NRG---ERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQmSRQELFAA 88
Cdd:PRK13637 3 IKIENLTHiyMEGtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITD-KKVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 89 RARMGMLFQ--SGALFTDmSVYENVAF-PIRahTKLSENLIAELVALKLESVGL--RGTEQLMPTELSGGMNRRVALARA 163
Cdd:PRK13637 82 RKKVGLVFQypEYQLFEE-TIEKDIAFgPIN--LGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
7D06_B 164 IALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEE 236
Cdd:PRK13637 159 VAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPRE 231
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
31-239 |
1.06e-38 |
|
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: 138.70 E-value: 1.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 31 NISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGkDIAQMSRQELF--AARARMGMLFQSGALFTDMSVY 108
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGG-EVLQDSARGIFlpPHRRRIGYVFQEARLFPHLSVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 109 ENVAFPI-RAHTKLSENLIAELVALklesVGLRGTEQLMPTELSGGMNRRVALARAIALDPDLIMYDEPFAGQDPIVKGV 187
Cdd:COG4148 96 GNLLYGRkRAPRAERRISFDEVVEL----LGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
7D06_B 188 LTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELQA 239
Cdd:COG4148 172 ILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLS 223
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
14-232 |
2.06e-38 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 133.88 E-value: 2.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIaqmsrQELFAARARMG 93
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY-----QKNIEALRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 94 MLFQSGALFTDMSVYENvafpIRAHTKL---SENLIAELvalkLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPDL 170
Cdd:cd03268 76 ALIEAPGFYPNLTAREN----LRLLARLlgiRKKRIDEV----LDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
7D06_B 171 IMYDEPFAGQDPIvkGV--LTRLIRSLREAlDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEG 232
Cdd:cd03268 148 LILDEPTNGLDPD--GIkeLRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
12-251 |
3.02e-38 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 134.99 E-value: 3.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 12 SLIEVKNLSFN----RGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSrqelfa 87
Cdd:COG4525 2 SMLTVRHVSVRypggGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 88 arARMGMLFQSGALFTDMSVYENVAFPIRAhTKLSENLIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALD 167
Cdd:COG4525 76 --ADRGVVFQKDALLPWLNVLDNVAFGLRL-RGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAAD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 168 PDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVA--EGKIqgegtpeeLQAYASPFV 245
Cdd:COG4525 153 PRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSpgPGRI--------VERLELDFS 224
|
....*.
7D06_B 246 KQFLTG 251
Cdd:COG4525 225 RRFLAG 230
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
14-233 |
3.14e-38 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 136.85 E-value: 3.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLS--FNRGERVIY--DNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELFAAR 89
Cdd:PRK11153 2 IELKNISkvFPQGGRTIHalNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 90 ARMGMLFQSGALFTDMSVYENVAFPIRAhTKLSENLIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPD 169
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVALPLEL-AGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
7D06_B 170 LIMYDEPFAGQDP-IVKGVLTrLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGT 233
Cdd:PRK11153 161 VLLCDEATSALDPaTTRSILE-LLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGT 224
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
14-238 |
3.87e-38 |
|
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: 133.26 E-value: 3.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQelfaARARMG 93
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE----VRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 94 MLFQSGALFTDMSVYENVAFPIRAHTKLSENL---IAELvalkLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPDL 170
Cdd:cd03265 77 IVFQDLSVDDELTGWENLYIHARLYGVPGAERrerIDEL----LDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
7D06_B 171 IMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELQ 238
Cdd:cd03265 153 LFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
13-243 |
4.37e-37 |
|
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: 137.51 E-value: 4.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 13 LIEVKNLS---------FNRGERVIY--DNISLNIRRGQITAIMGPSGTGKTTL----LRLIggqlvPDQGEVLLDGKDI 77
Cdd:COG4172 275 LLEARDLKvwfpikrglFRRTVGHVKavDGVSLTLRRGETLGLVGESGSGKSTLglalLRLI-----PSEGEIRFDGQDL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 78 AQMSRQELFAARARMGMLFQS--GALFTDMSVYENVAFPIRAH-TKLSENLIAELVALKLESVGLrgTEQLM---PTELS 151
Cdd:COG4172 350 DGLSRRALRPLRRRMQVVFQDpfGSLSPRMTVGQIIAEGLRVHgPGLSAAERRARVAEALEEVGL--DPAARhryPHEFS 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 152 GGMNRRVALARAIALDPDLIMYDEPFAGQDPIV-KGVLTrLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQG 230
Cdd:COG4172 428 GGQRQRIAIARALILEPKLLVLDEPTSALDVSVqAQILD-LLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVE 506
|
250
....*....|...
7D06_B 231 EGTPEELqaYASP 243
Cdd:COG4172 507 QGPTEQV--FDAP 517
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
12-239 |
5.46e-37 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 131.17 E-value: 5.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 12 SLIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQElfAARAR 91
Cdd:PRK10895 2 ATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA--RARRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 92 MGMLFQSGALFTDMSVYENVAFPIRAHTKLSENLIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPDLI 171
Cdd:PRK10895 80 IGYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
7D06_B 172 MYDEPFAGQDPIVKGVLTRLIRSLREAlDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELQA 239
Cdd:PRK10895 160 LLDEPFAGVDPISVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
7-237 |
8.59e-37 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 132.24 E-value: 8.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 7 PLSTqSLIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQelf 86
Cdd:PRK13537 2 PMSV-APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARH--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 87 aARARMGMLFQSGALFTDMSVYENVAFPIRaHTKLSENLIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIAL 166
Cdd:PRK13537 78 -ARQRVGVVPQFDNLDPDFTVRENLLVFGR-YFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
7D06_B 167 DPDLIMYDEPFAGQDPIVKGVLTRLIRSLReALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEEL 237
Cdd:PRK13537 156 DPDVLVLDEPTTGLDPQARHLMWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
10-237 |
1.02e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 131.39 E-value: 1.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 10 TQSLIEVKNLSF---NRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKdiaQMSRQELF 86
Cdd:PRK13650 1 MSNIIEVKNLTFkykEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD---LLTEENVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 87 AARARMGMLFQS-GALFTDMSVYENVAFPIRaHTKLSENLIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIA 165
Cdd:PRK13650 78 DIRHKIGMVFQNpDNQFVGATVEDDVAFGLE-NKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
7D06_B 166 LDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPEtLSIADYIYVVAEGKIQGEGTPEEL 237
Cdd:PRK13650 157 MRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPREL 227
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
41-239 |
1.32e-36 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 132.93 E-value: 1.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 41 ITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKdIAQMSRQELF--AARARMGMLFQSGALFTDMSVYENVAFPIR-- 116
Cdd:TIGR02142 25 VTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGR-TLFDSRKGIFlpPEKRRIGYVFQEARLFPHLSVRGNLRYGMKra 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 117 --AHTKLSENLIAELvaLKLESVGLRGteqlmPTELSGGMNRRVALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRS 194
Cdd:TIGR02142 104 rpSERRISFERVIEL--LGIGHLLGRL-----PGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLER 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
7D06_B 195 LREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELQA 239
Cdd:TIGR02142 177 LHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWA 221
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
30-226 |
1.57e-36 |
|
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: 129.51 E-value: 1.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 30 DNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQmsrqelfAARARMgMLFQSGALFTDMSVYE 109
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITE-------PGPDRM-VVFQNYSLLPWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 110 NVAFPI-RAHTKLSENLIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPDLIMYDEPFAGQDPIVKGVL 188
Cdd:TIGR01184 74 NIALAVdRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190
....*....|....*....|....*....|....*...
7D06_B 189 TRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEG 226
Cdd:TIGR01184 154 QEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
24-239 |
2.65e-36 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 130.97 E-value: 2.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 24 GERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQelfaARARMGMLFQSGALFT 103
Cdd:TIGR01188 4 GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRK----VRRSIGIVPQYASVDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 104 DMSVYENVAFPIRAH---TKLSENLIAELvalkLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPDLIMYDEPFAGQ 180
Cdd:TIGR01188 80 DLTGRENLEMMGRLYglpKDEAEERAEEL----LELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
7D06_B 181 DPIVKGVLTRLIRSLREAlDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELQA 239
Cdd:TIGR01188 156 DPRTRRAIWDYIRALKEE-GVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKR 213
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
17-232 |
3.16e-36 |
|
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: 128.25 E-value: 3.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 17 KNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAqmsrQELFAARARMGMLF 96
Cdd:cd03266 9 KRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVV----KEPAEARRRLGFVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 97 QSGALFTDMSVYENVAFPIRAHTKLSENLIAELVALklesVGLRGTEQLM--PTE-LSGGMNRRVALARAIALDPDLIMY 173
Cdd:cd03266 85 DSTGLYDRLTARENLEYFAGLYGLKGDELTARLEEL----ADRLGMEELLdrRVGgFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 174 DEPFAGQDPIVKGVLTRLIRSLREAldLTTIIVS-HDVPETLSIADYIYVVAEGKIQGEG 232
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQLRAL--GKCILFStHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
12-249 |
5.78e-36 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 128.71 E-value: 5.78e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 12 SLIEVKNL--SFNrGERVIYdNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQG-----EVLLDG-KDIAQMSRQ 83
Cdd:PRK11264 2 SAIEVKNLvkKFH-GQTVLH-GIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIDTaRSLSQQKGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 84 eLFAARARMGMLFQSGALFTDMSVYENV-AFPIRAHTKLSENLIAELVALkLESVGLRGTEQLMPTELSGGMNRRVALAR 162
Cdd:PRK11264 80 -IRQLRQHVGFVFQNFNLFPHRTVLENIiEGPVIVKGEPKEEATARAREL-LAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 163 AIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREAlDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELQAYAS 242
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQ 236
|
....*...
7D06_B 243 -PFVKQFL 249
Cdd:PRK11264 237 qPRTRQFL 244
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
33-243 |
8.30e-36 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 127.78 E-value: 8.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 33 SLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSrqelfAARARMGMLFQSGALFTDMSVYENVA 112
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTP-----PSRRPVSMLFQENNLFSHLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 113 FPIRAHTKLSENLIAELVALkLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLI 192
Cdd:PRK10771 94 LGLNPGLKLNAAQREKLHAI-ARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
7D06_B 193 RSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELQAYASP 243
Cdd:PRK10771 173 SQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKAS 223
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
14-237 |
1.08e-35 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 127.89 E-value: 1.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELfaARaRMG 93
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSREL--AK-RLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 94 MLFQSGALFTDMSVYENVAF---PiraHTK--LSENlIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDP 168
Cdd:COG4604 79 ILRQENHINSRLTVRELVAFgrfP---YSKgrLTAE-DREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDT 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
7D06_B 169 DLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEEL 237
Cdd:COG4604 155 DYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-252 |
1.42e-35 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 127.78 E-value: 1.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 1 MMNNKtplstqslIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQM 80
Cdd:PRK10619 1 MSENK--------LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 81 ----------SRQELFAARARMGMLFQSGALFTDMSVYENV-AFPIRAhTKLSENLIAELVALKLESVGLRGTEQL-MPT 148
Cdd:PRK10619 73 rdkdgqlkvaDKNQLRLLRTRLTMVFQHFNLWSHMTVLENVmEAPIQV-LGLSKQEARERAVKYLAKVGIDERAQGkYPV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 149 ELSGGMNRRVALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREAlDLTTIIVSHDVPETLSIADYIYVVAEGKI 228
Cdd:PRK10619 152 HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
250 260
....*....|....*....|....*
7D06_B 229 QGEGTPEELQAY-ASPFVKQFLTGS 252
Cdd:PRK10619 231 EEEGAPEQLFGNpQSPRLQQFLKGS 255
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
13-239 |
2.35e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 128.04 E-value: 2.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 13 LIEVKNLSFN--RGERVIYDnISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIaQMSRQELFAARA 90
Cdd:PRK13636 5 ILKVEELNYNysDGTHALKG-ININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGLMKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 91 RMGMLFQS--GALFTdMSVYENVAFPIrAHTKLSENLIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDP 168
Cdd:PRK13636 83 SVGMVFQDpdNQLFS-ASVYQDVSFGA-VNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
7D06_B 169 DLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELQA 239
Cdd:PRK13636 161 KVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFA 231
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
13-237 |
2.77e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 127.61 E-value: 2.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 13 LIEVKNLSFN-RGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELfaaRAR 91
Cdd:PRK13652 3 LIETRDLCYSySGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREV---RKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 92 MGMLFQS--GALFTDmSVYENVAF-PIraHTKLSENLIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDP 168
Cdd:PRK13652 80 VGLVFQNpdDQIFSP-TVEQDIAFgPI--NLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
7D06_B 169 DLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEEL 237
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
14-232 |
2.93e-35 |
|
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: 125.77 E-value: 2.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRGERVIYDNISLNIRRGqITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMsRQELfaaRARMG 93
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQ-PQKL---RRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 94 MLFQSGALFTDMSVYENVAFPIRAHtKLSENLIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPDLIMY 173
Cdd:cd03264 76 YLPQEFGVYPNFTVREFLDYIAWLK-GIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
7D06_B 174 DEPFAGQDPIVKGVLTRLIRSLREalDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEG 232
Cdd:cd03264 155 DEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
10-246 |
4.90e-35 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 127.05 E-value: 4.90e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 10 TQSLIEVKNLSFN--RGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKdiaQMSRQELFA 87
Cdd:PRK13635 2 KEEIIRVEHISFRypDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM---VLSEETVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 88 ARARMGMLFQS-GALFTDMSVYENVAFPIRAHTKLSENLIaELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIAL 166
Cdd:PRK13635 79 VRRQVGMVFQNpDNQFVGATVQDDVAFGLENIGVPREEMV-ERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 167 DPDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSiADYIYVVAEGKIQGEGTPEELQAYASPFVK 246
Cdd:PRK13635 158 QPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKSGHMLQE 236
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-251 |
7.99e-35 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 125.80 E-value: 7.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 11 QSLIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGG--QLVPD---QGEVLLDGKDIAQMSRQEL 85
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRliELYPEarvSGEVYLDGQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 86 faaRARMGMLFQSGALFTDMSVYENVAFPIRAHTKL-SENLIAELVALKLESVGL----RGTEQLMPTELSGGMNRRVAL 160
Cdd:PRK14247 81 ---RRRVQMVFQIPNPIPNLSIFENVALGLKLNRLVkSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 161 ARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREalDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELqaY 240
Cdd:PRK14247 158 ARALAFQPEVLLADEPTANLDPENTAKIESLFLELKK--DMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREV--F 233
|
250
....*....|....
7D06_B 241 ASP---FVKQFLTG 251
Cdd:PRK14247 234 TNPrheLTEKYVTG 247
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
15-228 |
8.51e-35 |
|
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: 124.29 E-value: 8.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 15 EVKNLSF--NRGERVIyDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQElfaaraRM 92
Cdd:cd03226 1 RIENISFsyKKGTEIL-DDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRK------SI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 93 GMLFQS--GALFTDmSVYENVAFPIRAhTKLSENLIAELvalkLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPDL 170
Cdd:cd03226 74 GYVMQDvdYQLFTD-SVREELLLGLKE-LDAGNEQAETV----LKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
7D06_B 171 IMYDEPFAGQDPIVKGVLTRLIRSLREAlDLTTIIVSHDVPETLSIADYIYVVAEGKI 228
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
13-193 |
4.84e-34 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 122.22 E-value: 4.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 13 LIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMsRQELFAARARM 92
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQ-RDEYHQDLLYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 93 GMLfqsGALFTDMSVYENVAFPIRAHTKLSENLIAELvalkLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPDLIM 172
Cdd:PRK13538 80 GHQ---PGIKTELTALENLRFYQRLHGPGDDEALWEA----LAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWI 152
|
170 180
....*....|....*....|...
7D06_B 173 YDEPFAGQDpiVKGV--LTRLIR 193
Cdd:PRK13538 153 LDEPFTAID--KQGVarLEALLA 173
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
2-237 |
4.91e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 124.09 E-value: 4.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 2 MNNKTPLstqslIEVKNLSF--NRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQ 79
Cdd:PRK13648 1 MEDKNSI-----IVFKNVSFqyQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 80 MSRQELfaaRARMGMLFQSGA-LFTDMSVYENVAFPIRAHTKLSENLIaELVALKLESVGLRGTEQLMPTELSGGMNRRV 158
Cdd:PRK13648 76 DNFEKL---RKHIGIVFQNPDnQFVGSIVKYDVAFGLENHAVPYDEMH-RRVSEALKQVDMLERADYEPNALSGGQKQRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
7D06_B 159 ALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSiADYIYVVAEGKIQGEGTPEEL 237
Cdd:PRK13648 152 AIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEI 229
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-228 |
7.27e-34 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 123.25 E-value: 7.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 2 MNNKTPLStqslieVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEvLLDGkdiaqms 81
Cdd:PRK11247 7 LNQGTPLL------LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE-LLAG------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 82 RQELFAARARMGMLFQSGALFTDMSVYENVAFPIRAHTKlsenlIAELVALklESVGLRGTEQLMPTELSGGMNRRVALA 161
Cdd:PRK11247 73 TAPLAEAREDTRLMFQDARLLPWKKVIDNVGLGLKGQWR-----DAALQAL--AAVGLADRANEWPAALSGGQKQRVALA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
7D06_B 162 RAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKI 228
Cdd:PRK11247 146 RALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
15-228 |
1.00e-33 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 120.61 E-value: 1.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 15 EVKNLSFNRGERviydNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQElfAARARMGM 94
Cdd:cd03215 6 EVRGLSVKGAVR----DVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRD--AIRAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 95 L---FQSGALFTDMSVYENVAFPIRahtklsenliaelvalklesvglrgteqlmpteLSGGMNRRVALARAIALDPDLI 171
Cdd:cd03215 80 VpedRKREGLVLDLSVAENIALSSL---------------------------------LSGGNQQKVVLARWLARDPRVL 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
7D06_B 172 MYDEPFAGQDPIVKGVLTRLIRSLREAlDLTTIIVSHDVPETLSIADYIYVVAEGKI 228
Cdd:cd03215 127 ILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
14-228 |
1.11e-33 |
|
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: 120.40 E-value: 1.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRG--ERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELfaaRAR 91
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNEL---GDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 92 MGMLFQSGALFTDmSVYENVafpirahtklsenliaelvalklesvglrgteqlmpteLSGGMNRRVALARAIALDPDLI 171
Cdd:cd03246 78 VGYLPQDDELFSG-SIAENI--------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
7D06_B 172 MYDEPFAGQDPIVKGVLTRLIRSLREAlDLTTIIVSHDvPETLSIADYIYVVAEGKI 228
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALKAA-GATRIVIAHR-PETLASADRILVLEDGRV 173
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-219 |
1.41e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 122.84 E-value: 1.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGgQLVPDQGEVLLDGKdiAQMSRQELFAARA--- 90
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLN-RMNELESEVRVEGR--VEFFNQNIYERRVnln 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 91 ----RMGMLFQSGALFTdMSVYENVAFPIRA---HTKLSENLIAElVALKLESVGLRGTEQLMPT--ELSGGMNRRVALA 161
Cdd:PRK14258 85 rlrrQVSMVHPKPNLFP-MSVYDNVAYGVKIvgwRPKLEIDDIVE-SALKDADLWDEIKHKIHKSalDLSGGQQQRLCIA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
7D06_B 162 RAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADY 219
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDF 220
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
14-237 |
2.86e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 122.15 E-value: 2.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSF--NRGERVIyDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELfaaRAR 91
Cdd:PRK13647 5 IEVEDLHFryKDGTKAL-KGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWV---RSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 92 MGMLFQ--SGALFTdMSVYENVAF-PIraHTKLSENLIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDP 168
Cdd:PRK13647 81 VGLVFQdpDDQVFS-STVWDDVAFgPV--NMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
7D06_B 169 DLIMYDEPFAGQDPIVKGVLTRLIRSLREAlDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEEL 237
Cdd:PRK13647 158 DVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLL 225
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
14-237 |
3.44e-33 |
|
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: 120.79 E-value: 3.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSF--NRGERVIyDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELfaaRAR 91
Cdd:cd03254 3 IEFENVNFsyDEKKPVL-KDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSL---RSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 92 MGMLFQSGALFTDmSVYENVAFPIRAHTKLSENLIAELVAL-----KLE-----SVGLRGteqlmpTELSGGMNRRVALA 161
Cdd:cd03254 79 IGVVLQDTFLFSG-TIMENIRLGRPNATDEEVIEAAKEAGAhdfimKLPngydtVLGENG------GNLSQGERQLLAIA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
7D06_B 162 RAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREalDLTTIIVSHDvPETLSIADYIYVVAEGKIQGEGTPEEL 237
Cdd:cd03254 152 RAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHR-LSTIKNADKILVLDDGKIIEEGTHDEL 224
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
14-239 |
6.73e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 121.75 E-value: 6.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQmsrqelfAARARMG 93
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP-------EDRRRIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 94 MLFQSGALFTDMSVYENVAF--------PIRAHTKLSENL----IAELVALKLEsvglrgteqlmptELSGGMNRRVALA 161
Cdd:COG4152 75 YLPEERGLYPKMKVGEQLVYlarlkglsKAEAKRRADEWLerlgLGDRANKKVE-------------ELSKGNQQKVQLI 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
7D06_B 162 RAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREAldLTTIIVS-HDVPETLSIADYIYVVAEGKIQGEGTPEELQA 239
Cdd:COG4152 142 AALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAK--GTTVIFSsHQMELVEELCDRIVIINKGRKVLSGSVDEIRR 218
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
26-237 |
6.81e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 121.67 E-value: 6.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 26 RVIYDnISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDI-AQMSRQELFAARARMGMLFQ--SGALF 102
Cdd:PRK13634 21 RALYD-VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItAGKKNKKLKPLRKKVGIVFQfpEHQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 103 TDmSVYENVAF-PIRAHTKLSEnliAELVALK-LESVGLrgTEQLM---PTELSGGMNRRVALARAIALDPDLIMYDEPF 177
Cdd:PRK13634 100 EE-TVEKDICFgPMNFGVSEED---AKQKAREmIELVGL--PEELLarsPFELSGGQMRRVAIAGVLAMEPEVLVLDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 178 AGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEEL 237
Cdd:PRK13634 174 AGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
14-228 |
2.20e-32 |
|
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: 118.15 E-value: 2.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAqmsrqelFAARARMG 93
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD-------IAARNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 94 MLFQSGALFTDMSVYENVAFPIRAHtKLSENLIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPDLIMY 173
Cdd:cd03269 74 YLPEERGLYPKMKVIDQLVYLAQLK-GLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
7D06_B 174 DEPFAGQDPIVKGVLTRLIRSLREAlDLTTIIVSHDVPETLSIADYIYVVAEGKI 228
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
13-242 |
2.48e-32 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 123.98 E-value: 2.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 13 LIEVKNLSfnRGERViyDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQElfAARARM 92
Cdd:COG1129 256 VLEVEGLS--VGGVV--RDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRD--AIRAGI 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 93 GML----FQSGaLFTDMSVYENVAFP-IRAHTK---LSENLIAELVALKLESVGLR--GTEQLMpTELSGGMNRRVALAR 162
Cdd:COG1129 330 AYVpedrKGEG-LVLDLSIRENITLAsLDRLSRgglLDRRRERALAEEYIKRLRIKtpSPEQPV-GNLSGGNQQKVVLAK 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 163 AIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREAlDLTTIIVSHDVPETLSIADYIYVVAEGKIQGE-----GTPEEL 237
Cdd:COG1129 408 WLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIVGEldreeATEEAI 486
|
....*
7D06_B 238 QAYAS 242
Cdd:COG1129 487 MAAAT 491
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
13-237 |
2.64e-32 |
|
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: 124.14 E-value: 2.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 13 LIEVKNL-----SFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEV-LLDGKDIAQMSRQElF 86
Cdd:TIGR03269 279 IIKVRNVskryiSVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnVRVGDEWVDMTKPG-P 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 87 AARAR----MGMLFQSGALFTDMSVYENVAFPIrahtklSENLIAELVALK----LESVGL---RGTEQL--MPTELSGG 153
Cdd:TIGR03269 358 DGRGRakryIGILHQEYDLYPHRTVLDNLTEAI------GLELPDELARMKavitLKMVGFdeeKAEEILdkYPDELSEG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 154 MNRRVALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGT 233
Cdd:TIGR03269 432 ERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGD 511
|
....
7D06_B 234 PEEL 237
Cdd:TIGR03269 512 PEEI 515
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
14-228 |
4.26e-32 |
|
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: 117.69 E-value: 4.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSF--NRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELfaaRAR 91
Cdd:cd03245 3 IEFRNVSFsyPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADL---RRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 92 MGMLFQSGALFTDmSVYENVAFpirAHTKLSENLIaelvalkLESVGLRGTEQLMPT--------------ELSGGMNRR 157
Cdd:cd03245 80 IGYVPQDVTLFYG-TLRDNITL---GAPLADDERI-------LRAAELAGVTDFVNKhpngldlqigergrGLSGGQRQA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
7D06_B 158 VALARAIALDPDLIMYDEPFAGQDpivKGVLTRLIRSLREAL-DLTTIIVSHDvPETLSIADYIYVVAEGKI 228
Cdd:cd03245 149 VALARALLNDPPILLLDEPTSAMD---MNSEERLKERLRQLLgDKTLIIITHR-PSLLDLVDRIIVMDSGRI 216
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
11-237 |
4.46e-32 |
|
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: 118.26 E-value: 4.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 11 QSLIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQG-EVLLDGKDIAQMSRQELfaaR 89
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWEL---R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 90 ARMGMLfqSGALFTDMSVYENV-------AFP-IRAHTKLSENLIAELVALkLESVGLRGTEQLMPTELSGGMNRRVALA 161
Cdd:COG1119 78 KRIGLV--SPALQLRFPRDETVldvvlsgFFDsIGLYREPTDEQRERAREL-LELLGLAHLADRPFGTLSQGEQRRVLIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
7D06_B 162 RAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPEtlsIADYIY---VVAEGKIQGEGTPEEL 237
Cdd:COG1119 155 RALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEE---IPPGIThvlLLKDGRVVAAGPKEEV 230
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
30-237 |
5.09e-32 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 117.85 E-value: 5.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 30 DNISLNIRRGQITAIMGPSGTGKTT----LLRLIGGQLVPDQGEVLLDGKDIAQMS-RQELFAararmgMLFQS--GALF 102
Cdd:TIGR02770 3 QDLNLSLKRGEVLALVGESGSGKSLtclaILGLLPPGLTQTSGEILLDGRPLLPLSiRGRHIA------TIMQNprTAFN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 103 TDMSVYENVAFPIRAHTKLSENLIAELVAlKLESVGLRGTEQLM---PTELSGGMNRRVALARAIALDPDLIMYDEPFAG 179
Cdd:TIGR02770 77 PLFTMGNHAIETLRSLGKLSKQARALILE-ALEAVGLPDPEEVLkkyPFQLSGGMLQRVMIALALLLEPPFLIADEPTTD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
7D06_B 180 QDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEEL 237
Cdd:TIGR02770 156 LDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEI 213
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
9-237 |
6.52e-32 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 122.87 E-value: 6.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 9 STQSLIEVKNLS--FNRGERV--IYDNISLNIRRGQITAIMGPSGTGKT----TLLRLIGGQLVPDQGEVLLDGKDIAQM 80
Cdd:COG4172 2 MSMPLLSVEDLSvaFGQGGGTveAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 81 SRQELFAAR-ARMGMLFQ--SGALFTDMSVYENVAFPIRAHTKLS-ENLIAELVALkLESVGLRGTEQLM---PTELSGG 153
Cdd:COG4172 82 SERELRRIRgNRIAMIFQepMTSLNPLHTIGKQIAEVLRLHRGLSgAAARARALEL-LERVGIPDPERRLdayPHQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 154 MNRRVALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDvpetLSI----ADYIYVVAEGKIQ 229
Cdd:COG4172 161 QRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHD----LGVvrrfADRVAVMRQGEIV 236
|
....*...
7D06_B 230 GEGTPEEL 237
Cdd:COG4172 237 EQGPTAEL 244
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
5-237 |
9.88e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 119.18 E-value: 9.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 5 KTPLSTQSLIEVKNLS--FNR---GERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLdgKDI-- 77
Cdd:PRK13631 13 PNPLSDDIILRVKNLYcvFDEkqeNELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQV--GDIyi 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 78 ---AQMSRQELFAA----------RARMGMLFQ--SGALFTDmSVYENVAF-PIraHTKLSENLIAELVALKLESVGLRG 141
Cdd:PRK13631 91 gdkKNNHELITNPYskkiknfkelRRRVSMVFQfpEYQLFKD-TIEKDIMFgPV--ALGVKKSEAKKLAKFYLNKMGLDD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 142 TE-QLMPTELSGGMNRRVALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLReALDLTTIIVSHDVPETLSIADYI 220
Cdd:PRK13631 168 SYlERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAK-ANNKTVFVITHTMEHVLEVADEV 246
|
250
....*....|....*..
7D06_B 221 YVVAEGKIQGEGTPEEL 237
Cdd:PRK13631 247 IVMDKGKILKTGTPYEI 263
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
9-237 |
1.10e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 118.36 E-value: 1.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 9 STQSLIEVKNLSFN--RGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELF 86
Cdd:PRK13640 1 MKDNIVEFKHVSFTypDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 87 AARARMGMLFQS-GALFTDMSVYENVAFPIRaHTKLSENLIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIA 165
Cdd:PRK13640 81 DIREKVGIVFQNpDNQFVGATVGDDVAFGLE-NRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
7D06_B 166 LDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETlSIADYIYVVAEGKIQGEGTPEEL 237
Cdd:PRK13640 160 VEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEI 230
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
17-252 |
1.35e-31 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 120.13 E-value: 1.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 17 KNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGK---DIAQMSRQelfaararMG 93
Cdd:PRK11000 7 RNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmnDVPPAERG--------VG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 94 MLFQSGALFTDMSVYENVAFPIR-AHTKLSE-----NLIAELvaLKLESVGLRgteqlMPTELSGGMNRRVALARAIALD 167
Cdd:PRK11000 79 MVFQSYALYPHLSVAENMSFGLKlAGAKKEEinqrvNQVAEV--LQLAHLLDR-----KPKALSGGQRQRVAIGRTLVAE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 168 PDLIMYDEPFAGQDPIVKgVLTRL-IRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELQAY-ASPFV 245
Cdd:PRK11000 152 PSVFLLDEPLSNLDAALR-VQMRIeISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYpANRFV 230
|
....*..
7D06_B 246 KQFLtGS 252
Cdd:PRK11000 231 AGFI-GS 236
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
14-237 |
1.56e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 117.92 E-value: 1.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRGE------RVIYDnISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDI-AQMSRQELF 86
Cdd:PRK13649 3 INLQNVSYTYQAgtpfegRALFD-VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItSTSKNKDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 87 AARARMGMLFQ--SGALFtDMSVYENVAF-PIRAHTKLSEnliAELVAL-KLESVGLrgTEQLM---PTELSGGMNRRVA 159
Cdd:PRK13649 82 QIRKKVGLVFQfpESQLF-EETVLKDVAFgPQNFGVSQEE---AEALAReKLALVGI--SESLFeknPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
7D06_B 160 LARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREAlDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEEL 237
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
14-247 |
1.63e-31 |
|
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: 116.56 E-value: 1.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFN-RGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELfaaRARM 92
Cdd:cd03253 1 IEFENVTFAyDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSL---RRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 93 GMLFQSGALFTDmSVYENVAF--------PIRAHTKLSEnlIAELVaLKLES-----VGLRGteqlmpTELSGGMNRRVA 159
Cdd:cd03253 78 GVVPQDTVLFND-TIGYNIRYgrpdatdeEVIEAAKAAQ--IHDKI-MRFPDgydtiVGERG------LKLSGGEKQRVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 160 LARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREalDLTTIIVSHDVpETLSIADYIYVVAEGKIQGEGTPEELQA 239
Cdd:cd03253 148 IARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRL-STIVNADKIIVLKDGRIVERGTHEELLA 224
|
250
....*....|..
7D06_B 240 ----YASPFVKQ 247
Cdd:cd03253 225 kgglYAEMWKAQ 236
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
14-232 |
1.73e-31 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 114.72 E-value: 1.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRGE--RVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRqelfAARAR 91
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK----ALSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 92 MGMLFQSGALFtDMSVYENVafpirahtklsenliaelvalklesvGLRgteqlmpteLSGGMNRRVALARAIALDPDLI 171
Cdd:cd03247 77 ISVLNQRPYLF-DTTLRNNL--------------------------GRR---------FSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
7D06_B 172 MYDEPFAGQDPIVKGVLTRLIrsLREALDLTTIIVSHDVpETLSIADYIYVVAEGKIQGEG 232
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLI--FEVLKDKTLIWITHHL-TGIEHMDKILFLENGKIIMQG 178
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
24-237 |
2.55e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 117.53 E-value: 2.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 24 GERVIYDnISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQ-ELFAARARMGMLFQ--SGA 100
Cdd:PRK13643 18 ASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQkEIKPVRKKVGVVFQfpESQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 101 LFTDmSVYENVAFPIRaHTKLSENLIAELVALKLESVGL-RGTEQLMPTELSGGMNRRVALARAIALDPDLIMYDEPFAG 179
Cdd:PRK13643 97 LFEE-TVLKDVAFGPQ-NFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
7D06_B 180 QDPIVKGVLTRLIRSLREAlDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEEL 237
Cdd:PRK13643 175 LDPKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDV 231
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
9-219 |
3.70e-31 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 116.42 E-value: 3.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 9 STQSLIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLR-------LIGGQLVpdQGEVLLDGKDIAQmS 81
Cdd:PRK14243 6 GTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFRV--EGKVTFHGKNLYA-P 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 82 RQELFAARARMGMLFQSGALFTDmSVYENVAFPIR-----------AHTKLSENLIAELVALKLESVGLrgteqlmptEL 150
Cdd:PRK14243 83 DVDPVEVRRRIGMVFQKPNPFPK-SIYDNIAYGARingykgdmdelVERSLRQAALWDEVKDKLKQSGL---------SL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
7D06_B 151 SGGMNRRVALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREalDLTTIIVSHDVPETLSIADY 219
Cdd:PRK14243 153 SGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKE--QYTIIIVTHNMQQAARVSDM 219
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
14-239 |
4.33e-31 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 115.71 E-value: 4.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFN---RGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELfaaRA 90
Cdd:cd03249 1 IEFKNVSFRypsRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWL---RS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 91 RMGMLFQSGALFtDMSVYENVAF--------PIRAHTKLSE--NLIAELvALKLES-VGLRGteqlmpTELSGGMNRRVA 159
Cdd:cd03249 78 QIGLVSQEPVLF-DGTIAENIRYgkpdatdeEVEEAAKKANihDFIMSL-PDGYDTlVGERG------SQLSGGQKQRIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 160 LARAIALDPDLIMYDEPFAGQDP----IVKGVLTRLIRslrealDLTTIIVSHDVpETLSIADYIYVVAEGKIQGEGTPE 235
Cdd:cd03249 150 IARALLRNPKILLLDEATSALDAesekLVQEALDRAMK------GRTTIVIAHRL-STIRNADLIAVLQNGQVVEQGTHD 222
|
....
7D06_B 236 ELQA 239
Cdd:cd03249 223 ELMA 226
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-243 |
4.79e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 115.91 E-value: 4.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 9 STQSLIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQL------VPDQGEVLLDGKDIAQMSR 82
Cdd:PRK14246 6 SAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIeiydskIKVDGKVLYFGKDIFQIDA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 83 QELfaaRARMGMLFQSGALFTDMSVYENVAFPIRAHTKLSENLIAELVALKLESVGL----RGTEQLMPTELSGGMNRRV 158
Cdd:PRK14246 86 IKL---RKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 159 ALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREalDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELq 238
Cdd:PRK14246 163 TIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKN--EIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI- 239
|
....*
7D06_B 239 aYASP 243
Cdd:PRK14246 240 -FTSP 243
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
14-236 |
8.85e-31 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 115.11 E-value: 8.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELfaARaRMG 93
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQL--AR-RLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 94 MLFQSGALFTDMSVYENVAFPIRAHTKLSENLIAE---LVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPDL 170
Cdd:PRK11231 80 LLPQHHLTPEGITVRELVAYGRSPWLSLWGRLSAEdnaRVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
7D06_B 171 IMYDEPFAGQDPIVKGVLTRLIRSLREAlDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEE 236
Cdd:PRK11231 160 VLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEE 224
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
11-237 |
1.93e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 114.80 E-value: 1.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 11 QSLIEVKNLSF------NRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSrqE 84
Cdd:PRK13633 2 NEMIKCKNVSYkyesneESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEE--N 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 85 LFAARARMGMLFQS--GALFTDMsVYENVAF-PirahtklsENL------IAELVALKLESVGLRGTEQLMPTELSGGMN 155
Cdd:PRK13633 80 LWDIRNKAGMVFQNpdNQIVATI-VEEDVAFgP--------ENLgippeeIRERVDESLKKVGMYEYRRHAPHLLSGGQK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 156 RRVALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSiADYIYVVAEGKIQGEGTPE 235
Cdd:PRK13633 151 QRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPK 229
|
..
7D06_B 236 EL 237
Cdd:PRK13633 230 EI 231
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
18-243 |
4.64e-30 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 113.63 E-value: 4.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 18 NLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELFAARARMGMLFQ 97
Cdd:PRK10419 17 GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRDIQMVFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 98 S--GALFTDMSVYENVAFPIRAHTKLSENLIAELVALKLESVGLRGTE-QLMPTELSGGMNRRVALARAIALDPDLIMYD 174
Cdd:PRK10419 97 DsiSAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVlDKRPPQLSGGQLQRVCLARALAVEPKLLILD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
7D06_B 175 EPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELQAYASP 243
Cdd:PRK10419 177 EAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKLTFSSP 245
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
13-217 |
7.51e-30 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 112.87 E-value: 7.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 13 LIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSrqelfaarARM 92
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG--------AER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 93 GMLFQSGALFTDMSVYENVAFPIR-AHTKLSENLIAELVALKLesVGLRGTEQLMPTELSGGMNRRVALARAIALDPDLI 171
Cdd:PRK11248 73 GVVFQNEGLLPWRNVQDNVAFGLQlAGVEKMQRLEIAHQMLKK--VGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
7D06_B 172 MYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIA 217
Cdd:PRK11248 151 LLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMA 196
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-243 |
9.69e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 113.27 E-value: 9.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 18 NLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIggQLVPDQ-------GEVLLDGKDIaqMSRQELFAARA 90
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTL--NRMNDKvsgyrysGDVLLGGRSI--FNYRDVLEFRR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 91 RMGMLFQSGALFTdMSVYENVAFPIRAHTKLSENLIAELVALKLESVGL----RGTEQLMPTELSGGMNRRVALARAIAL 166
Cdd:PRK14271 102 RVGMLFQRPNPFP-MSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAV 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
7D06_B 167 DPDLIMYDEPFAGQDPIVKGVLTRLIRSLreALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELqaYASP 243
Cdd:PRK14271 181 NPEVLLLDEPTSALDPTTTEKIEEFIRSL--ADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL--FSSP 253
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
14-248 |
1.58e-29 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 111.64 E-value: 1.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDI---AQMSRQELFAARA 90
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 91 RMGMLFQSGALFTDMSVYEN-VAFPIRAhTKLSENLIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPD 169
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENlIEAPCKV-LGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
7D06_B 170 LIMYDEPFAGQDPIVKGVLTRLIRSLREAlDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEelqAYASPFVKQF 248
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEIIRELSQT-GITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDAS---HFTQPQTEAF 236
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
14-240 |
1.89e-29 |
|
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: 111.17 E-value: 1.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRG--ERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELfaaRAR 91
Cdd:cd03251 1 VEFKNVTFRYPgdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASL---RRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 92 MGMLFQSGALFTDmSVYENVAFPIR----------AHTKLSENLIAELVALKLESVGLRGteqlmpTELSGGMNRRVALA 161
Cdd:cd03251 78 IGLVSQDVFLFND-TVAENIAYGRPgatreeveeaARAANAHEFIMELPEGYDTVIGERG------VKLSGGQRQRIAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 162 RAIALDPDLIMYDEPFAGQDpivkGVLTRLI-RSLREAL-DLTTIIVSHDVpETLSIADYIYVVAEGKIQGEGTPEELQA 239
Cdd:cd03251 151 RALLKDPPILILDEATSALD----TESERLVqAALERLMkNRTTFVIAHRL-STIENADRIVVLEDGKIVERGTHEELLA 225
|
.
7D06_B 240 Y 240
Cdd:cd03251 226 Q 226
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
25-237 |
2.78e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 112.18 E-value: 2.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 25 ERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSR-QELFAARARMGMLFQ--SGAL 101
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdKYIRPVRKRIGMVFQfpESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 102 FTDmSVYENVAFPIRAHTKLSENLIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPDLIMYDEPFAGQD 181
Cdd:PRK13646 99 FED-TVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
7D06_B 182 PIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEEL 237
Cdd:PRK13646 178 PQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
10-218 |
2.81e-29 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 111.02 E-value: 2.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 10 TQSLIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIG--GQLVPD---QGEVLLDGKDIAQmSRQE 84
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPEvtiTGSIVYNGHNIYS-PRTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 85 LFAARARMGMLFQSGALFTdMSVYENVAFPIRAHTKLSENLIAELV--ALKLESVGLRGTEQLMPTE--LSGGMNRRVAL 160
Cdd:PRK14239 81 TVDLRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAVekSLKGASIWDEVKDRLHDSAlgLSGGQQQRVCI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
7D06_B 161 ARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREalDLTTIIVSHDVPETLSIAD 218
Cdd:PRK14239 160 ARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKD--DYTMLLVTRSMQQASRISD 215
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
14-237 |
6.33e-29 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 112.23 E-value: 6.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRqelfAARARMG 93
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARAR----LARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 94 MLFQSGALFTDMSVYEN-VAFP--IRAHTKLSENLIAELvalkLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPDL 170
Cdd:PRK13536 118 VVPQFDNLDLEFTVRENlLVFGryFGMSTREIEAVIPSL----LEFARLESKADARVSDLSGGMKRRLTLARALINDPQL 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
7D06_B 171 IMYDEPFAGQDPIVKGVLTRLIRSLReALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEEL 237
Cdd:PRK13536 194 LILDEPTTGLDPHARHLIWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-212 |
7.87e-29 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 109.42 E-value: 7.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 2 MNNKTPLstqslIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMS 81
Cdd:PRK10247 1 MQENSPL-----LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 82 RQelfAARARMGMLFQSGALFTDmSVYENVAFP--IRAHTKLSENLIAELVALKLESVGLrgteQLMPTELSGGMNRRVA 159
Cdd:PRK10247 76 PE---IYRQQVSYCAQTPTLFGD-TVYDNLIFPwqIRNQQPDPAIFLDDLERFALPDTIL----TKNIAELSGGEKQRIS 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
7D06_B 160 LARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPE 212
Cdd:PRK10247 148 LIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE 200
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-252 |
8.89e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 109.93 E-value: 8.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGG--QLVPD---QGEVLLDGKDIAQmSRQELFAA 88
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRllELNEEarvEGEVRLFGRNIYS-PDVDPIEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 89 RARMGMLFQSGALFTDMSVYENVAFPIRAHTKL-SENLIAELV--ALKLESVGLRGTEQL--MPTELSGGMNRRVALARA 163
Cdd:PRK14267 84 RREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVkSKKELDERVewALKKAALWDEVKDRLndYPSNLSGGQRQRLVIARA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 164 IALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREalDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELqaYASP 243
Cdd:PRK14267 164 LAMKPKILLMDEPTANIDPVGTAKIEELLFELKK--EYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKV--FENP 239
|
250
....*....|..
7D06_B 244 ---FVKQFLTGS 252
Cdd:PRK14267 240 eheLTEKYVTGA 251
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
14-223 |
9.67e-29 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 114.31 E-value: 9.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFN-RGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELfaaRARM 92
Cdd:TIGR02857 322 LEFSGVSVAyPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW---RDQI 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 93 GMLFQSGALFTDmSVYENVAFPIRAHTklsenliAELVALKLESVGLRGTEQLMP-----------TELSGGMNRRVALA 161
Cdd:TIGR02857 399 AWVPQHPFLFAG-TIAENIRLARPDAS-------DAEIREALERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLALA 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
7D06_B 162 RAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREAldLTTIIVSHDvPETLSIADYIYVV 223
Cdd:TIGR02857 471 RAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQG--RTVLLVTHR-LALAALADRIVVL 529
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
13-229 |
2.60e-28 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 112.85 E-value: 2.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 13 LIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLdgkdiaqmsrqelfAARARM 92
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL--------------GETVKI 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 93 GMLFQSGALF-TDMSVYENVAfpiRAHTKLSEnliAELVALkLESVGLRGTEQLMPTE-LSGGMNRRVALARAIALDPDL 170
Cdd:COG0488 381 GYFDQHQEELdPDKTVLDELR---DGAPGGTE---QEVRGY-LGRFLFSGDDAFKPVGvLSGGEKARLALAKLLLSPPNV 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
7D06_B 171 IMYDEPfagqdpivkgvlT-----RLIRSLREALDL---TTIIVSHDvPETL-SIADYIYVVAEGKIQ 229
Cdd:COG0488 454 LLLDEP------------TnhldiETLEALEEALDDfpgTVLLVSHD-RYFLdRVATRILEFEDGGVR 508
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
7-252 |
2.69e-28 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 112.88 E-value: 2.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 7 PLSTQS--LIEVKNLS---------FNR--GERVIYDNISLNIRRGQITAIMGPSGTGKTT----LLRLIggqlvPDQGE 69
Cdd:PRK15134 267 PLPEPAspLLDVEQLQvafpirkgiLKRtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 70 VLLDGKDIAQMSRQELFAARARMGMLFQ--SGALFTDMSVYENVAFPIRAHTK-LSENLIAELVALKLESVGLR-GTEQL 145
Cdd:PRK15134 342 IWFDGQPLHNLNRRQLLPVRHRIQVVFQdpNSSLNPRLNVLQIIEEGLRVHQPtLSAAQREQQVIAVMEEVGLDpETRHR 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 146 MPTELSGGMNRRVALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAE 225
Cdd:PRK15134 422 YPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQ 501
|
250 260
....*....|....*....|....*...
7D06_B 226 GKIQGEGTPEEL-QAYASPFVKQFLTGS 252
Cdd:PRK15134 502 GEVVEQGDCERVfAAPQQEYTRQLLALS 529
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
14-236 |
2.90e-28 |
|
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: 112.92 E-value: 2.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSF--NRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELfaaRAR 91
Cdd:COG4618 331 LSVENLTVvpPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREEL---GRH 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 92 MGMLFQSGALFtDMSVYENVA-FP-------IRAhtklsenliAELVA-----LKLES-----VGLRGteqlmpTELSGG 153
Cdd:COG4618 408 IGYLPQDVELF-DGTIAENIArFGdadpekvVAA---------AKLAGvhemiLRLPDgydtrIGEGG------ARLSGG 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 154 MNRRVALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREAlDLTTIIVSHDvPETLSIADYIYVVAEGKIQGEGT 233
Cdd:COG4618 472 QRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHR-PSLLAAVDKLLVLRDGRVQAFGP 549
|
...
7D06_B 234 PEE 236
Cdd:COG4618 550 RDE 552
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
14-248 |
5.68e-28 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 107.41 E-value: 5.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGK--DIAQ-MSRQELFAARA 90
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKtPSDKAIRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 91 RMGMLFQSGALFTDMSVYENVafpIRAHTK---LSENlIAELVALK-LESVGLRGTEQLMPTELSGGMNRRVALARAIAL 166
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNL---IEAPCRvlgLSKD-QALARAEKlLERLRLKPYADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 167 DPDLIMYDEPFAGQDPIVKGVLTRLIRSLREAlDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPeelQAYASPFVK 246
Cdd:PRK11124 159 EPQVLLFDEPTAALDPEITAQIVSIIRELAET-GITQVIVTHEVEVARKTASRVVYMENGHIVEQGDA---SCFTQPQTE 234
|
..
7D06_B 247 QF 248
Cdd:PRK11124 235 AF 236
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
16-176 |
5.95e-28 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 111.70 E-value: 5.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 16 VKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGkdiaqmsrqelfaaRARMGML 95
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK--------------GLRIGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 96 FQSGALFTDMSVYENVafpIRAHTKLSEnLIAELVAL-------------------------------KLESV----GLR 140
Cdd:COG0488 67 PQEPPLDDDLTVLDTV---LDGDAELRA-LEAELEELeaklaepdedlerlaelqeefealggweaeaRAEEIlsglGFP 142
|
170 180 190
....*....|....*....|....*....|....*..
7D06_B 141 GTEQLMP-TELSGGMNRRVALARAIALDPDLIMYDEP 176
Cdd:COG0488 143 EEDLDRPvSELSGGWRRRVALARALLSEPDLLLLDEP 179
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
14-237 |
8.58e-28 |
|
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: 106.80 E-value: 8.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRG--ERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELfaaRAR 91
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWL---RRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 92 MGMLFQSGALFtDMSVYENVAFP--------IRAHTKL--SENLIAELVALKLESVGLRGteqlmpTELSGGMNRRVALA 161
Cdd:cd03252 78 VGVVLQENVLF-NRSIRDNIALAdpgmsmerVIEAAKLagAHDFISELPEGYDTIVGEQG------AGLSGGQRQRIAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
7D06_B 162 RAIALDPDLIMYDEPFAGQDPIVKGVltrLIRSLREALD-LTTIIVSHDVpETLSIADYIYVVAEGKIQGEGTPEEL 237
Cdd:cd03252 151 RALIHNPRILIFDEATSALDYESEHA---IMRNMHDICAgRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGSHDEL 223
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
30-237 |
9.85e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 107.99 E-value: 9.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 30 DNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDI-AQMSRQELFAARARMGMLFQ--SGALFTDmS 106
Cdd:PRK13641 24 DNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItPETGNKNLKKLRKKVSLVFQfpEAQLFEN-T 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 107 VYENVAFPIRaHTKLSENLiAELVALK-LESVGLrgTEQLM---PTELSGGMNRRVALARAIALDPDLIMYDEPFAGQDP 182
Cdd:PRK13641 103 VLKDVEFGPK-NFGFSEDE-AKEKALKwLKKVGL--SEDLIsksPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
7D06_B 183 IVKGVLTRLIRSLREAlDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEEL 237
Cdd:PRK13641 179 EGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEI 232
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
14-194 |
1.01e-27 |
|
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: 105.52 E-value: 1.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMsRQELFAARARMG 93
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQ-RDEPHENILYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 94 mlfQSGALFTDMSVYENVAFPIRAHTKLSENLIAelvalKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPDLIMY 173
Cdd:TIGR01189 80 ---HLPGLKPELSALENLHFWAAIHGGAQRTIED-----ALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWIL 151
|
170 180
....*....|....*....|.
7D06_B 174 DEPFAGQDPIVKGVLTRLIRS 194
Cdd:TIGR01189 152 DEPTTALDKAGVALLAGLLRA 172
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
14-236 |
1.29e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 107.86 E-value: 1.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLS--FNRG---ERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEV---LLDGKDIAQMSRQEL 85
Cdd:PRK13651 3 IKVKNIVkiFNKKlptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 86 FAA------------------RARMGMLFQSG--ALFtDMSVYENVAF-PIRAHTKLSEnliAELVALK-LESVGL-RGT 142
Cdd:PRK13651 83 VLEklviqktrfkkikkikeiRRRVGVVFQFAeyQLF-EQTIEKDIIFgPVSMGVSKEE---AKKRAAKyIELVGLdESY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 143 EQLMPTELSGGMNRRVALARAIALDPDLIMYDEPFAGQDPivKGVLtrlirslrEALDL---------TTIIVSHDVPET 213
Cdd:PRK13651 159 LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDP--QGVK--------EILEIfdnlnkqgkTIILVTHDLDNV 228
|
250 260
....*....|....*....|...
7D06_B 214 LSIADYIYVVAEGKIQGEGTPEE 236
Cdd:PRK13651 229 LEWTKRTIFFKDGKIIKDGDTYD 251
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
32-252 |
1.69e-27 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 108.78 E-value: 1.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 32 ISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELFAArarmgMLFQSGALFTDMSVYENV 111
Cdd:PRK11650 23 IDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIA-----MVFQNYALYPHMSVRENM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 112 AF--PIRahtKLSENLIAELVAlklESVGLRGTEQLM---PTELSGGMNRRVALARAIALDPDLIMYDEPFAGQDPIVKg 186
Cdd:PRK11650 98 AYglKIR---GMPKAEIEERVA---EAARILELEPLLdrkPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLR- 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
7D06_B 187 VLTRL-IRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELQAY-ASPFVKQFLtGS 252
Cdd:PRK11650 171 VQMRLeIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKpASTFVASFI-GS 237
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
14-231 |
1.87e-27 |
|
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: 103.66 E-value: 1.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQElfAARARMG 93
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD--ARRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 94 MLFQsgalftdmsvyenvafpirahtklsenliaelvalklesvglrgteqlmpteLSGGMNRRVALARAIALDPDLIMY 173
Cdd:cd03216 79 MVYQ----------------------------------------------------LSVGERQMVEIARALARNARLLIL 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
7D06_B 174 DEPFAGQDPIVKGVLTRLIRSLREAlDLTTIIVSHDVPETLSIADYIYVVAEGKIQGE 231
Cdd:cd03216 107 DEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
14-237 |
2.30e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 107.02 E-value: 2.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRGERVIY-----DNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLL-DGKDIAQMSR-QELF 86
Cdd:PRK13645 7 IILDNVSYTYAKKTPFefkalNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgDYAIPANLKKiKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 87 AARARMGMLFQ--SGALFTDmSVYENVAF-PI-------RAHTKLSENLiaELVALKLESVglrgteQLMPTELSGGMNR 156
Cdd:PRK13645 87 RLRKEIGLVFQfpEYQLFQE-TIEKDIAFgPVnlgenkqEAYKKVPELL--KLVQLPEDYV------KRSPFELSGGQKR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 157 RVALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEE 236
Cdd:PRK13645 158 RVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFE 237
|
.
7D06_B 237 L 237
Cdd:PRK13645 238 I 238
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
15-235 |
2.52e-27 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 105.92 E-value: 2.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 15 EVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGG--QLVPDQGEVLLDGKDIAQMSRQElfaaRARM 92
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSILLDGEDILELSPDE----RARA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 93 GML--FQSGALFTDMSVYE--NVAFPIRAHTKLSENLIAELVALKLESVGlrgteqlMPTE---------LSGGMNRRVA 159
Cdd:COG0396 78 GIFlaFQYPVEIPGVSVSNflRTALNARRGEELSAREFLKLLKEKMKELG-------LDEDfldryvnegFSGGEKKRNE 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
7D06_B 160 LARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREAlDLTTIIVSHdVPETLSI--ADYIYVVAEGKIQGEGTPE 235
Cdd:COG0396 151 ILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSP-DRGILIITH-YQRILDYikPDFVHVLVDGRIVKSGGKE 226
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
14-237 |
2.90e-27 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 108.78 E-value: 2.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQElfaARARMG 93
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARA---ASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 94 MLFQSGALFTDMSVYENVAFPIRAH-TKLSENLIAELVALK--LESVGLRGTEQLMPTELSGGMNRRVALARAIALDPDL 170
Cdd:PRK09536 81 SVPQDTSLSFEFDVRQVVEMGRTPHrSRFDTWTETDRAAVEraMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
7D06_B 171 IMYDEPFAGQDpivkgvLTRLIRSLREALDL-----TTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEEL 237
Cdd:PRK09536 161 LLLDEPTASLD------INHQVRTLELVRRLvddgkTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV 226
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
14-209 |
3.65e-27 |
|
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: 109.76 E-value: 3.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNR-GERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELfaaRARM 92
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEV---RRRV 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 93 GMLFQSGALFtDMSVYENVAFpirAHTKLSEnliAELVALkLESVGL----RGTEQLMPTE-------LSGGMNRRVALA 161
Cdd:TIGR02868 412 SVCAQDAHLF-DTTVRENLRL---ARPDATD---EELWAA-LERVGLadwlRALPDGLDTVlgeggarLSGGERQRLALA 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
7D06_B 162 RAIALDPDLIMYDEPFAGQDPivkGVLTRLIRSLREALD-LTTIIVSHD 209
Cdd:TIGR02868 484 RALLADAPILLLDEPTEHLDA---ETADELLEDLLAALSgRTVVLITHH 529
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
10-237 |
3.70e-27 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 109.34 E-value: 3.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 10 TQSLIEVKNLS--FNrGERVIyDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQElfA 87
Cdd:COG1129 1 AEPLLEMRGISksFG-GVKAL-DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRD--A 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 88 ARARMGMLFQSGALFTDMSVYENVAF--PIRAHTKLSENLIAELVALKLESVGLRgteqLMPT----ELSGGMNRRVALA 161
Cdd:COG1129 77 QAAGIAIIHQELNLVPNLSVAENIFLgrEPRRGGLIDWRAMRRRARELLARLGLD----IDPDtpvgDLSVAQQQLVEIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 162 RAIALDPDLIMYDEPFAgqdpivkgVLT--------RLIRSLREAlDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGT 233
Cdd:COG1129 153 RALSRDARVLILDEPTA--------SLTereverlfRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGP 223
|
....
7D06_B 234 PEEL 237
Cdd:COG1129 224 VAEL 227
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
16-234 |
3.98e-27 |
|
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: 110.49 E-value: 3.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 16 VKNLS--FNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIaqmsRQELFAARARMG 93
Cdd:TIGR01257 931 VKNLVkiFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI----ETNLDAVRQSLG 1006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 94 MLFQSGALFTDMSVYENVAFPIRAHTKLSENLIAELVALkLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPDLIMY 173
Cdd:TIGR01257 1007 MCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAM-LEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVL 1085
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
7D06_B 174 DEPFAGQDPIVKGVLTRLIRSLREAldLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTP 234
Cdd:TIGR01257 1086 DEPTSGVDPYSRRSIWDLLLKYRSG--RTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
14-238 |
4.89e-27 |
|
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: 103.76 E-value: 4.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGqlVPD----QGEVLLDGKDIAQMSRQElfaaR 89
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG--HPKyevtEGEILFKGEDITDLPPEE----R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 90 ARMG--MLFQSGALFTDMSVyenvafpirahtklsENLIAELvalkleSVGlrgteqlmpteLSGGMNRRVALARAIALD 167
Cdd:cd03217 75 ARLGifLAFQYPPEIPGVKN---------------ADFLRYV------NEG-----------FSGGEKKRNEILQLLLLE 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
7D06_B 168 PDLIMYDEPFAGQDPIVKGVLTRLIRSLREAlDLTTIIVSH--DVPEtLSIADYIYVVAEGKIQGEGTPEELQ 238
Cdd:cd03217 123 PDLAILDEPDSGLDIDALRLVAEVINKLREE-GKSVLIITHyqRLLD-YIKPDRVHVLYDGRIVKSGDKELAL 193
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
24-231 |
7.85e-27 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 103.80 E-value: 7.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 24 GERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELFAARARMGMLFQSGALFT 103
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQIGMIFQDHHLLM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 104 DMSVYENVAFPIRAHTKLSENlIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPDLIMYDEPFAGQDPI 183
Cdd:PRK10908 93 DRTVYDNVAIPLIIAGASGDD-IRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
7D06_B 184 VKGVLTRLIRSLREaLDLTTIIVSHDVPETLSIADYIYVVAEGKIQGE 231
Cdd:PRK10908 172 LSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHLHGG 218
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
31-210 |
1.20e-26 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 103.74 E-value: 1.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 31 NISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRqelfAARA-----RMGMLFQSGALFTDM 105
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSS----AAKAelrnqKLGFIYQFHHLLPDF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 106 SVYENVAFPI--------RAHTKLSENLIAelvalklesVGLRGTEQLMPTELSGGMNRRVALARAIALDPDLIMYDEPF 177
Cdd:PRK11629 103 TALENVAMPLligkkkpaEINSRALEMLAA---------VGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPT 173
|
170 180 190
....*....|....*....|....*....|...
7D06_B 178 AGQDPIVKGVLTRLIRSLREALDLTTIIVSHDV 210
Cdd:PRK11629 174 GNLDARNADSIFQLLGELNRLQGTAFLVVTHDL 206
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
30-243 |
1.64e-26 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 105.56 E-value: 1.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 30 DNISLNIRRGQITAIMGPSGTGKTTLLRLIGGqLVP-DQGEVLLDGKDIAQMSRQELFAARARMGMLFQS--GALFTDMS 106
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIG-LVKaTDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFQDplASLNPRMT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 107 VYENVAFPIRA-HTKLSENLIAELVALKLESVGLRgtEQLM---PTELSGGMNRRVALARAIALDPDLIMYDEPFAGQDP 182
Cdd:PRK15079 117 IGEIIAEPLRTyHPKLSRQEVKDRVKAMMLKVGLL--PNLInryPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
7D06_B 183 IVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELqaYASP 243
Cdd:PRK15079 195 SIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV--YHNP 253
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
13-237 |
2.03e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 104.30 E-value: 2.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 13 LIEVKNLSFNRGERV-IYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRqeLFAARAR 91
Cdd:PRK13644 1 MIRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSK--LQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 92 MGMLFQSGAL-FTDMSVYENVAFPirahtklSENL------IAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAI 164
Cdd:PRK13644 79 VGIVFQNPETqFVGRTVEEDLAFG-------PENLclppieIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGIL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
7D06_B 165 ALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREAlDLTTIIVSHDVpETLSIADYIYVVAEGKIQGEGTPEEL 237
Cdd:PRK13644 152 TMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNL-EELHDADRIIVMDRGKIVLEGEPENV 222
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
13-246 |
3.42e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 103.63 E-value: 3.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 13 LIEVKNLSFN---RGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKdiaQMSRQELFAAR 89
Cdd:PRK13642 4 ILEVENLVFKyekESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE---LLTAENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 90 ARMGMLFQS-GALFTDMSVYENVAFPIRAHTKLSENLIAElVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDP 168
Cdd:PRK13642 81 RKIGMVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKR-VDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
7D06_B 169 DLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSiADYIYVVAEGKIQGEGTPEELQAYASPFVK 246
Cdd:PRK13642 160 EIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEDMVE 236
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
14-198 |
6.34e-26 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 101.10 E-value: 6.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIaqmsrqELFAARARMG 93
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI------DDPDVAEACH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 94 MLFQSGALFTDMSVYENVAFpiRAHTKLSENLIAELValkLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPDLIMY 173
Cdd:PRK13539 77 YLGHRNAMKPALTVAENLEF--WAAFLGGEELDIAAA---LEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWIL 151
|
170 180
....*....|....*....|....*
7D06_B 174 DEPFAGQDPIVKGVLTRLIRSLREA 198
Cdd:PRK13539 152 DEPTAALDAAAVALFAELIRAHLAQ 176
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
9-228 |
7.59e-26 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 102.31 E-value: 7.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 9 STQSLIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGK-----DIAQMSRQ 83
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 84 EL-FAARARMGMLFQSGALFTDMSVyenvafpiRAHTKLSENLIAelvalklesVGLRGTEQL----------------- 145
Cdd:PRK11701 82 ERrRLLRTEWGFVHQHPRDGLRMQV--------SAGGNIGERLMA---------VGARHYGDIratagdwlerveidaar 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 146 ---MPTELSGGMNRRVALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYV 222
Cdd:PRK11701 145 iddLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLV 224
|
....*.
7D06_B 223 VAEGKI 228
Cdd:PRK11701 225 MKQGRV 230
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
8-210 |
1.05e-25 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 101.01 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 8 LSTQSLIEVKNL--SFNRGERV--IYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQ 83
Cdd:PRK10584 1 MPAENIVEVHHLkkSVGQGEHElsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 84 ELFAARAR-MGMLFQSGALFTDMSVYENVAFP--IRAHtklSENLIAELVALKLESVGLRGTEQLMPTELSGGMNRRVAL 160
Cdd:PRK10584 81 ARAKLRAKhVGFVFQSFMLIPTLNALENVELPalLRGE---SSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVAL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
7D06_B 161 ARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDV 210
Cdd:PRK10584 158 ARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDL 207
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
14-228 |
2.17e-25 |
|
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: 99.16 E-value: 2.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFN------RGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVP--DQGEVLLDGKDIaqmsrqEL 85
Cdd:cd03213 4 LSFRNLTVTvksspsKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPL------DK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 86 FAARARMGMLFQSGALFTDMSVYENVAFpirahtklsenliaelvalkleSVGLRGteqlmpteLSGGMNRRVALARAIA 165
Cdd:cd03213 78 RSFRKIIGYVPQDDILHPTLTVRETLMF----------------------AAKLRG--------LSGGERKRVSIALELV 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
7D06_B 166 LDPDLIMYDEPFAGQDPIVKGVLTRLIRSLreALDLTTIIVS-HDVP-ETLSIADYIYVVAEGKI 228
Cdd:cd03213 128 SNPSLLFLDEPTSGLDSSSALQVMSLLRRL--ADTGRTIICSiHQPSsEIFELFDKLLLLSQGRV 190
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
13-237 |
2.60e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 104.34 E-value: 2.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 13 LIEVKNLSF--NRGERVIyDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRqelfAARA 90
Cdd:COG3845 257 VLEVENLSVrdDRGVPAL-KDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSP----RERR 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 91 RMGMLF-----QSGALFTDMSVYENVAF------PIRAHTKLSENLIAELVALKLESVGLR-GTEQLMPTELSGGMNRRV 158
Cdd:COG3845 332 RLGVAYipedrLGRGLVPDMSVAENLILgryrrpPFSRGGFLDRKAIRAFAEELIEEFDVRtPGPDTPARSLSGGNQQKV 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 159 ALARAIALDPDLIMYDEPFAGQDpiVKGVLT--RLIRSLREAlDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEE 236
Cdd:COG3845 412 ILARELSRDPKLLIAAQPTRGLD--VGAIEFihQRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAE 488
|
.
7D06_B 237 L 237
Cdd:COG3845 489 A 489
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-239 |
3.26e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 100.85 E-value: 3.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 13 LIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIaQMSRQELFAARARM 92
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRGLLALRQQV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 93 GMLFQ---SGALFTDMSvyENVAFPIRaHTKLSENLIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPD 169
Cdd:PRK13638 80 ATVFQdpeQQIFYTDID--SDIAFSLR-NLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQAR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 170 LIMYDEPFAGQDPIVKGVLTRLIRSLrEALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELQA 239
Cdd:PRK13638 157 YLLLDEPTAGLDPAGRTQMIAIIRRI-VAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
14-181 |
5.27e-25 |
|
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: 98.72 E-value: 5.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMsRQELFAARARMG 93
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQ-RDSIARGLLYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 94 mlfQSGALFTDMSVYENVAFPIRAHTKlsenliaELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPDLIMY 173
Cdd:cd03231 80 ---HAPGIKTTLSVLENLRFWHADHSD-------EQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWIL 149
|
....*...
7D06_B 174 DEPFAGQD 181
Cdd:cd03231 150 DEPTTALD 157
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
11-232 |
5.64e-25 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 99.90 E-value: 5.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 11 QSLIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKD-----IAQMSRQEL 85
Cdd:TIGR02323 1 KPLLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgaeleLYQLSEAER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 86 -FAARARMGMLFQSGA--LFTDMSVYENV-----AFPIRAHTKLSENLIAELVALKLEsvglRGTEQLMPTELSGGMNRR 157
Cdd:TIGR02323 81 rRLMRTEWGFVHQNPRdgLRMRVSAGANIgerlmAIGARHYGNIRATAQDWLEEVEID----PTRIDDLPRAFSGGMQQR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
7D06_B 158 VALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEG 232
Cdd:TIGR02323 157 LQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESG 231
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
17-237 |
5.72e-25 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 100.06 E-value: 5.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 17 KNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELfaARaRMGMLF 96
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEV--AR-RIGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 97 QSGALFTDMSVYENVAFPIRAHTKL-----SENliAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPDLI 171
Cdd:PRK10253 88 QNATTPGDITVQELVARGRYPHQPLftrwrKED--EEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIM 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
7D06_B 172 MYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEEL 237
Cdd:PRK10253 166 LLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-239 |
1.44e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 102.60 E-value: 1.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 3 NNKTPLSTQSLIEVKNLSF---NRGERVIyDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQ 79
Cdd:PRK11160 328 TTSTAAADQVSLTLNNVSFtypDQPQPVL-KGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIAD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 80 MSRQELfaaRARMGMLFQSGALFTDmSVYENVAfpIRAHTKLSENLIAelvalKLESVGLrgtEQLMPTE---------- 149
Cdd:PRK11160 407 YSEAAL---RQAISVVSQRVHLFSA-TLRDNLL--LAAPNASDEALIE-----VLQQVGL---EKLLEDDkglnawlgeg 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 150 ---LSGGMNRRVALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLreALDLTTIIVSHDVPEtLSIADYIYVVAEG 226
Cdd:PRK11160 473 grqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEH--AQNKTVLMITHRLTG-LEQFDRICVMDNG 549
|
250
....*....|...
7D06_B 227 KIQGEGTPEELQA 239
Cdd:PRK11160 550 QIIEQGTHQELLA 562
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
30-243 |
3.53e-24 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 99.27 E-value: 3.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 30 DNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELFAARARMGMLFQS--GALFTDMSV 107
Cdd:PRK11308 32 DGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQKIQIVFQNpyGSLNPRKKV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 108 YENVAFPIRAHTKLSENLIAELVALKLESVGLRgTE--QLMPTELSGGMNRRVALARAIALDPDLIMYDEPFAGQDPIVK 185
Cdd:PRK11308 112 GQILEEPLLINTSLSAAERREKALAMMAKVGLR-PEhyDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQ 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
7D06_B 186 GVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELqaYASP 243
Cdd:PRK11308 191 AQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQI--FNNP 246
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
30-236 |
2.39e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 98.56 E-value: 2.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 30 DNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQElfAARARMGMLFQSGALFTDMSVYE 109
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRD--AIALGIGMVHQHFMLVPNLTVAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 110 NVA--FPIRAHTKLSENLIAELVALKLESVGLrgteQLMPT----ELSGGMNRRVALARAIALDPDLIMYDEPFAgqdpi 183
Cdd:COG3845 100 NIVlgLEPTKGGRLDRKAARARIRELSERYGL----DVDPDakveDLSVGEQQRVEILKALYRGARILILDEPTA----- 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 184 vkgVLT-----RLIRSLRE--ALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEE 236
Cdd:COG3845 171 ---VLTpqeadELFEILRRlaAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAE 227
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
14-242 |
2.67e-23 |
|
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: 98.74 E-value: 2.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFN-RGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELfaaRARM 92
Cdd:COG5265 358 VRFENVSFGyDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASL---RAAI 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 93 GMLFQSGALFTDmSVYENVAFP--------IRAHTKLSEnlIAELVAL---KLES-VGLRGTEqlmpteLSGGMNRRVAL 160
Cdd:COG5265 435 GIVPQDTVLFND-TIAYNIAYGrpdaseeeVEAAARAAQ--IHDFIESlpdGYDTrVGERGLK------LSGGEKQRVAI 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 161 ARAIALDPDLIMYDEPFAGQDpivkgvlTRLIRSLREALDL-----TTIIVSHdvpeTLSI---ADYIYVVAEGKIQGEG 232
Cdd:COG5265 506 ARTLLKNPPILIFDEATSALD-------SRTERAIQAALREvargrTTLVIAH----RLSTivdADEILVLEAGRIVERG 574
|
250
....*....|....
7D06_B 233 TPEELQA----YAS 242
Cdd:COG5265 575 THAELLAqgglYAQ 588
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
6-239 |
3.78e-23 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 98.64 E-value: 3.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 6 TPLSTQSLIEVKNLSF---NRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSR 82
Cdd:TIGR00958 471 APLNLEGLIEFQDVSFsypNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDH 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 83 QELfaaRARMGMLFQSGALFTDmSVYENVAF--------PIRAHTKLS--ENLIAELVALKLESVGLRGteqlmpTELSG 152
Cdd:TIGR00958 551 HYL---HRQVALVGQEPVLFSG-SVRENIAYgltdtpdeEIMAAAKAAnaHDFIMEFPNGYDTEVGEKG------SQLSG 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 153 GMNRRVALARAIALDPDLIMYDEPFAGQDPIVKgvltRLIRSLREALDLTTIIVSHDVPeTLSIADYIYVVAEGKIQGEG 232
Cdd:TIGR00958 621 GQKQRIAIARALVRKPRVLILDEATSALDAECE----QLLQESRSRASRTVLLIAHRLS-TVERADQILVLKKGSVVEMG 695
|
....*..
7D06_B 233 TPEELQA 239
Cdd:TIGR00958 696 THKQLME 702
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
8-243 |
6.61e-23 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 97.55 E-value: 6.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 8 LSTQSLIEVKNLSFNRGERViyDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAqmSRQELFA 87
Cdd:PRK09700 260 LAHETVFEVRNVTSRDRKKV--RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS--PRSPLDA 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 88 ARARMGMLFQS---GALFTDMSVYENVA----------------FPIRAHTKLSENLiAELVALKLESVglrgtEQLMpT 148
Cdd:PRK09700 336 VKKGMAYITESrrdNGFFPNFSIAQNMAisrslkdggykgamglFHEVDEQRTAENQ-RELLALKCHSV-----NQNI-T 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 149 ELSGGMNRRVALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREAlDLTTIIVSHDVPETLSIADYIYVVAEGKI 228
Cdd:PRK09700 409 ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
250 260
....*....|....*....|.
7D06_B 229 ------QGEGTPEELQAYASP 243
Cdd:PRK09700 488 tqiltnRDDMSEEEIMAWALP 508
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
11-237 |
7.08e-23 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 94.31 E-value: 7.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 11 QSLIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQ---GEVLLDGKDIAQMSR--QEL 85
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagSHIELLGRTVQREGRlaRDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 86 FAARARMGMLFQSGALFTDMSVYENVAFPIRAHTKLSENLIAELVALK-------LESVGLRGTEQLMPTELSGGMNRRV 158
Cdd:PRK09984 82 RKSRANTGYIFQQFNLVNRLSVLENVLIGALGSTPFWRTCFSWFTREQkqralqaLTRVGMVHFAHQRVSTLSGGQQQRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
7D06_B 159 ALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEEL 237
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
14-241 |
1.07e-22 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 97.00 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSfnrGERViyDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELFAA----- 88
Cdd:PRK10762 258 LKVDNLS---GPGV--NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANgivyi 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 89 ---RARMGmlfqsgaLFTDMSVYENVAfpIRAHTKLSENLI-----AELVA----LKLESVGLRGTEQLMpTELSGGMNR 156
Cdd:PRK10762 333 sedRKRDG-------LVLGMSVKENMS--LTALRYFSRAGGslkhaDEQQAvsdfIRLFNIKTPSMEQAI-GLLSGGNQQ 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 157 RVALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREAlDLTTIIVSHDVPETLSIADYIYVVAEGKIQGE----- 231
Cdd:PRK10762 403 KVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRISGEftreq 481
|
250
....*....|
7D06_B 232 GTPEELQAYA 241
Cdd:PRK10762 482 ATQEKLMAAA 491
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
41-243 |
2.48e-22 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 94.56 E-value: 2.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 41 ITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGK---DIAQmsRQELFAARARMGMLFQSGALFTDMSVYENVAFPIRA 117
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAEK--GICLPPEKRRIGYVFQDARLFPHYKVRGNLRYGMAK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 118 HTKLSENLIaelvalklesVGLRGTEQLM---PTELSGGMNRRVALARAIALDPDLIMYDEPFAGQD-PIVKGVLTRLIR 193
Cdd:PRK11144 104 SMVAQFDKI----------VALLGIEPLLdryPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRKRELLPYLER 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
7D06_B 194 sLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELqaYASP 243
Cdd:PRK11144 174 -LAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEV--WASS 220
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
14-227 |
7.50e-22 |
|
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: 90.22 E-value: 7.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRGERVIYD-----NISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKdIAQMSrQE--LF 86
Cdd:cd03250 1 ISVEDASFTWDSGEQETsftlkDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-IAYVS-QEpwIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 87 AARARMGMLFqsGALFtDMSVYENVafpIRAhTKLSENLiAELVALKLESVGLRGteqlmpTELSGGMNRRVALARAIAL 166
Cdd:cd03250 79 NGTIRENILF--GKPF-DEERYEKV---IKA-CALEPDL-EILPDGDLTEIGEKG------INLSGGQKQRISLARAVYS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
7D06_B 167 DPDLIMYDEPFAGQDPIV-KGVLTRLIRSLReALDLTTIIVSHDVpETLSIADYIYVVAEGK 227
Cdd:cd03250 145 DADIYLLDDPLSAVDAHVgRHIFENCILGLL-LNNKTRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
14-239 |
9.44e-22 |
|
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: 94.10 E-value: 9.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGG--QLVPDQGEVL----------------LDGK 75
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIyhvalcekcgyverpsKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 76 --------------DIAQMSRQELFAARARMGMLFQ-SGALFTDMSVYENVafpIRAHTKLS-ENLIAELVALKL-ESVG 138
Cdd:TIGR03269 81 pcpvcggtlepeevDFWNLSDKLRRRIRKRIAIMLQrTFALYGDDTVLDNV---LEALEEIGyEGKEAVGRAVDLiEMVQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 139 LRGTEQLMPTELSGGMNRRVALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHdVPETLS-IA 217
Cdd:TIGR03269 158 LSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSH-WPEVIEdLS 236
|
250 260
....*....|....*....|..
7D06_B 218 DYIYVVAEGKIQGEGTPEELQA 239
Cdd:TIGR03269 237 DKAIWLENGEIKEEGTPDEVVA 258
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
24-218 |
1.31e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 89.22 E-value: 1.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 24 GERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLdgkdiaqmsrqelfAARARMGMLFQSGALFT 103
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRR--------------AGGARVAYVPQRSEVPD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 104 DM--SVYENVAFPIRAHTKLSENLIAE---LVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPDLIMYDEPFA 178
Cdd:NF040873 69 SLplTVRDLVAMGRWARRGLWRRLTRDdraAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTT 148
|
170 180 190 200
....*....|....*....|....*....|....*....|
7D06_B 179 GQDPIVKGVLTRLIRSLREAlDLTTIIVSHDvPETLSIAD 218
Cdd:NF040873 149 GLDAESRERIIALLAEEHAR-GATVVVVTHD-LELVRRAD 186
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
6-228 |
1.53e-21 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 89.84 E-value: 1.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 6 TPLSTQSLIEVKNLSF---NRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSR 82
Cdd:cd03248 4 APDHLKGIVKFQNVTFaypTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 83 QELfaaRARMGMLFQSGALFTDmSVYENVAFPIR----------AHTKLSENLIAELVALKLESVGLRGteqlmpTELSG 152
Cdd:cd03248 84 KYL---HSKVSLVGQEPVLFAR-SLQDNIAYGLQscsfecvkeaAQKAHAHSFISELASGYDTEVGEKG------SQLSG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
7D06_B 153 GMNRRVALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREalDLTTIIVSHDVpETLSIADYIYVVAEGKI 228
Cdd:cd03248 154 GQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPE--RRTVLVIAHRL-STVERADQILVLDGGRI 226
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
11-243 |
2.02e-21 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 90.62 E-value: 2.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 11 QSLIEVKNLS---------FNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKdiaQMS 81
Cdd:PRK15112 2 ETLLEVRNLSktfryrtgwFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDH---PLH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 82 RQELFAARARMGMLFQ--SGALFTDMSVYENVAFPIRAHTKLSENLIAELVALKLESVGLRGTE-QLMPTELSGGMNRRV 158
Cdd:PRK15112 79 FGDYSYRSQRIRMIFQdpSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHaSYYPHMLAPGQKQRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 159 ALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELq 238
Cdd:PRK15112 159 GLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADV- 237
|
....*
7D06_B 239 aYASP 243
Cdd:PRK15112 238 -LASP 241
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
32-251 |
3.49e-21 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 89.61 E-value: 3.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 32 ISLNIRRGQITAIMGPSGTGKTTLLRLIGGqLVPDQGEVLLDGKDIAQMSRQELfaARARMGMLFQSGALFTdMSVYENV 111
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQPLEAWSAAEL--ARHRAYLSQQQTPPFA-MPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 112 AF--PIRAHTKLSENLIAELValklESVGLrgTEQL--MPTELSGGMNRRVALARAI-----ALDPD--LIMYDEPFAGQ 180
Cdd:PRK03695 91 TLhqPDKTRTEAVASALNEVA----EALGL--DDKLgrSVNQLSGGEWQRVRLAAVVlqvwpDINPAgqLLLLDEPMNSL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
7D06_B 181 DPIVKGVLTRLIRSLrEALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEEL-------QAYASPFVKQFLTG 251
Cdd:PRK03695 165 DVAQQAALDRLLSEL-CQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVltpenlaQVFGVNFRRLDVEG 241
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
13-232 |
6.00e-21 |
|
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: 88.54 E-value: 6.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 13 LIEVKNLSFNRGERVI--YDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGkdIAQMSRQELFaaRA 90
Cdd:cd03267 19 LIGSLKSLFKRKYREVeaLKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG--LVPWKRRKKF--LR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 91 RMGMLF-QSGALFTDMSVYENVAF--------PIRAHTKLSEnlIAELVALklesvglrgtEQLMPT---ELSGGMNRRV 158
Cdd:cd03267 95 RIGVVFgQKTQLWWDLPVIDSFYLlaaiydlpPARFKKRLDE--LSELLDL----------EELLDTpvrQLSLGQRMRA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
7D06_B 159 ALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEG 232
Cdd:cd03267 163 EIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
21-228 |
7.85e-21 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 91.84 E-value: 7.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 21 FNRGERVIY--DNISLNIRRGQITAIMGPSGTGKTT----LLRLIGGQlvpdQGEVLLDGKDIAQMSRQELFAARARMGM 94
Cdd:PRK10261 330 LNRVTREVHavEKVSFDLWPGETLSLVGESGSGKSTtgraLLRLVESQ----GGEIIFNGQRIDTLSPGKLQALRRDIQF 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 95 LFQS--GALFTDMSVYENVAFPIRAHTKLSENLIAELVALKLESVGLRGTEQL-MPTELSGGMNRRVALARAIALDPDLI 171
Cdd:PRK10261 406 IFQDpyASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWrYPHEFSGGQRQRICIARALALNPKVI 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
7D06_B 172 MYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKI 228
Cdd:PRK10261 486 IADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQI 542
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
7-203 |
1.60e-20 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 86.83 E-value: 1.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 7 PLSTQSLIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQmsrqelf 86
Cdd:PRK13543 5 LHTAPPLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 87 AARAR-MGMLFQSGALFTDMSVYENVAFPIRAHTKLSENLIAELVALklesVGLRGTEQLMPTELSGGMNRRVALARaIA 165
Cdd:PRK13543 78 GDRSRfMAYLGHLPGLKADLSTLENLHFLCGLHGRRAKQMPGSALAI----VGLAGYEDTLVRQLSAGQKKRLALAR-LW 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
7D06_B 166 LDP-DLIMYDEPFAGQDP----IVKGVLTRLIRSLREALdLTT 203
Cdd:PRK13543 153 LSPaPLWLLDEPYANLDLegitLVNRMISAHLRGGGAAL-VTT 194
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
23-182 |
1.72e-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: 86.94 E-value: 1.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 23 RGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPD---QGEVLLDGKdiaQMSRQELfaaRARMGMLFQSG 99
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQ---PRKPDQF---QKCVAYVRQDD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 100 ALFTDMSVYENVAF--PIRAHTKLSENLIAELVALKLES-VGLRGTEQLMPTELSGGMNRRVALARAIALDPDLIMYDEP 176
Cdd:cd03234 91 ILLPGLTVRETLTYtaILRLPRKSSDAIRKKRVEDVLLRdLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
....*.
7D06_B 177 FAGQDP 182
Cdd:cd03234 171 TSGLDS 176
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
12-254 |
1.99e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 90.55 E-value: 1.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 12 SLIEVKNL--SFNRGERVI--YDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELFA 87
Cdd:PRK10535 3 ALLELKDIrrSYPSGEEQVevLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 88 -ARARMGMLFQSGALFTDMSVYENVAFP-IRAHTKLSENLiAELVALkLESVGLRGTEQLMPTELSGGMNRRVALARAIA 165
Cdd:PRK10535 83 lRREHFGFIFQRYHLLSHLTAAQNVEVPaVYAGLERKQRL-LRAQEL-LQRLGLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 166 LDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREAlDLTTIIVSHDvPETLSIADYIYVVAEGKI----------QGEGTPE 235
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHD-PQVAAQAERVIEIRDGEIvrnppaqekvNVAGGTE 238
|
250
....*....|....*....
7D06_B 236 ELQAYASPFvKQFLTGSAE 254
Cdd:PRK10535 239 PVVNTASGW-RQFVSGFRE 256
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
12-264 |
2.59e-20 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 87.09 E-value: 2.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 12 SLIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKdiaqmsrqelfaarAR 91
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK--------------LR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 92 MGMLFQSGALFTDMSVYENVAFPIRAHTKLSENLIAelvalkLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPDLI 171
Cdd:PRK09544 69 IGYVPQKLYLDTTLPLTVNRFLRLRPGTKKEDILPA------LKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 172 MYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVaEGKIQGEGTPEELQAYASpFVKQFLTG 251
Cdd:PRK09544 143 VLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPEVVSLHPE-FISMFGPR 220
|
250
....*....|...
7D06_B 252 SAEGPVEYQFSHQ 264
Cdd:PRK09544 221 GAEQLGIYRHHHN 233
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-249 |
3.49e-20 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 89.91 E-value: 3.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 2 MNNKTPLSTQSLIEVKNLSF----NRGERVIYDNISLNIRRGQITAIMGPSGTGKT----TLLRLI---GGQLvpDQGEV 70
Cdd:PRK10261 1 MPHSDELDARDVLAVENLNIafmqEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqaGGLV--QCDKM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 71 LLDGK-----DIAQMSRQELFAAR-ARMGMLFQS--GALFTDMSVYENVAFPIRAHTKLS-ENLIAELVALkLESVGLRG 141
Cdd:PRK10261 79 LLRRRsrqviELSEQSAAQMRHVRgADMAMIFQEpmTSLNPVFTVGEQIAESIRLHQGASrEEAMVEAKRM-LDQVRIPE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 142 TEQLM---PTELSGGMNRRVALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIAD 218
Cdd:PRK10261 158 AQTILsryPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIAD 237
|
250 260 270
....*....|....*....|....*....|..
7D06_B 219 YIYVVAEGKIQGEGTPEEL-QAYASPFVKQFL 249
Cdd:PRK10261 238 RVLVMYQGEAVETGSVEQIfHAPQHPYTRALL 269
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1-237 |
6.57e-20 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 86.38 E-value: 6.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 1 MMNNktPLSTQSLIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQM 80
Cdd:PRK10575 1 MQEY--TNHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 81 SrQELFAarARMGMLFQSGALFTDMSVYENVA---FPirAHTKLSENLIA--ELVALKLESVGLRGTEQLMPTELSGGMN 155
Cdd:PRK10575 79 S-SKAFA--RKVAYLPQQLPAAEGMTVRELVAigrYP--WHGALGRFGAAdrEKVEEAISLVGLKPLAHRLVDSLSGGER 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 156 RRVALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPE 235
Cdd:PRK10575 154 QRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPA 233
|
..
7D06_B 236 EL 237
Cdd:PRK10575 234 EL 235
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
13-239 |
1.32e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 84.93 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 13 LIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELFaaRARM 92
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIM--REAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 93 GMLFQSGALFTDMSVYENVA----FPIRAHTKLSENLIAELVALKLESVGLR-GTeqlmpteLSGGMNRRVALARAIALD 167
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAmggfFAERDQFQERIKWVYELFPRLHERRIQRaGT-------MSGGEQQMLAIGRALMSQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
7D06_B 168 PDLIMYDEPFAGQDPIVKGVLTRLIRSLREAlDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELQA 239
Cdd:PRK11614 156 PRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLA 226
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
21-232 |
1.48e-19 |
|
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: 84.51 E-value: 1.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 21 FNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAqmsrqeLFAararMGMLFQSga 100
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSS------LLG----LGGGFNP-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 101 lftDMSVYENVAFPIRAHtKLSENLIAELVALKLESVGLrGTEQLMPT-ELSGGMNRRVALARAIALDPDLIMYDEPFAG 179
Cdd:cd03220 98 ---ELTGRENIYLNGRLL-GLSRKEIDEKIDEIIEFSEL-GDFIDLPVkTYSSGMKARLAFAIATALEPDILLIDEVLAV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
7D06_B 180 QDPIVKGVLTRLIRSLREALDlTTIIVSHDVPETLSIADYIYVVAEGKIQGEG 232
Cdd:cd03220 173 GDAAFQEKCQRRLRELLKQGK-TVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
35-246 |
1.72e-19 |
|
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: 84.77 E-value: 1.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 35 NIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAqMSRQELFAArarmgmlfqsgalfTDMSVYENVAFP 114
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS-YKPQYIKAD--------------YEGTVRDLLSSI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 115 IRAHTKLS--ENLIAElvALKLESVglrgTEQLMPtELSGGMNRRVALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLI 192
Cdd:cd03237 86 TKDFYTHPyfKTEIAK--PLQIEQI----LDREVP-ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 193 RSLREALDLTTIIVSHDVpetlSIADYI---YVVAEGK--IQGEG-TPEELQAYASPFVK 246
Cdd:cd03237 159 RRFAENNEKTAFVVEHDI----IMIDYLadrLIVFEGEpsVNGVAnPPQSLRSGMNRFLK 214
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
22-240 |
1.78e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 84.75 E-value: 1.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 22 NRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGkdiaqmsrqelfaaraRMGMLFQSGAL 101
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG----------------RVSALLELGAG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 102 FT-DMSVYENVafpirahtklsenliaELVALKLesvGLRGTE--QLMP-----TEL-----------SGGMNRRVALAR 162
Cdd:COG1134 99 FHpELTGRENI----------------YLNGRLL---GLSRKEidEKFDeivefAELgdfidqpvktySSGMRARLAFAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 163 AIALDPDLIMYDEPFAGQDPI----VKGVLTRLIRSLRealdlTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEE-L 237
Cdd:COG1134 160 ATAVDPDILLVDEVLAVGDAAfqkkCLARIRELRESGR-----TVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEvI 234
|
...
7D06_B 238 QAY 240
Cdd:COG1134 235 AAY 237
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
23-237 |
2.11e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 87.41 E-value: 2.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 23 RGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPD---QGEVLLDGKdiaQMSRQELfaaRARMGMLFQSG 99
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGM---PIDAKEM---RAISAYVQQDD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 100 ALFTDMSVYENVAFpiRAHTKLSENLIA----ELVALKLESVGLR-------GTEQLMPTeLSGGMNRRVALARAIALDP 168
Cdd:TIGR00955 109 LFIPTLTVREHLMF--QAHLRMPRRVTKkekrERVDEVLQALGLRkcantriGVPGRVKG-LSGGERKRLAFASELLTDP 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
7D06_B 169 DLIMYDEPFAGQDPIVKGVLTRLIRSLreALDLTTIIVSHDVP--ETLSIADYIYVVAEGKIQGEGTPEEL 237
Cdd:TIGR00955 186 PLLFCDEPTSGLDSFMAYSVVQVLKGL--AQKGKTIICTIHQPssELFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
14-227 |
2.15e-19 |
|
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: 82.11 E-value: 2.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDgkdiaqmsrqelfaARARMG 93
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG--------------STVKIG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 94 MLFQsgalftdmsvyenvafpirahtklsenliaelvalklesvglrgteqlmpteLSGGMNRRVALARAIALDPDLIMY 173
Cdd:cd03221 67 YFEQ----------------------------------------------------LSGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
7D06_B 174 DEPFAGQDPIVKGVLTRLIRSLREALdlttIIVSHDvpETL--SIADYIYVVAEGK 227
Cdd:cd03221 95 DEPTNHLDLESIEALEEALKEYPGTV----ILVSHD--RYFldQVATKIIELEDGK 144
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
3-256 |
3.88e-19 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 86.55 E-value: 3.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 3 NNKTPLSTQSLIEVKNLSF---NRGERViyDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQ 79
Cdd:PRK13657 324 GAIDLGRVKGAVEFDDVSFsydNSRQGV--EDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRT 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 80 MSRQELfaaRARMGMLFQSGALFtDMSVYEN--VAFP------IRAHTKLSENLiaELVALKLES----VGLRGTEqlmp 147
Cdd:PRK13657 402 VTRASL---RRNIAVVFQDAGLF-NRSIEDNirVGRPdatdeeMRAAAERAQAH--DFIERKPDGydtvVGERGRQ---- 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 148 teLSGGMNRRVALARAIALDPDLIMYDEPFAGQDpivkgVLTRliRSLREALDL-----TTIIVSHDVpETLSIADYIYV 222
Cdd:PRK13657 472 --LSGGERQRLAIARALLKDPPILILDEATSALD-----VETE--AKVKAALDElmkgrTTFIIAHRL-STVRNADRILV 541
|
250 260 270
....*....|....*....|....*....|....*...
7D06_B 223 VAEGKIQGEGTPEELQAYASPFVK----QFLTGSAEGP 256
Cdd:PRK13657 542 FDNGRVVESGSFDELVARGGRFAAllraQGMLQEDERR 579
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
11-226 |
5.09e-19 |
|
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: 83.25 E-value: 5.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 11 QSLIEVKNLS--F---NRGERVI--YDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGK----DIAQ 79
Cdd:COG4778 2 TTLLEVENLSktFtlhLQGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 80 MSRQELFAARAR-MGMLFQsgalFTD----MSVYENVAFPIRAHTklsenlIAELVALK-----LESVGLRgtE---QLM 146
Cdd:COG4778 82 ASPREILALRRRtIGYVSQ----FLRviprVSALDVVAEPLLERG------VDREEARArarelLARLNLP--ErlwDLP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 147 PTELSGGMNRRVALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREAldLTTII-VSHDVPETLSIADYIYVVAE 225
Cdd:COG4778 150 PATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR--GTAIIgIFHDEEVREAVADRVVDVTP 227
|
.
7D06_B 226 G 226
Cdd:COG4778 228 F 228
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
30-227 |
6.36e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 85.73 E-value: 6.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 30 DNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELFAarARMGMLFQSGALFTDMSVYE 109
Cdd:PRK11288 21 DDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALA--AGVAIIYQELHLVPEMTVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 110 NV---AFPIRAHTKLSENLIAElVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPDLIMYDEPFAGQDPIVKG 186
Cdd:PRK11288 99 NLylgQLPHKGGIVNRRLLNYE-AREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
7D06_B 187 VLTRLIRSLREalDLTTII-VSHDVPETLSIADYIYVVAEGK 227
Cdd:PRK11288 178 QLFRVIRELRA--EGRVILyVSHRMEEIFALCDAITVFKDGR 217
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
9-255 |
8.64e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 85.53 E-value: 8.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 9 STQSLIEVKNLS--FNRG--ERVIYDNISLNIRRGQITAIMGPSGTGKT----TLLRLI-GGQLVPDQGEVLLDGKDIAQ 79
Cdd:PRK15134 1 MTQPLLAIENLSvaFRQQqtVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLpSPPVVYPSGDIRFHGESLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 80 MSRQELFAARA-RMGMLFQS-----GALFT-DMSVYENVAFpiraHTKLS-ENLIAELVALkLESVGLRGTEQLM---PT 148
Cdd:PRK15134 81 ASEQTLRGVRGnKIAMIFQEpmvslNPLHTlEKQLYEVLSL----HRGMRrEAARGEILNC-LDRVGIRQAAKRLtdyPH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 149 ELSGGMNRRVALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGK- 227
Cdd:PRK15134 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRc 235
|
250 260
....*....|....*....|....*...
7D06_B 228 IQGEGTPEELQAYASPFVKQFLTGSAEG 255
Cdd:PRK15134 236 VEQNRAATLFSAPTHPYTQKLLNSEPSG 263
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
32-231 |
1.07e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 85.35 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 32 ISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQElfAARArmGMLF-----QSGALFTDMS 106
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRD--AIRA--GIMLcpedrKAEGIIPVHS 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 107 VYENVAFPIRAHTKLSENLI-----AELVALKLES--VGLRGTEQLMPTeLSGGMNRRVALARAIALDPDLIMYDEPFAG 179
Cdd:PRK11288 348 VADNINISARRHHLRAGCLInnrweAENADRFIRSlnIKTPSREQLIMN-LSGGNQQKAILGRWLSEDMKVILLDEPTRG 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
7D06_B 180 QDPIVKGVLTRLIRSLREAlDLTTIIVSHDVPETLSIADYIYVVAEGKIQGE 231
Cdd:PRK11288 427 IDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRIAGE 477
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
10-222 |
1.39e-18 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 81.93 E-value: 1.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 10 TQSLIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLV--PDQGEVLLDGKDIAQmsrqelfa 87
Cdd:COG2401 27 VAIVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFGR-------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 88 ararmgmlfqsgalftDMSVYENVAfpirahtklSENLIAELVALkLESVGLrGTEQLM---PTELSGGMNRRVALARAI 164
Cdd:COG2401 99 ----------------EASLIDAIG---------RKGDFKDAVEL-LNAVGL-SDAVLWlrrFKELSTGQKFRFRLALLL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 165 ALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSH--DVPETLSIADYIYV 222
Cdd:COG2401 152 AERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHhyDVIDDLQPDLLIFV 211
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
13-257 |
1.46e-18 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 82.95 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 13 LIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQL--------VPDQGEVLLDGKDIAQMSRQE 84
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggaprgARVTGDVTLNGEPLAAIDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 85 LFAARARMGMLFQSGALFtdmSVYENVAFPIRAHTKLSENLIAELVALKLESVGLRGTEQLMP---TELSGGMNRRVALA 161
Cdd:PRK13547 81 LARLRAVLPQAAQPAFAF---SAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGrdvTTLSGGELARVQFA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 162 RAIA---------LDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEG 232
Cdd:PRK13547 158 RVLAqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHG 237
|
250 260 270
....*....|....*....|....*....|..
7D06_B 233 TPEEL-------QAYASPfVKQFLTGSAEGPV 257
Cdd:PRK13547 238 APADVltpahiaRCYGFA-VRLVDAGDGVPPV 268
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
7-239 |
2.70e-18 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 84.38 E-value: 2.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 7 PLSTQSlIEVKNLSFN-RGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQEL 85
Cdd:PRK10790 335 PLQSGR-IDIDNVSFAyRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 86 faaRARMGMLFQSGALFTDmSVYENVAfpirahtkLSENLIAELVALKLESVGLRGTEQLMP-----------TELSGGM 154
Cdd:PRK10790 414 ---RQGVAMVQQDPVVLAD-TFLANVT--------LGRDISEEQVWQALETVQLAELARSLPdglytplgeqgNNLSVGQ 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 155 NRRVALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREAldlTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTP 234
Cdd:PRK10790 482 KQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREH---TTLVVIAHRLSTIVEADTILVLHRGQAVEQGTH 558
|
....*
7D06_B 235 EELQA 239
Cdd:PRK10790 559 QQLLA 563
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-228 |
8.31e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 82.79 E-value: 8.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 4 NKTPLSTQSLIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSrq 83
Cdd:PRK15439 2 QTSDTTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLT-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 84 elfAARA-RMGMLF--QSGALFTDMSVYENVAFPIRAHTKLS---ENLIAEL-VALKLESVG--LRGTEQLMptelsggm 154
Cdd:PRK15439 80 ---PAKAhQLGIYLvpQEPLLFPNLSVKENILFGLPKRQASMqkmKQLLAALgCQLDLDSSAgsLEVADRQI-------- 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
7D06_B 155 nrrVALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLReALDLTTIIVSHDVPETLSIADYIYVVAEGKI 228
Cdd:PRK15439 149 ---VEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELL-AQGVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
14-234 |
1.22e-17 |
|
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: 79.07 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSF--NRGERVIYDNISLNIRRGQITAIMGPSGTGKTT----LLRLIGgqlvPDQGEVLLDGKDIAQMSRQELfa 87
Cdd:cd03244 3 IEFKNVSLryRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLVE----LSSGSILIDGVDISKIGLHDL-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 88 aRARMGMLFQSGALFTDmSVYENVAfPIRAHTKLSENLIAELVALKLESVGLRGTEQLMPTE----LSGGMNRRVALARA 163
Cdd:cd03244 77 -RSRISIIPQDPVLFSG-TIRSNLD-PFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEggenLSVGQRQLLCLARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
7D06_B 164 IALDPDLIMYDEPFAGQDPIvkgvLTRLI-RSLREAL-DLTTIIVSHDVPetlSIADY--IYVVAEGKIQGEGTP 234
Cdd:cd03244 154 LLRKSKILVLDEATASVDPE----TDALIqKTIREAFkDCTVLTIAHRLD---TIIDSdrILVLDKGRVVEFDSP 221
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
14-272 |
1.62e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 82.09 E-value: 1.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFN---RGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVP-DQGEVLLDGK--DIAQMSRqeLFA 87
Cdd:PLN03130 615 ISIKNGYFSwdsKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPrSDASVVIRGTvaYVPQVSW--IFN 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 88 ARARMGMLFqsGALFtDMSVYENVafpIRAhTKLSENLiAELVALKLESVGLRGteqlmpTELSGGMNRRVALARAIALD 167
Cdd:PLN03130 693 ATVRDNILF--GSPF-DPERYERA---IDV-TALQHDL-DLLPGGDLTEIGERG------VNISGGQKQRVSMARAVYSN 758
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 168 PDLIMYDEPFAGQDPIV-KGVLTRLIRslREALDLTTIIVSHDVpETLSIADYIYVVAEGKIQGEGTPEELQAyASPFVK 246
Cdd:PLN03130 759 SDVYIFDDPLSALDAHVgRQVFDKCIK--DELRGKTRVLVTNQL-HFLSQVDRIILVHEGMIKEEGTYEELSN-NGPLFQ 834
|
250 260
....*....|....*....|....*...
7D06_B 247 QFL--TGSAEGPVEYQFSHQAYLDNEVR 272
Cdd:PLN03130 835 KLMenAGKMEEYVEENGEEEDDQTSSKP 862
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
14-209 |
4.81e-17 |
|
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: 80.36 E-value: 4.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLL-DGKDIAQM--SRQELFAARA 90
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETVKLAYVdqSRDALDPNKT 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 91 rmgmLFQ--SGALftDMSVYENVAFPIRAHtklsenliaelvalkLESVGLRGTEQLMPT-ELSGGMNRRVALARAIALD 167
Cdd:TIGR03719 403 ----VWEeiSGGL--DIIKLGKREIPSRAY---------------VGRFNFKGSDQQKKVgQLSGGERNRVHLAKTLKSG 461
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
7D06_B 168 PDLIMYDEPFAGQDpivkgVLTrlIRSLREALDL---TTIIVSHD 209
Cdd:TIGR03719 462 GNVLLLDEPTNDLD-----VET--LRALEEALLNfagCAVVISHD 499
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
30-231 |
6.64e-17 |
|
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: 79.87 E-value: 6.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 30 DNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLvPDQ--GEVLLDGKDIAqmSRQELFAARARMGMLFQS---GALFTD 104
Cdd:TIGR02633 277 DDVSFSLRRGEILGVAGLVGAGRTELVQALFGAY-PGKfeGNVFINGKPVD--IRNPAQAIRAGIAMVPEDrkrHGIVPI 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 105 MSVYENVAFPI--RAHTKLSENLIAELVALK--LESVGLRGTEQLMP-TELSGGMNRRVALARAIALDPDLIMYDEPFAG 179
Cdd:TIGR02633 354 LGVGKNITLSVlkSFCFKMRIDAAAELQIIGsaIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRG 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
7D06_B 180 QDPIVKGVLTRLIRSL-REALDLttIIVSHDVPETLSIADYIYVVAEGKIQGE 231
Cdd:TIGR02633 434 VDVGAKYEIYKLINQLaQEGVAI--IVVSSELAEVLGLSDRVLVIGEGKLKGD 484
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
14-250 |
8.23e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 79.89 E-value: 8.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRGE-RVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLvPDQGEVLLDGKDIAQMSRQELfaaRARM 92
Cdd:PRK11174 350 IEAEDLEILSPDgKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESW---RKHL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 93 GMLFQSGALFTDmSVYENVAFpirAHTKLSENLIAELVA-------LKLESVGLRGTEQLMPTELSGGMNRRVALARAIA 165
Cdd:PRK11174 426 SWVGQNPQLPHG-TLRDNVLL---GNPDASDEQLQQALEnawvsefLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALL 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 166 LDPDLIMYDEPFAGQDPIVKgvlTRLIRSLREA-LDLTTIIVSHDVpETLSIADYIYVVAEGKIQGEGTPEELQAYASPF 244
Cdd:PRK11174 502 QPCQLLLLDEPTASLDAHSE---QLVMQALNAAsRRQTTLMVTHQL-EDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLF 577
|
....*.
7D06_B 245 vKQFLT 250
Cdd:PRK11174 578 -ATLLA 582
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
9-247 |
9.22e-17 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 77.37 E-value: 9.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 9 STQSLIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQlvPD----QGEVLLDGKDIAQMSRQE 84
Cdd:CHL00131 3 KNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH--PAykilEGDILFKGESILDLEPEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 85 lfaaRARMGML--FQ--------SGALFTdMSVYENVafpiRAHTKLSE-NLIA--ELVALKLESVGLRgteqlmPTEL- 150
Cdd:CHL00131 81 ----RAHLGIFlaFQypieipgvSNADFL-RLAYNSK----RKFQGLPElDPLEflEIINEKLKLVGMD------PSFLs 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 151 -------SGGMNRRVALARAIALDPDLIMYDEPFAGQD----PIVKGVLTRLIRSlrealDLTTIIVSHdVPETLS--IA 217
Cdd:CHL00131 146 rnvnegfSGGEKKRNEILQMALLDSELAILDETDSGLDidalKIIAEGINKLMTS-----ENSIILITH-YQRLLDyiKP 219
|
250 260 270
....*....|....*....|....*....|...
7D06_B 218 DYIYVVAEGKIQGEGTPE---ELQAYASPFVKQ 247
Cdd:CHL00131 220 DYVHVMQNGKIIKTGDAElakELEKKGYDWLKQ 252
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-231 |
2.06e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 78.55 E-value: 2.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 3 NNKTPLSTQSLIEVKNLSfnrGERVIydNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSR 82
Cdd:PRK15439 258 NRRQQAAGAPVLTVEDLT---GEGFR--NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALST 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 83 qelfAARARMGMLF-----QSGALFTDMSVYENVA------FPIRAHTKlSENLIAELVALKLeSVGLRGTEQLMPTeLS 151
Cdd:PRK15439 333 ----AQRLARGLVYlpedrQSSGLYLDAPLAWNVCalthnrRGFWIKPA-RENAVLERYRRAL-NIKFNHAEQAART-LS 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 152 GGMNRRVALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLrEALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGE 231
Cdd:PRK15439 406 GGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSI-AAQNVAVLFISSDLEEIEQMADRVLVMHQGEISGA 484
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
15-237 |
2.07e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 78.43 E-value: 2.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 15 EVKNLS----FNRGERVIyDNISLNIRRGQITAIMGPSGTGKTTLLR-LIGGQLVPDQGEVLLDGKDIAQMSRQElfAAR 89
Cdd:PRK13549 261 EVRNLTawdpVNPHIKRV-DDVSFSLRRGEILGIAGLVGAGRTELVQcLFGAYPGRWEGEIFIDGKPVKIRNPQQ--AIA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 90 ARMGMLFQS---GALFTDMSVYENVAFP-IRAHTKLSE-NLIAELVALKLESVGLR---GTEQLMPTELSGGMNRRVALA 161
Cdd:PRK13549 338 QGIAMVPEDrkrDGIVPVMGVGKNITLAaLDRFTGGSRiDDAAELKTILESIQRLKvktASPELAIARLSGGNQQKAVLA 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
7D06_B 162 RAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREAlDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEEL 237
Cdd:PRK13549 418 KCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKLKGDLINHNL 492
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
14-239 |
3.12e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 78.24 E-value: 3.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELFAAR-ARM 92
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVCPRiAYM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 93 ----GmlfqsGALFTDMSVYENVAFpiraHTKL-------SENLIAELvalkLESVGL-----RgteqlmPT-ELSGGMN 155
Cdd:NF033858 82 pqglG-----KNLYPTLSVFENLDF----FGRLfgqdaaeRRRRIDEL----LRATGLapfadR------PAgKLSGGMK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 156 RRVALARAIALDPDLIMYDEPFAGQDPivkgvLTR-----LIRSLREALDLTTIIVShdvpeTLSI---ADYIYVVA--E 225
Cdd:NF033858 143 QKLGLCCALIHDPDLLILDEPTTGVDP-----LSRrqfweLIDRIRAERPGMSVLVA-----TAYMeeaERFDWLVAmdA 212
|
250
....*....|....
7D06_B 226 GKIQGEGTPEELQA 239
Cdd:NF033858 213 GRVLATGTPAELLA 226
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-234 |
7.57e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 76.77 E-value: 7.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 29 YDNISLN-----IRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKdIAqMSRQELFAArarmgmlfqsgalfT 103
Cdd:PRK13409 350 LGDFSLEveggeIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK-IS-YKPQYIKPD--------------Y 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 104 DMSVYENVAfpiRAHTKLSENLIAELVALKLesvglrGTEQLMP---TELSGGMNRRVALARAIALDPDLIMYDEPFAGQ 180
Cdd:PRK13409 414 DGTVEDLLR---SITDDLGSSYYKSEIIKPL------QLERLLDknvKDLSGGELQRVAIAACLSRDADLYLLDEPSAHL 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
7D06_B 181 DPIVKGVLTRLIRSLREALDLTTIIVSHDvpetLSIADYI---YVVAEGK--IQGEGTP 234
Cdd:PRK13409 485 DVEQRLAVAKAIRRIAEEREATALVVDHD----IYMIDYIsdrLMVFEGEpgKHGHASG 539
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
14-248 |
8.77e-16 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 76.60 E-value: 8.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNR--GERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELfaaRAR 91
Cdd:PRK11176 342 IEFRNVTFTYpgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASL---RNQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 92 MGMLFQSGALFTDmSVYENVAFPirAHTKLSENLIAELVAL--------KLES-----VGLRGteqlmpTELSGGMNRRV 158
Cdd:PRK11176 419 VALVSQNVHLFND-TIANNIAYA--RTEQYSREQIEEAARMayamdfinKMDNgldtvIGENG------VLLSGGQRQRI 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 159 ALARAIALDPDLIMYDEPFAGQDpivkgvlTRLIRSLREALDL-----TTIIVSHDVpETLSIADYIYVVAEGKIQGEGT 233
Cdd:PRK11176 490 AIARALLRDSPILILDEATSALD-------TESERAIQAALDElqknrTSLVIAHRL-STIEKADEILVVEDGEIVERGT 561
|
250
....*....|....*....
7D06_B 234 PEEL----QAYASPFVKQF 248
Cdd:PRK11176 562 HAELlaqnGVYAQLHKMQF 580
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
12-237 |
1.26e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 75.16 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 12 SLIEVKNLSFNRGE-----RVIyDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGqLVPDQGEVL-----LDGKDIAQMS 81
Cdd:PRK11022 2 ALLNVDKLSVHFGDesapfRAV-DRISYSVKQGEVVGIVGESGSGKSVSSLAIMG-LIDYPGRVMaekleFNGQDLQRIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 82 ---RQELFAARarMGMLFQSGalFTDMSVYENVAFPI----RAHTKLSENLIAELVALKLESVGLRGTE---QLMPTELS 151
Cdd:PRK11022 80 ekeRRNLVGAE--VAMIFQDP--MTSLNPCYTVGFQImeaiKVHQGGNKKTRRQRAIDLLNQVGIPDPAsrlDVYPHQLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 152 GGMNRRVALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGE 231
Cdd:PRK11022 156 GGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVET 235
|
....*.
7D06_B 232 GTPEEL 237
Cdd:PRK11022 236 GKAHDI 241
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
14-239 |
1.43e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 76.32 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLL-----DGKDIaqmsrqelfAA 88
Cdd:NF033858 267 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfgqpvDAGDI---------AT 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 89 RARMGMLFQSGALFTDMSVYENVAFpiraHTKL---SENLIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIA 165
Cdd:NF033858 338 RRRVGYMSQAFSLYGELTVRQNLEL----HARLfhlPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVI 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
7D06_B 166 LDPDLIMYDEPFAGQDPIVKGVLTRLIRSL-REalDLTTIIVS-HDVPEtlsiA---DYIYVVAEGKIQGEGTPEELQA 239
Cdd:NF033858 414 HKPELLILDEPTSGVDPVARDMFWRLLIELsRE--DGVTIFIStHFMNE----AercDRISLMHAGRVLASDTPAALVA 486
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
32-239 |
1.69e-15 |
|
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: 75.99 E-value: 1.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 32 ISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQ---ELFAArarmgmLFQSGALFTDMSVY 108
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREayrQLFSA------VFSDFHLFDRLLGL 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 109 ENVAFPIRAHtklsenliAELVALKLES-VGLRGTEqLMPTELSGGMNRRVALARAIALDPDLIMYDEPFAGQDPIVKGV 187
Cdd:COG4615 425 DGEADPARAR--------ELLERLELDHkVSVEDGR-FSTTDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFRRV 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
7D06_B 188 L-TRLIRSLReALDLTTIIVSHDvpET-LSIADYIYVVAEGKIQGEGTPEELQA 239
Cdd:COG4615 496 FyTELLPELK-ARGKTVIAISHD--DRyFDLADRVLKMDYGKLVELTGPAALAA 546
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
2-237 |
2.78e-15 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 74.38 E-value: 2.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 2 MNNKTPLSTQSLIEVKNLSFN----RGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPD---QGEVLLDG 74
Cdd:PRK09473 1 TVPLAQQQADALLDVKDLRVTfstpDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 75 KDIAQMSRQELFAARA-RMGMLFQS--GALFTDMSVYENVAFPIRAHTKLSENLIAELVALKLESVGLRGTEQLM---PT 148
Cdd:PRK09473 81 REILNLPEKELNKLRAeQISMIFQDpmTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMkmyPH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 149 ELSGGMNRRVALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKI 228
Cdd:PRK09473 161 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRT 240
|
....*....
7D06_B 229 QGEGTPEEL 237
Cdd:PRK09473 241 MEYGNARDV 249
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
31-249 |
2.96e-15 |
|
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: 75.72 E-value: 2.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 31 NISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELFAARARMGMLFqsgALFTDMSVYEN 110
Cdd:TIGR01271 444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMPGTIKDNIIF---GLSYDEYRYTS 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 111 VafpIRAhTKLSENLiaELVALKLESVGLRGTeqlmpTELSGGMNRRVALARAIALDPDLIMYDEPFAGQDPIV-KGVLT 189
Cdd:TIGR01271 521 V---IKA-CQLEEDI--ALFPEKDKTVLGEGG-----ITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTeKEIFE 589
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 190 RLIRSLreALDLTTIIVSHDVpETLSIADYIYVVAEGKIQGEGTPEELQAYASPFVKQFL 249
Cdd:TIGR01271 590 SCLCKL--MSNKTRILVTSKL-EHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLLL 646
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
14-239 |
4.63e-15 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 74.75 E-value: 4.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMsrqELFAARARMG 93
Cdd:PRK10789 316 VNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL---QLDSWRSRLA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 94 MLFQSGALFTDmSVYENVAFPIRAHTKLSENLIAELVA-----LKL-----ESVGLRGteqLMpteLSGGMNRRVALARA 163
Cdd:PRK10789 393 VVSQTPFLFSD-TVANNIALGRPDATQQEIEHVARLASvhddiLRLpqgydTEVGERG---VM---LSGGQKQRISIARA 465
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
7D06_B 164 IALDPDLIMYDEPFAGQDPIVKgvlTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELQA 239
Cdd:PRK10789 466 LLLNAEILILDDALSAVDGRTE---HQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQ 538
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
14-237 |
4.63e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 72.81 E-value: 4.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNrGERVIYDNISLNIRRGQITAIMGPSGTGKT-TLLRLIGgqLVP-----DQGEVLLDGKDIAQMSrqelfa 87
Cdd:PRK10418 5 IELRNIALQ-AAQPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALG--ILPagvrqTAGRVLLDGKPVAPCA------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 88 ARARmgmlfqsgalfTDMSVYEN--VAF-PIRA-HTKLSENLIA-------ELVALKLESVGLRGTE---QLMPTELSGG 153
Cdd:PRK10418 76 LRGR-----------KIATIMQNprSAFnPLHTmHTHARETCLAlgkpaddATLTAALEAVGLENAArvlKLYPFEMSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 154 MNRRVALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGT 233
Cdd:PRK10418 145 MLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGD 224
|
....
7D06_B 234 PEEL 237
Cdd:PRK10418 225 VETL 228
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
10-232 |
8.91e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 73.67 E-value: 8.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 10 TQSLIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQelFAAR 89
Cdd:PRK09700 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHK--LAAQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 90 ARMGMLFQSGALFTDMSVYENVaFPIRAHTK--LSENLI-----AELVALKLESVGLRGTEQLMPTELSGGMNRRVALAR 162
Cdd:PRK09700 80 LGIGIIYQELSVIDELTVLENL-YIGRHLTKkvCGVNIIdwremRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
7D06_B 163 AIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREalDLTTII-VSHDVPETLSIADYIYVVAEGKIQGEG 232
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRK--EGTAIVyISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
14-209 |
1.13e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 73.61 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLdGkDIAQMSRQElfaararmg 93
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-G-ETVKLAYVD--------- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 94 mlfQS-GALFTDMSVYENVA------------FPIRAHtklsenliaelvalkLESVGLRGTEQLMPT-ELSGGMNRRVA 159
Cdd:PRK11819 394 ---QSrDALDPNKTVWEEISggldiikvgnreIPSRAY---------------VGRFNFKGGDQQKKVgVLSGGERNRLH 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
7D06_B 160 LARAIALDPDLIMYDEPFAGQDpivkgVLTrlIRSLREALDL---TTIIVSHD 209
Cdd:PRK11819 456 LAKTLKQGGNVLLLDEPTNDLD-----VET--LRALEEALLEfpgCAVVISHD 501
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
14-209 |
1.29e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 73.08 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRGERVIYDN-ISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQE---LFAar 89
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGpINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDyrkLFS-- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 90 armgmlfqsgALFTDMSVYENVAFP--IRAHTKLSENLIAEL-VALKLESVGLRgteqLMPTELSGGMNRRVALARAIAL 166
Cdd:PRK10522 401 ----------AVFTDFHLFDQLLGPegKPANPALVEKWLERLkMAHKLELEDGR----ISNLKLSKGQKKRLALLLALAE 466
|
170 180 190 200
....*....|....*....|....*....|....*....|...
7D06_B 167 DPDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHD 209
Cdd:PRK10522 467 ERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD 509
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
14-249 |
1.42e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 73.52 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSF---NRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLI------------------------------- 59
Cdd:PTZ00265 1166 IEIMDVNFryiSRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehtndmtneqdyqgd 1245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 60 ------------------GGQ-----LVPDQGEVLLDGKDIAQMSRQELfaaRARMGMLFQSGALFtDMSVYENVAFPIR 116
Cdd:PTZ00265 1246 eeqnvgmknvnefsltkeGGSgedstVFKNSGKILLDGVDICDYNLKDL---RNLFSIVSQEPMLF-NMSIYENIKFGKE 1321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 117 AHTKLSENLIAELVALK--LESVGLRGTEQLMP--TELSGGMNRRVALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLI 192
Cdd:PTZ00265 1322 DATREDVKRACKFAAIDefIESLPNKYDTNVGPygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTI 1401
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
7D06_B 193 RSLREALDLTTIIVSHDVPeTLSIADYIYVVAEGK-----IQGEGTPEELQAYASPFVKQFL 249
Cdd:PTZ00265 1402 VDIKDKADKTIITIAHRIA-SIKRSDKIVVFNNPDrtgsfVQAHGTHEELLSVQDGVYKKYV 1462
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-234 |
1.73e-14 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 72.89 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 29 YDNISLN-----IRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKdIA---QMSRQElfaararmgmlfqsga 100
Cdd:COG1245 351 YGGFSLEveggeIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK-ISykpQYISPD---------------- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 101 lfTDMSVYENVAFPIRahTKLSENLIAELVALKLesvglrGTEQLMP---TELSGGMNRRVALARAIALDPDLIMYDEPF 177
Cdd:COG1245 414 --YDGTVEEFLRSANT--DDFGSSYYKTEIIKPL------GLEKLLDknvKDLSGGELQRVAIAACLSRDADLYLLDEPS 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
7D06_B 178 AGQDPIVKGVLTRLIRSLREALDLTTIIVSHDvpetLSIADYI---YVVAEGK--IQGEGTP 234
Cdd:COG1245 484 AHLDVEQRLAVAKAIRRFAENRGKTAMVVDHD----IYLIDYIsdrLMVFEGEpgVHGHASG 541
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
25-240 |
1.88e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 72.99 E-value: 1.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 25 ERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPD--QGEVLLDGKDIAQMSRQelfaaraRMGMLFQSGALF 102
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQILK-------RTGFVTQDDILY 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 103 TDMSVYENVAF----------PIRAHTKLSENLIAELVALKLES--VG---LRGteqlmpteLSGGMNRRVALARAIALD 167
Cdd:PLN03211 153 PHLTVRETLVFcsllrlpkslTKQEKILVAESVISELGLTKCENtiIGnsfIRG--------ISGGERKRVSIAHEMLIN 224
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
7D06_B 168 PDLIMYDEPFAGQDPIVKGVLTRLIRSLreALDLTTIIVSHDVPET--LSIADYIYVVAEGKIQGEGTPEELQAY 240
Cdd:PLN03211 225 PSLLILDEPTSGLDATAAYRLVLTLGSL--AQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGKGSDAMAY 297
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
31-254 |
1.89e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.45 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 31 NISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELFAARARMGMLFQSGALFTD----MS 106
Cdd:PRK15056 25 DASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQSEEVDWSFPVLVEdvvmMG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 107 VYENVAFPIRAHTKLSEnliaeLVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPDLIMYDEPFAGQDPIVKG 186
Cdd:PRK15056 105 RYGHMGWLRRAKKRDRQ-----IVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEA 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
7D06_B 187 VLTRLIRSLREAlDLTTIIVSHDVPETLSIADYIY-----VVAEGKIQGEGTPEEL-QAYASPFVKQFLTGSAE 254
Cdd:PRK15056 180 RIISLLRELRDE-GKTMLVSTHNLGSVTEFCDYTVmvkgtVLASGPTETTFTAENLeLAFSGVLRHVALNGSEE 252
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
13-219 |
2.31e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 69.98 E-value: 2.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 13 LIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIaqmsRQELFAARARM 92
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCTYQKQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 93 GMLFQSGALFTDMSVYENVAFPIraHTKLSENLIAELVAL-KLESV-----GLrgteqlmpteLSGGMNRRVALARAIAL 166
Cdd:PRK13540 77 CFVGHRSGINPYLTLRENCLYDI--HFSPGAVGITELCRLfSLEHLidypcGL----------LSSGQKRQVALLRLWMS 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
7D06_B 167 DPDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPetLSIADY 219
Cdd:PRK13540 145 KAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQDLP--LNKADY 195
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
14-234 |
2.61e-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: 2.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRG---ERVIyDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELfaaRA 90
Cdd:cd03369 7 IEVENLSVRYApdlPPVL-KNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL---RS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 91 RMGMLFQ-----SGALFTDMSVYEnvafpirahtKLSENLIAElvALKLESVGLrgteqlmptELSGGMNRRVALARAIA 165
Cdd:cd03369 83 SLTIIPQdptlfSGTIRSNLDPFD----------EYSDEEIYG--ALRVSEGGL---------NLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
7D06_B 166 LDPDLIMYDEPFAGQDPIVKGVLTRLIRSlrEALDLTTIIVSHDVPetlSIADY--IYVVAEGKIQGEGTP 234
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIRE--EFTNSTILTIAHRLR---TIIDYdkILVMDAGEVKEYDHP 207
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
31-249 |
2.71e-14 |
|
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: 71.04 E-value: 2.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 31 NISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELFAARARMGMLFqsgALFTDMSVYEN 110
Cdd:cd03291 55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIF---GVSYDEYRYKS 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 111 V-----------AFPIRAHTKLSENLIAelvalklesvglrgteqlmpteLSGGMNRRVALARAIALDPDLIMYDEPFAG 179
Cdd:cd03291 132 VvkacqleeditKFPEKDNTVLGEGGIT----------------------LSGGQRARISLARAVYKDADLYLLDSPFGY 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
7D06_B 180 QD-----PIVKGVLTRLIRSlrealdLTTIIVSHDVpETLSIADYIYVVAEGKIQGEGTPEELQAYASPFVKQFL 249
Cdd:cd03291 190 LDvftekEIFESCVCKLMAN------KTRILVTSKM-EHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKLM 257
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
13-272 |
3.99e-14 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 71.74 E-value: 3.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 13 LIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEV-LLDGKDIAQMSRQELFAARAr 91
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAQHQLEFLRA- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 92 mgmlfqsgalftDMSvyenvafPIRAHTKLSENLIAELVALKLESVGLRGTEQLMPTE-LSGGMNRRVALARAIALDPDL 170
Cdd:PRK10636 391 ------------DES-------PLQHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRrFSGGEKARLVLALIVWQRPNL 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 171 IMYDEPFAGQDPIVKGVLTRLIRSLREALdlttIIVSHDVPETLSIADYIYVVAEGKIQG-EGTPEELQAYASPFVKQFL 249
Cdd:PRK10636 452 LLLDEPTNHLDLDMRQALTEALIDFEGAL----VVVSHDRHLLRSTTDDLYLVHDGKVEPfDGDLEDYQQWLSDVQKQEN 527
|
250 260
....*....|....*....|...
7D06_B 250 TGSAEGPVEYQFSHQAYLDNEVR 272
Cdd:PRK10636 528 QTDEAPKENNANSAQARKDQKRR 550
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
14-249 |
4.48e-14 |
|
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: 71.90 E-value: 4.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFN--RGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKdIAQMSRQelfaarar 91
Cdd:TIGR00957 637 ITVHNATFTwaRDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-VAYVPQQ-------- 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 92 mgmlfqsgALFTDMSVYENVAFpiraHTKLSENLIAELvalkLESVGLRGTEQLMP----TE-------LSGGMNRRVAL 160
Cdd:TIGR00957 708 --------AWIQNDSLRENILF----GKALNEKYYQQV----LEACALLPDLEILPsgdrTEigekgvnLSGGQKQRVSL 771
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 161 ARAIALDPDLIMYDEPFAGQDPIV-KGVLTRLIRSLREALDLTTIIVSHDVpETLSIADYIYVVAEGKIQGEGTPEELQA 239
Cdd:TIGR00957 772 ARAVYSNADIYLFDDPLSAVDAHVgKHIFEHVIGPEGVLKNKTRILVTHGI-SYLPQVDVIIVMSGGKISEMGSYQELLQ 850
|
250
....*....|
7D06_B 240 YASPFVkQFL 249
Cdd:TIGR00957 851 RDGAFA-EFL 859
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
9-208 |
4.84e-14 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 71.76 E-value: 4.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 9 STQSLIEVKNLSFNRGE-RVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGqLVPD-QGEVLL-DGKDIaqmsrqeL 85
Cdd:COG4178 358 SEDGALALEDLTLRTPDgRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG-LWPYgSGRIARpAGARV-------L 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 86 FAA-RARMgmlfQSGALftdmsvYENVAFPiRAHTKLSEnliAELVALkLESVGL-----R-GTEQLMPTELSGGMNRRV 158
Cdd:COG4178 430 FLPqRPYL----PLGTL------REALLYP-ATAEAFSD---AELREA-LEAVGLghlaeRlDEEADWDQVLSLGEQQRL 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
7D06_B 159 ALARAIALDPDLIMYDEPFAGQDPivkGVLTRLIRSLREALDLTTII-VSH 208
Cdd:COG4178 495 AFARLLLHKPDWLFLDEATSALDE---ENEAALYQLLREELPGTTVIsVGH 542
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
14-237 |
6.69e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 70.50 E-value: 6.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLS-------------------FNRGERVIY--DNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLL 72
Cdd:COG4586 2 IEVENLSktyrvyekepglkgalkglFRREYREVEavDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 73 DGKDIAQmSRQELfaaRARMGMLF-QSGALFTDMSVYENVAFpIRAHTKLSENLIAELVAlklESVGLRGTEQLMPT--- 148
Cdd:COG4586 82 LGYVPFK-RRKEF---ARRIGVVFgQRSQLWWDLPAIDSFRL-LKAIYRIPDAEYKKRLD---ELVELLDLGELLDTpvr 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 149 ELSGGMNRRVALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDlTTIIV-SHDVPETLSIADYIYVVAEGK 227
Cdd:COG4586 154 QLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERG-TTILLtSHDMDDIEALCDRVIVIDHGR 232
|
250
....*....|
7D06_B 228 IQGEGTPEEL 237
Cdd:COG4586 233 IIYDGSLEEL 242
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
14-246 |
1.57e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 70.39 E-value: 1.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFN---RGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVP-DQGEVLLDGKDIAQMSRQELFAAR 89
Cdd:PLN03232 615 ISIKNGYFSwdsKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHaETSSVVIRGSVAYVPQVSWIFNAT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 90 ARMGMLFqsGALFTDMSVYENVAFpirahTKLSENLiaELVALK-LESVGLRGteqlmpTELSGGMNRRVALARAIALDP 168
Cdd:PLN03232 695 VRENILF--GSDFESERYWRAIDV-----TALQHDL--DLLPGRdLTEIGERG------VNISGGQKQRVSMARAVYSNS 759
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
7D06_B 169 DLIMYDEPFAGQDP-IVKGVLTRLIRSlrEALDLTTIIVSHDVpETLSIADYIYVVAEGKIQGEGTPEELQAYASPFVK 246
Cdd:PLN03232 760 DIYIFDDPLSALDAhVAHQVFDSCMKD--ELKGKTRVLVTNQL-HFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKK 835
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
14-208 |
2.44e-13 |
|
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: 66.41 E-value: 2.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRGE-RVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGqLVPdqgevlldgkdiaqmsrqelfAARARM 92
Cdd:cd03223 1 IELENLSLATPDgRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG-LWP---------------------WGSGRI 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 93 GMLFQSGALFtdmsvyenvafpIRAHTKLSENLIAELVALKLESVglrgteqlmpteLSGGMNRRVALARAIALDPDLIM 172
Cdd:cd03223 59 GMPEGEDLLF------------LPQRPYLPLGTLREQLIYPWDDV------------LSGGEQQRLAFARLLLHKPKFVF 114
|
170 180 190
....*....|....*....|....*....|....*..
7D06_B 173 YDEPFAGQDPivkGVLTRLIRSLREAldLTTII-VSH 208
Cdd:cd03223 115 LDEATSALDE---ESEDRLYQLLKEL--GITVIsVGH 146
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
13-237 |
2.73e-13 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 68.78 E-value: 2.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 13 LIEVKNLSFN----RGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGqLVPDQGEV-----LLDGKDIAQMS-- 81
Cdd:COG4170 3 LLDIRNLTIEidtpQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICG-ITKDNWHVtadrfRWNGIDLLKLSpr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 82 -RQELFaaRARMGMLFQSGALFTDMSvyenvafpIRAHTKLSENL----------------IAELVALkLESVGLRGTEQ 144
Cdd:COG4170 82 eRRKII--GREIAMIFQEPSSCLDPS--------AKIGDQLIEAIpswtfkgkwwqrfkwrKKRAIEL-LHRVGIKDHKD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 145 LM---PTELSGGMNRRVALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIY 221
Cdd:COG4170 151 IMnsyPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTIT 230
|
250
....*....|....*.
7D06_B 222 VVAEGKIQGEGTPEEL 237
Cdd:COG4170 231 VLYCGQTVESGPTEQI 246
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
10-227 |
8.42e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 67.65 E-value: 8.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 10 TQSLIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGqLVPD---QGEVLLDGKDIAQMSRQElf 86
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEIIFEGEELQASNIRD-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 87 AARARMGMLFQSGALFTDMSVYENV---------------AFPIRAHTKLSENLIAELVALKLESVGLrGTEQLmptels 151
Cdd:PRK13549 79 TERAGIAIIHQELALVKELSVLENIflgneitpggimdydAMYLRAQKLLAQLKLDINPATPVGNLGL-GQQQL------ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
7D06_B 152 ggmnrrVALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLReALDLTTIIVSHDVPETLSIADYIYVVAEGK 227
Cdd:PRK13549 152 ------VEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLK-AHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
12-176 |
2.42e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 66.51 E-value: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 12 SLIEVKN--LSFnrGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDgKDIAqMSRQELFAAR 89
Cdd:PRK11147 2 SLISIHGawLSF--SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE-QDLI-VARLQQDPPR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 90 ARMGmlfqsgalftdmSVYENVAFPI--------RAH-------TKLSENLIAELVALK------------------LES 136
Cdd:PRK11147 78 NVEG------------TVYDFVAEGIeeqaeylkRYHdishlveTDPSEKNLNELAKLQeqldhhnlwqlenrinevLAQ 145
|
170 180 190 200
....*....|....*....|....*....|....*....|
7D06_B 137 VGLRGTEQLmpTELSGGMNRRVALARAIALDPDLIMYDEP 176
Cdd:PRK11147 146 LGLDPDAAL--SSLSGGWLRKAALGRALVSNPDVLLLDEP 183
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
13-232 |
3.58e-12 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 64.43 E-value: 3.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 13 LIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGG--QLVPDQGEVLLDGKDIAQMSRQElfaaRA 90
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKGKDLLELSPED----RA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 91 RMG--MLFQ--------SGALFTDMSVyeNVAFPIRAHTKLSENLIAELVALKLESVGlrgteqlMPTEL---------S 151
Cdd:PRK09580 77 GEGifMAFQypveipgvSNQFFLQTAL--NAVRSYRGQEPLDRFDFQDLMEEKIALLK-------MPEDLltrsvnvgfS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 152 GGMNRRVALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREAlDLTTIIVSHdvpeTLSIADYI-----YVVAEG 226
Cdd:PRK09580 148 GGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDG-KRSFIIVTH----YQRILDYIkpdyvHVLYQG 222
|
....*.
7D06_B 227 KIQGEG 232
Cdd:PRK09580 223 RIVKSG 228
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
12-228 |
6.02e-12 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 65.65 E-value: 6.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 12 SLIEVKNLSFNR-GERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKdiaqmSRQELFAARA 90
Cdd:PLN03073 507 PIISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAK-----VRMAVFSQHH 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 91 RMGMLFQSGALFTDMSVYENV-AFPIRAHtklsenliaelvalkLESVGLRGTEQLMPT-ELSGGMNRRVALARAIALDP 168
Cdd:PLN03073 582 VDGLDLSSNPLLYMMRCFPGVpEQKLRAH---------------LGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKP 646
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
7D06_B 169 DLIMYDEPFAGQDpivkgvlTRLIRSLREALDL---TTIIVSHDVPETLSIADYIYVVAEGKI 228
Cdd:PLN03073 647 HILLLDEPSNHLD-------LDAVEALIQGLVLfqgGVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
13-227 |
6.55e-12 |
|
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: 65.23 E-value: 6.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 13 LIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGqLVPD---QGEVLLDGKDIAQMSRQElfAAR 89
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHgtwDGEIYWSGSPLKASNIRD--TER 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 90 ARMGMLFQSGALFTDMSVYENV----------------AFPIRAHTKLSE-NLIAELVALKLESVGLrGTEQLMptELSG 152
Cdd:TIGR02633 78 AGIVIIHQELTLVPELSVAENIflgneitlpggrmaynAMYLRAKNLLRElQLDADNVTRPVGDYGG-GQQQLV--EIAK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
7D06_B 153 GMNRRVALaraialdpdLIMyDEPFAGQDPIVKGVLTRLIRSLReALDLTTIIVSHDVPETLSIADYIYVVAEGK 227
Cdd:TIGR02633 155 ALNKQARL---------LIL-DEPSSSLTEKETEILLDIIRDLK-AHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
14-224 |
1.15e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 64.67 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFN---RGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDgkDIAQMSRQELFAARA 90
Cdd:PTZ00265 383 IQFKNVRFHydtRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKDINLKWWRS 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 91 RMGMLFQSGALFTDmSVYENVAFPI------------------------------RAHTKLSENLIA------ELVALKL 134
Cdd:PTZ00265 461 KIGVVSQDPLLFSN-SIKNNIKYSLyslkdlealsnyynedgndsqenknkrnscRAKCAGDLNDMSnttdsnELIEMRK 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 135 ESVGLRGTEQL--------------MP-----------TELSGGMNRRVALARAIALDPDLIMYDEPFAGQDPIVKGVLT 189
Cdd:PTZ00265 540 NYQTIKDSEVVdvskkvlihdfvsaLPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQ 619
|
250 260 270
....*....|....*....|....*....|....*
7D06_B 190 RLIRSLREALDLTTIIVSHDVpETLSIADYIYVVA 224
Cdd:PTZ00265 620 KTINNLKGNENRITIIIAHRL-STIRYANTIFVLS 653
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
30-239 |
1.34e-11 |
|
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: 64.65 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 30 DNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQmsrqELFAARARMGMLFQSGALFTDMSVYE 109
Cdd:TIGR01257 1956 DRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT----NISDVHQNMGYCPQFDAIDDLLTGRE 2031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 110 NVAFPIRAHTKLSENlIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPDLIMYDEPFAGQDPIVKGVLT 189
Cdd:TIGR01257 2032 HLYLYARLRGVPAEE-IEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLW 2110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
7D06_B 190 RLIRS-LREalDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELQA 239
Cdd:TIGR01257 2111 NTIVSiIRE--GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKS 2159
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
15-209 |
2.48e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.43 E-value: 2.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 15 EVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGK-DIAQMSRQelfaaRArmg 93
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKlEVAYFDQH-----RA--- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 94 mlfqsgALFTDMSVYENVA---------------------F---PIRAHTKLSenliaelvalklesvglrgteqlmptE 149
Cdd:PRK11147 393 ------ELDPEKTVMDNLAegkqevmvngrprhvlgylqdFlfhPKRAMTPVK--------------------------A 440
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
7D06_B 150 LSGGMNRRVALARaIALDP-DLIMYDEPFAGQDpivkgVLT-RLIRSLREALDLTTIIVSHD 209
Cdd:PRK11147 441 LSGGERNRLLLAR-LFLKPsNLLILDEPTNDLD-----VETlELLEELLDSYQGTVLLVSHD 496
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
14-229 |
2.52e-11 |
|
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: 62.56 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLS--FNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIgGQLVPDQGEVLLDGKDIAQMSRQELfaaRAR 91
Cdd:cd03289 3 MTVKDLTakYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAF-LRLLNTEGDIQIDGVSWNSVPLQKW---RKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 92 MGMLFQSGALFTDmsvyenvafPIRAHTKLSENLIAELVALKLESVGLRGTEQLMPTE-----------LSGGMNRRVAL 160
Cdd:cd03289 79 FGVIPQKVFIFSG---------TFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
7D06_B 161 ARAIALDPDLIMYDEPFAGQDPIVKGVLTrliRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQ 229
Cdd:cd03289 150 ARSVLSKAKILLLDEPSAHLDPITYQVIR---KTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVR 215
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
37-220 |
2.73e-11 |
|
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: 62.00 E-value: 2.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 37 RRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEvlLDGK----DIAQMSR----QELFAaRARMGmlfqsgalftDMSVY 108
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGK--FDDPpdwdEILDEFRgselQNYFT-KLLEG----------DVKVI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 109 ENVAF----PIRAHTKLSENL--------IAELV-ALKLESVGLRGTEQLmptelSGGMNRRVALARAIALDPDLIMYDE 175
Cdd:cd03236 91 VKPQYvdliPKAVKGKVGELLkkkdergkLDELVdQLELRHVLDRNIDQL-----SGGELQRVAIAAALARDADFYFFDE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
7D06_B 176 PFAGQDpiVKGVLT--RLIRSLREAlDLTTIIVSHDvpetLSIADYI 220
Cdd:cd03236 166 PSSYLD--IKQRLNaaRLIRELAED-DNYVLVVEHD----LAVLDYL 205
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
2-256 |
6.94e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 62.49 E-value: 6.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 2 MNNKTPLSTQSLIEVKNLSFNRGE---RVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDgKDIA 78
Cdd:PTZ00243 646 GHEATPTSERSAKTPKMKTDDFFElepKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-RSIA 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 79 QMSRQELFaararMGMLFQSGALFTDMSVYENVAFPIRAhtklsENLIAELVALK--LES-VGLRGteqlmpTELSGGMN 155
Cdd:PTZ00243 725 YVPQQAWI-----MNATVRGNILFFDEEDAARLADAVRV-----SQLEADLAQLGggLETeIGEKG------VNLSGGQK 788
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 156 RRVALARAIALDPDLIMYDEPFAGQDPIVKgvlTRLIRS-LREAL-DLTTIIVSHDVpETLSIADYIYVVAEGKIQGEGT 233
Cdd:PTZ00243 789 ARVSLARAVYANRDVYLLDDPLSALDAHVG---ERVVEEcFLGALaGKTRVLATHQV-HVVPRADYVVALGDGRVEFSGS 864
|
250 260
....*....|....*....|...
7D06_B 234 PEELQayASPFVKQFLTGSAEGP 256
Cdd:PTZ00243 865 SADFM--RTSLYATLAAELKENK 885
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
13-175 |
7.55e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 59.89 E-value: 7.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 13 LIEVKNLSFNRGERVIYDnISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELFAARARM 92
Cdd:PRK13541 1 MLSLHQLQFNIEQKNLFD-LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIGHNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 93 GmlfqsgaLFTDMSVYENVAFPIRAHTKlSENLIAELVALKLESVGLRGTeqlmpTELSGGMNRRVALARAIALDPDLIM 172
Cdd:PRK13541 80 G-------LKLEMTVFENLKFWSEIYNS-AETLYAAIHYFKLHDLLDEKC-----YSLSSGMQKIVAIARLIACQSDLWL 146
|
...
7D06_B 173 YDE 175
Cdd:PRK13541 147 LDE 149
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
14-70 |
1.75e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 61.06 E-value: 1.75e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
7D06_B 14 IEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEV 70
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
23-230 |
2.55e-10 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 58.77 E-value: 2.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 23 RGERVIYDNISLNIRRGqITAIMGPSGTGKTTLLRLIG----GQLVPDQGEVLLDGKDIAQMSRqelfaaRARMGMLFQS 98
Cdd:cd03240 7 RNIRSFHERSEIEFFSP-LTLIVGQNGAGKTTIIEALKyaltGELPPNSKGGAHDPKLIREGEV------RAQVKLAFEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 99 --GALFT---DMSVYENVAFpirAHTKLSENLIAElvalklesvglrgteqlMPTELSGG------MNRRVALARAIALD 167
Cdd:cd03240 80 anGKKYTitrSLAILENVIF---CHQGESNWPLLD-----------------MRGRCSGGekvlasLIIRLALAETFGSN 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
7D06_B 168 PDLIMYDEPFAGQDPI-VKGVLTRLIRSLREALDLTTIIVSHDvPETLSIADYIYVVAEGKIQG 230
Cdd:cd03240 140 CGILALDEPTTNLDEEnIEESLAEIIEERKSQKNFQLIVITHD-EELVDAADHIYRVEKDGRQK 202
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
33-241 |
2.61e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.41 E-value: 2.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 33 SLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELfaaRARMGMLFQSGAlfTDM-SVYE-- 109
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQL---QKLVSDEWQRNN--TDMlSPGEdd 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 110 ---NVAFPIRAHTKlSENLIAELVALklesvglRGTEQLMP---TELSGGMNRRVALARAIALDPDLIMYDEPFAGQDPI 183
Cdd:PRK10938 98 tgrTTAEIIQDEVK-DPARCEQLAQQ-------FGITALLDrrfKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
7D06_B 184 VKGVLTRLIRSLREAlDLTTIIVS---HDVPEtlsIADYIYVVAEGKIQGEGTPEELQAYA 241
Cdd:PRK10938 170 SRQQLAELLASLHQS-GITLVLVLnrfDEIPD---FVQFAGVLADCTLAETGEREEILQQA 226
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
5-242 |
2.80e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.13 E-value: 2.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 5 KTPLSTQSLIEVKNLSFNRGERViyDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQE 84
Cdd:PRK10982 242 KENKPGEVILEVRNLTSLRQPSI--RDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 85 L----FA----------ARARMGMLFQSgaLFTDMSVYENvAFPIRAHTKLSENLIAELVALKLESVGlrgtEQLMPTEL 150
Cdd:PRK10982 320 AinhgFAlvteerrstgIYAYLDIGFNS--LISNIRNYKN-KVGLLDNSRMKSDTQWVIDSMRVKTPG----HRTQIGSL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 151 SGGMNRRVALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREAlDLTTIIVSHDVPETLSIADYIYVVAEGKIQG 230
Cdd:PRK10982 393 SGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLVAG 471
|
250
....*....|....*..
7D06_B 231 -----EGTPEELQAYAS 242
Cdd:PRK10982 472 ivdtkTTTQNEILRLAS 488
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
31-226 |
3.02e-10 |
|
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: 58.50 E-value: 3.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 31 NISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSrQELFAARARMGMLFQS-GALFTDMSVYE 109
Cdd:cd03290 19 NINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPS-FEATRSRNRYSVAYAAqKPWLLNATVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 110 NVAFPiRAHTKLSENLIAELVALKLE----------SVGLRGteqlmpTELSGGMNRRVALARAIALDPDLIMYDEPFAG 179
Cdd:cd03290 98 NITFG-SPFNKQRYKAVTDACSLQPDidllpfgdqtEIGERG------INLSGGQRQRICVARALYQNTNIVFLDDPFSA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
7D06_B 180 QDPIVKGVLTR--LIRSLREAlDLTTIIVSHDVpETLSIADYIYVVAEG 226
Cdd:cd03290 171 LDIHLSDHLMQegILKFLQDD-KRTLVLVTHKL-QYLPHADWIIAMKDG 217
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
13-236 |
4.71e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 59.42 E-value: 4.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 13 LIEVKNLSF---NRGERVIYDNISLNIRRGQITAIMGPSGTGKTTL-LRLIG---GQLVpdQGEVLLDGKDIAQMSRQEL 85
Cdd:NF040905 257 VFEVKNWTVyhpLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELaMSVFGrsyGRNI--SGTVFKDGKEVDVSTVSDA 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 86 FAA--------RARMGmlfqsgaLFTDMSVYENVAFPirAHTKLSE----NLIAEL-VA--------LKLESVgLRGTEQ 144
Cdd:NF040905 335 IDAglayvtedRKGYG-------LNLIDDIKRNITLA--NLGKVSRrgviDENEEIkVAeeyrkkmnIKTPSV-FQKVGN 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 145 LmptelSGGMNRRVALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREAlDLTTIIVSHDVPETLSIADYIYVVA 224
Cdd:NF040905 405 L-----SGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAE-GKGVIVISSELPELLGMCDRIYVMN 478
|
250
....*....|..
7D06_B 225 EGKIQGEGTPEE 236
Cdd:NF040905 479 EGRITGELPREE 490
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
30-227 |
7.35e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.97 E-value: 7.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 30 DNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQElfAARARMGMLFQSGALFTDMSVYE 109
Cdd:PRK10982 15 DNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKE--ALENGISMVHQELNLVLQRSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 110 NV---AFPIRA----HTKLSENLIAELVALKLEsvglrgteqLMPTE----LSGGMNRRVALARAIALDPDLIMYDEPFA 178
Cdd:PRK10982 93 NMwlgRYPTKGmfvdQDKMYRDTKAIFDELDID---------IDPRAkvatLSVSQMQMIEIAKAFSYNAKIVIMDEPTS 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
7D06_B 179 GQDPIVKGVLTRLIRSLREAlDLTTIIVSHDVPETLSIADYIYVVAEGK 227
Cdd:PRK10982 164 SLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
17-195 |
7.46e-10 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 56.87 E-value: 7.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 17 KNLSF----NRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQ----LVpdQGEVLLDGKdiaqmSRQELFaa 88
Cdd:cd03232 7 KNLNYtvpvKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRktagVI--TGEILINGR-----PLDKNF-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 89 RARMGMLFQSGALFTDMSVYENVAFpirahtklsenliaelvalkleSVGLRGteqlmpteLSGGMNRRVALARAIALDP 168
Cdd:cd03232 78 QRSTGYVEQQDVHSPNLTVREALRF----------------------SALLRG--------LSVEQRKRLTIGVELAAKP 127
|
170 180
....*....|....*....|....*..
7D06_B 169 DLIMYDEPFAGQDPIVKGVLTRLIRSL 195
Cdd:cd03232 128 SILFLDEPTSGLDSQAAYNIVRFLKKL 154
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
30-238 |
1.07e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.48 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 30 DNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIA---QMSRQElfaarARMGMLFQSGALFTDMS 106
Cdd:PRK10762 21 SGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngPKSSQE-----AGIGIIHQELNLIPQLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 107 VYENVaFPIRAHTK-----LSENLIAELVALkLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPDLIMYDEPFAGQD 181
Cdd:PRK10762 96 IAENI-FLGREFVNrfgriDWKKMYAEADKL-LARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
7D06_B 182 PIVKGVLTRLIRSLREAlDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELQ 238
Cdd:PRK10762 174 DTETESLFRVIRELKSQ-GRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLT 229
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
30-227 |
2.08e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 57.49 E-value: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 30 DNISLNIRRGQITAIMGPSGTGKTTLLRLIGGqLVPD---QGEVLLDG-----KDIAQMSR-------QELfaararmgm 94
Cdd:NF040905 18 DDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHgsyEGEILFDGevcrfKDIRDSEAlgiviihQEL--------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 95 lfqsgALFTDMSVYENVaFPIRAHTK-------LSENLIAELvalkLESVGLRGTEQLMPTELSGGMNRRVALARAIALD 167
Cdd:NF040905 88 -----ALIPYLSIAENI-FLGNERAKrgvidwnETNRRAREL----LAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 168 PDLIMYDEPFAGQDPIVKGVLTRLIRSLREAlDLTTIIVSHDVPETLSIADYIYVVAEGK 227
Cdd:NF040905 158 VKLLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDGR 216
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
13-237 |
2.15e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 57.12 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 13 LIEVKNLSFN----RGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGqLVPDQGEVL-----LDGKDIAQMS-R 82
Cdd:PRK15093 3 LLDIRNLTIEfktsDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICG-VTKDNWRVTadrmrFDDIDLLRLSpR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 83 QELFAARARMGMLFQSGALFTDMSvyENV------AFP---------IRAHTKLSENLiaELvalkLESVGLRGTEQLM- 146
Cdd:PRK15093 82 ERRKLVGHNVSMIFQEPQSCLDPS--ERVgrqlmqNIPgwtykgrwwQRFGWRKRRAI--EL----LHRVGIKDHKDAMr 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 147 --PTELSGGMNRRVALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVA 224
Cdd:PRK15093 154 sfPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLY 233
|
250
....*....|...
7D06_B 225 EGKIQGEGTPEEL 237
Cdd:PRK15093 234 CGQTVETAPSKEL 246
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
24-176 |
2.16e-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: 57.64 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 24 GERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLdgkdiaqmsrqelfAARARMGMLFQSGALFT 103
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP--------------QPGIKVGYLPQEPQLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 104 DMSVYENVAF---PIRA--------HTKLSE------NLIAELVAL--KLESVGL----RGTEQLM-----P------TE 149
Cdd:TIGR03719 82 TKTVRENVEEgvaEIKDaldrfneiSAKYAEpdadfdKLAAEQAELqeIIDAADAwdldSQLEIAMdalrcPpwdadvTK 161
|
170 180
....*....|....*....|....*..
7D06_B 150 LSGGMNRRVALARAIALDPDLIMYDEP 176
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEP 188
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
10-248 |
3.00e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 57.61 E-value: 3.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 10 TQSLIEVKNLS--FNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIgGQLVPDQGEVLLDGKDIAQMSRQELfa 87
Cdd:TIGR01271 1214 SGGQMDVQGLTakYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSAL-LRLLSTEGEIQIDGVSWNSVTLQTW-- 1290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 88 aRARMGMLFQSGALFTDmSVYENvafpIRAHTKLSENLIAELValklESVGLRGTEQLMPTE-----------LSGGMNR 156
Cdd:TIGR01271 1291 -RKAFGVIPQKVFIFSG-TFRKN----LDPYEQWSDEEIWKVA----EEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQ 1360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 157 RVALARAIALDPDLIMYDEPFAGQDPIVKGVLTrliRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEE 236
Cdd:TIGR01271 1361 LMCLARSILSKAKILLLDEPSAHLDPVTLQIIR---KTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQK 1437
|
250
....*....|..
7D06_B 237 LQAYASPFVKQF 248
Cdd:TIGR01271 1438 LLNETSLFKQAM 1449
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
60-257 |
4.23e-09 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 56.95 E-value: 4.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 60 GGQLVPDQGEVLLDGKDIAQmsrqelfaararmgmlfqsgalFTDMSVYENVAFPIRAHTKLSENLIAELVaLK------ 133
Cdd:TIGR00630 413 GTRLKPEALAVTVGGKSIAD----------------------VSELSIREAHEFFNQLTLTPEEKKIAEEV-LKeirerl 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 134 --LESVGLrgtEQLMP----TELSGGMNRRVALARAIALDPDLIMY--DEPFAG---QDPivkgvlTRLIRSLREALDL- 201
Cdd:TIGR00630 470 gfLIDVGL---DYLSLsraaGTLSGGEAQRIRLATQIGSGLTGVLYvlDEPSIGlhqRDN------RRLINTLKRLRDLg 540
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
7D06_B 202 -TTIIVSHDvPETLSIADYI------------YVVAegkiqgEGTPEELQAYASPFVKQFLTGSAEGPV 257
Cdd:TIGR00630 541 nTLIVVEHD-EDTIRAADYVidigpgagehggEVVA------SGTPEEILANPDSLTGQYLSGRKKIEV 602
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
14-239 |
7.87e-09 |
|
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: 54.91 E-value: 7.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLS--FNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELfaaRAR 91
Cdd:cd03288 20 IKIHDLCvrYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTL---RSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 92 MGMLFQSGALFTDmsvyeNVAFPIRAHTKLSENLI---AELVALKLESVGLRGTEQLMPTE----LSGGMNRRVALARAI 164
Cdd:cd03288 97 LSIILQDPILFSG-----SIRFNLDPECKCTDDRLweaLEIAQLKNMVKSLPGGLDAVVTEggenFSVGQRQLFCLARAF 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
7D06_B 165 ALDPDLIMYDEPFAGQDPIVKGVLTRLIrsLREALDLTTIIVSHDVPETLSiADYIYVVAEGKIQGEGTPEELQA 239
Cdd:cd03288 172 VRKSSILIMDEATASIDMATENILQKVV--MTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLA 243
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
17-228 |
9.75e-09 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 54.19 E-value: 9.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 17 KNLSF----NRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPD---QGEVLLDGKDIAQmsrqelFAAR 89
Cdd:cd03233 7 RNISFttgkGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKE------FAEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 90 ARMGMLF--QSGALFTDMSVYENVAFPIRAhtKLSENliaelvalklesvgLRGteqlmpteLSGGMNRRVALARAIALD 167
Cdd:cd03233 81 YPGEIIYvsEEDVHFPTLTVRETLDFALRC--KGNEF--------------VRG--------ISGGERKRVSIAEALVSR 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
7D06_B 168 PDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTII-VSHDVPETLSIADYIYVVAEGKI 228
Cdd:cd03233 137 ASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVsLYQASDEIYDLFDKVLVLYEGRQ 198
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
17-195 |
1.23e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.50 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 17 KNLSFN----RGERVIYDNISLNIRRGQITAIMGPSGTGKTTLL-----RLIGGqlVPDQGEVLLDGKdiaqmSRQELFA 87
Cdd:TIGR00956 763 RNLTYEvkikKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLnvlaeRVTTG--VITGGDRLVNGR-----PLDSSFQ 835
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 88 arARMGMLFQSGALFTDMSVYENVAFPIR----AHTKLSENL-----IAELvaLKLES-----VGLRG----TEQlmpte 149
Cdd:TIGR00956 836 --RSIGYVQQQDLHLPTSTVRESLRFSAYlrqpKSVSKSEKMeyveeVIKL--LEMESyadavVGVPGeglnVEQ----- 906
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
7D06_B 150 lsggmNRRVALARAIALDPDLIMY-DEPFAGQDPIVKGVLTRLIRSL 195
Cdd:TIGR00956 907 -----RKRLTIGVELVAKPKLLLFlDEPTSGLDSQTAWSICKLMRKL 948
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
36-223 |
1.52e-08 |
|
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: 52.96 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 36 IRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIaqmsrqelfaararmgmlfqsgalftdmsvyenvafpi 115
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITP-------------------------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 116 rahtklsenliaelvALKLESVglrgteqlmptELSGGMNRRVALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSL 195
Cdd:cd03222 64 ---------------VYKPQYI-----------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRL 117
|
170 180
....*....|....*....|....*...
7D06_B 196 REALDLTTIIVSHDVPETLSIADYIYVV 223
Cdd:cd03222 118 SEEGKKTALVVEHDLAVLDYLSDRIHVF 145
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
24-176 |
2.83e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 54.35 E-value: 2.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 24 GERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLdgkdiaqmsrqelfAARARMGMLFQSGALFT 103
Cdd:PRK11819 18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARP--------------APGIKVGYLPQEPQLDP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 104 DMSVYENV--AFpirAHTK--------LSEN----------LIAELVAL--KLESVGL----RGTEQLM-----P----- 147
Cdd:PRK11819 84 EKTVRENVeeGV---AEVKaaldrfneIYAAyaepdadfdaLAAEQGELqeIIDAADAwdldSQLEIAMdalrcPpwdak 160
|
170 180 190
....*....|....*....|....*....|
7D06_B 148 -TELSGGMNRRVALARAIALDPDLIMYDEP 176
Cdd:PRK11819 161 vTKLSGGERRRVALCRLLLEKPDMLLLDEP 190
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
36-220 |
4.59e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.66 E-value: 4.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 36 IRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVllDGKDiaqmSRQELFAArarmgmlFQSGALFTDMS-VYENvafP 114
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDY--EEEP----SWDEVLKR-------FRGTELQNYFKkLYNG---E 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 115 IRAHTKLSE-NLIAELVALK----LESVGLRGT----------EQLMP---TELSGGMNRRVALARAIALDPDLIMYDEP 176
Cdd:PRK13409 160 IKVVHKPQYvDLIPKVFKGKvrelLKKVDERGKldevverlglENILDrdiSELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
7D06_B 177 FAGQDpiVKGVLT--RLIRSLreALDLTTIIVSHDvpetLSIADYI 220
Cdd:PRK13409 240 TSYLD--IRQRLNvaRLIREL--AEGKYVLVVEHD----LAVLDYL 277
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
13-209 |
8.14e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.97 E-value: 8.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 13 LIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDgkdiaqmsrqelfaARARM 92
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLD--------------PNERL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 93 GMLFQSGALFTDMSVYENVafpIRAHTKL----------------SEN---LIAELVALKLE---------------SVG 138
Cdd:PRK15064 67 GKLRQDQFAFEEFTVLDTV---IMGHTELwevkqerdriyalpemSEEdgmKVADLEVKFAEmdgytaearagelllGVG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
7D06_B 139 LrGTEQ---LMpTELSGGMNRRVALARAIALDPDLIMYDEPFAGQDpivkgvlTRLIRSLREAL---DLTTIIVSHD 209
Cdd:PRK15064 144 I-PEEQhygLM-SEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD-------INTIRWLEDVLnerNSTMIIISHD 211
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
38-217 |
1.10e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 50.06 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 38 RGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVL-LDGKDIAQMSRQELFAARARMGMLfqsgalftdmsvyenvafpir 116
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyIDGEDILEEVLDQLLLIIVGGKKA--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 117 ahtklsenliaelvalklesvglrgteqlmptELSGGMNRRVALARAIALDPDLIMYDEPFAGQDP-----IVKGVLTRL 191
Cdd:smart00382 60 --------------------------------SGSGELRLRLALALARKLKPDVLILDEITSLLDAeqealLLLLEELRL 107
|
170 180
....*....|....*....|....*.
7D06_B 192 IRSLREALDLTTIIVSHDVPETLSIA 217
Cdd:smart00382 108 LLLLKSEKNLTVILTTNDEKDLGPAL 133
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
11-212 |
1.71e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.94 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 11 QSLIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQ----------LVPDQ---GEVLLDGK-D 76
Cdd:PRK10938 258 EPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDhpqgysndltLFGRRrgsGETIWDIKkH 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 77 IAQMSRQELFAAR----ARMGMLfqSGaLFTDMSVYENVafPIRAHTKLSEnliaelvalKLESVGLRGTEQLMP-TELS 151
Cdd:PRK10938 338 IGYVSSSLHLDYRvstsVRNVIL--SG-FFDSIGIYQAV--SDRQQKLAQQ---------WLDILGIDKRTADAPfHSLS 403
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
7D06_B 152 GGMNRRVALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSH---DVPE 212
Cdd:PRK10938 404 WGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHhaeDAPA 467
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
37-223 |
1.76e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 51.71 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 37 RRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDG-KD--IAQMSRQELFAararmgmLFQsgalftdmSVYENvaf 113
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEPsWDevLKRFRGTELQD-------YFK--------KLANG--- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 114 PIRAHTKLSE-NLIAELVALK----LESVGLRGT----------EQLMP---TELSGGMNRRVALARAIALDPDLIMYDE 175
Cdd:COG1245 159 EIKVAHKPQYvDLIPKVFKGTvrelLEKVDERGKldelaeklglENILDrdiSELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
7D06_B 176 PFAGQDpiVKGVLT--RLIRSLREAlDLTTIIVSHDvpetLSI----ADYIYVV 223
Cdd:COG1245 239 PSSYLD--IYQRLNvaRLIRELAEE-GKYVLVVEHD----LAIldylADYVHIL 285
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
44-263 |
2.38e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.90 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 44 IMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELfaaRARMGMLFQSGALFT--------------DMSVYE 109
Cdd:PLN03232 1267 VVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDL---RRVLSIIPQSPVLFSgtvrfnidpfsehnDADLWE 1343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 110 NVAfpiRAHTKlsenliaelVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPDLIMYDEPFAGQDPIVKGVLT 189
Cdd:PLN03232 1344 ALE---RAHIK---------DVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQ 1411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
7D06_B 190 RLIRslREALDLTTIIVSHDVpETLSIADYIYVVAEGKIQGEGTPEELQAY-ASPFVKQFltgSAEGPVEYQFSH 263
Cdd:PLN03232 1412 RTIR--EEFKSCTMLVIAHRL-NTIIDCDKILVLSSGQVLEYDSPQELLSRdTSAFFRMV---HSTGPANAQYLS 1480
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
32-237 |
2.53e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 51.70 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 32 ISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELfaaRARMGMLFQSGALFtDMSVYENV 111
Cdd:PTZ00243 1329 VSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLREL---RRQFSMIPQDPVLF-DGTVRQNV 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 112 afpirahTKLSENLIAELVAlKLESVGLRG-----TEQLMPTELSGGMNRRVA------LARA-IALDPDLIMYDEPFAG 179
Cdd:PTZ00243 1405 -------DPFLEASSAEVWA-ALELVGLRErvaseSEGIDSRVLEGGSNYSVGqrqlmcMARAlLKKGSGFILMDEATAN 1476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 180 QDPivkgVLTRLIR-SLREALDLTTII-VSHDVpETLSIADYIYVVAEGKIQGEGTPEEL 237
Cdd:PTZ00243 1477 IDP----ALDRQIQaTVMSAFSAYTVItIAHRL-HTVAQYDKIIVMDHGAVAEMGSPREL 1531
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
14-237 |
2.55e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 51.48 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKN--LSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELfaaRAR 91
Cdd:TIGR00957 1285 VEFRNycLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDL---RFK 1361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 92 MGMLFQSGALFTDmSVYENVAfPIRAHTKlsenliaELVALKLESVGLRGTEQLMPTE-----------LSGGMNRRVAL 160
Cdd:TIGR00957 1362 ITIIPQDPVLFSG-SLRMNLD-PFSQYSD-------EEVWWALELAHLKTFVSALPDKldhecaeggenLSVGQRQLVCL 1432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
7D06_B 161 ARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREalDLTTIIVSHDVPetlSIADY--IYVVAEGKIQGEGTPEEL 237
Cdd:TIGR00957 1433 ARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFE--DCTVLTIAHRLN---TIMDYtrVIVLDKGEVAEFGAPSNL 1506
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
11-238 |
2.97e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 50.89 E-value: 2.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 11 QSLIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTG--KTTLLRLIGGqlvPDQGEvlldgkdiaQMSRQELFAA 88
Cdd:NF000106 11 RNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGR---------RPWRF*TWCA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 89 RARmgmlfqsgALFTDMSVYENVAFPIRAHTKLSENL--IAELVALKLESVGLRGTEQL-----------MPTELSGGMN 155
Cdd:NF000106 79 NRR--------ALRRTIG*HRPVR*GRRESFSGRENLymIGR*LDLSRKDARARADELLerfslteaagrAAAKYSGGMR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 156 RRVALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSL-REAldLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTP 234
Cdd:NF000106 151 RRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMvRDG--ATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKV 228
|
....
7D06_B 235 EELQ 238
Cdd:NF000106 229 DELK 232
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
36-257 |
3.46e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.26 E-value: 3.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 36 IRRGQITAIMGPSGTGKTTLLRLIGGQL----VPDQGEVLLDGKDIAQMSRQElfaaRARMGMLFQSGALFTDMSVYENV 111
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIASNTdgfhIGVEGVITYDGITPEEIKKHY----RGDVVYNAETDVHFPHLTVGETL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 112 AFPIRAHTK------LSENLIAE-LVALKLESVGLRGTEQL-----MPTELSGGMNRRVALARAIALDPDLIMYDEPFAG 179
Cdd:TIGR00956 160 DFAARCKTPqnrpdgVSREEYAKhIADVYMATYGLSHTRNTkvgndFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRG 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 180 QDpivKGVLTRLIRSLREALDL--TTIIVS--HDVPETLSIADYIYVVAEGKI---------------------QGEGTP 234
Cdd:TIGR00956 240 LD---SATALEFIRALKTSANIldTTPLVAiyQCSQDAYELFDKVIVLYEGYQiyfgpadkakqyfekmgfkcpDRQTTA 316
|
250 260
....*....|....*....|...
7D06_B 235 EELQAYASPFVKQFLTGSaEGPV 257
Cdd:TIGR00956 317 DFLTSLTSPAERQIKPGY-EKKV 338
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
32-237 |
5.10e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.89 E-value: 5.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 32 ISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELfaaRARMGMLFQSGALFT-------- 103
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDL---RKVLGIIPQAPVLFSgtvrfnld 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 104 ------DMSVYENVAfpiRAHTKlsenliaelVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPDLIMYDEPF 177
Cdd:PLN03130 1335 pfnehnDADLWESLE---RAHLK---------DVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEAT 1402
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 178 AGQDPIVKGVLTRLIRslREALDLTTIIVSHDVpETLSIADYIYVVAEGKIQGEGTPEEL 237
Cdd:PLN03130 1403 AAVDVRTDALIQKTIR--EEFKSCTMLIIAHRL-NTIIDCDRILVLDAGRVVEFDTPENL 1459
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
31-220 |
8.41e-07 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 48.79 E-value: 8.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 31 NISLNIRRGQITAIMGPSGTGKTTLL---------------------RLIGGQLVPDQGEVllDGKDIAQMSRQELFA-- 87
Cdd:cd03270 13 NVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayarQFLGQMDKPDVDSI--EGLSPAIAIDQKTTSrn 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 88 ARARMGMLfqsgalfTDMSVYENVAFpirAHTKLSENLiAELVALKLESVGLrgtEQLMPTeLSGGMNRRVALARAIALD 167
Cdd:cd03270 91 PRSTVGTV-------TEIYDYLRLLF---ARVGIRERL-GFLVDVGLGYLTL---SRSAPT-LSGGEAQRIRLATQIGSG 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
7D06_B 168 PDLIMY--DEPFAGQDPIVKgvlTRLIRSLREALDL--TTIIVSHDvPETLSIADYI 220
Cdd:cd03270 156 LTGVLYvlDEPSIGLHPRDN---DRLIETLKRLRDLgnTVLVVEHD-EDTIRAADHV 208
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
37-194 |
8.48e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 49.84 E-value: 8.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 37 RRGQITAIMGPSGTGKTTLL-----RLIGGQLvpdQGEVLLDGKDiaqmSRQELFAARArmGMLFQSGALFTDMSVYENV 111
Cdd:PLN03140 904 RPGVLTALMGVSGAGKTTLMdvlagRKTGGYI---EGDIRISGFP----KKQETFARIS--GYCEQNDIHSPQVTVRESL 974
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 112 AFP--IRAHTKLS--ENLI--------AELVALKLESVGLRGTeqlmpTELSGGMNRRVALARAIALDPDLIMYDEPFAG 179
Cdd:PLN03140 975 IYSafLRLPKEVSkeEKMMfvdevmelVELDNLKDAIVGLPGV-----TGLSTEQRKRLTIAVELVANPSIIFMDEPTSG 1049
|
170
....*....|....*
7D06_B 180 QDPIVKGVLTRLIRS 194
Cdd:PLN03140 1050 LDARAAAIVMRTVRN 1064
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
14-209 |
1.94e-06 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 47.31 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLsfnrgeRVIYDNISLNIRRGqITAIMGPSGTGKTTLLRLI--------------GGQLV---PDQGEVLL---- 72
Cdd:COG0419 5 LRLENF------RSYRDTETIDFDDG-LNLIVGPNGAGKSTILEAIryalygkarsrsklRSDLInvgSEEASVELefeh 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 73 DGKDI------AQMSRQELFAARARMGMLFQsgaLFtDMSVYENVAFPIRAHTKLSENLIAELVAL-KLESVGLRGTEQL 145
Cdd:COG0419 78 GGKRYrierrqGEFAEFLEAKPSERKEALKR---LL-GLEIYEELKERLKELEEALESALEELAELqKLKQEILAQLSGL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
7D06_B 146 MPTE-LSGGMNRRVALARAIALDPDlimydepFAGQDPIVKGVLTRLIRSLRealdlttiIVSHD 209
Cdd:COG0419 154 DPIEtLSGGERLRLALADLLSLILD-------FGSLDEERLERLLDALEELA--------IITHV 203
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
15-263 |
4.38e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.58 E-value: 4.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 15 EVKNLSFNRGERVIY---DNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVlldgkDIaqmsrqelfaaRAR 91
Cdd:PRK13545 23 KLKDLFFRSKDGEYHyalNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----DI-----------KGS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 92 MGMLFQSGALFTDMSVYENVAFPiRAHTKLSENLIAELVALKLESVGL-RGTEQLMPTeLSGGMNRRVALARAIALDPDL 170
Cdd:PRK13545 87 AALIAISSGLNGQLTGIENIELK-GLMMGLTKEKIKEIIPEIIEFADIgKFIYQPVKT-YSSGMKSRLGFAISVHINPDI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 171 IMYDEPFA-GQDPIVKGVLTRLiRSLREAlDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELQAYASPFVKQFL 249
Cdd:PRK13545 165 LVIDEALSvGDQTFTKKCLDKM-NEFKEQ-GKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHYDEFLKKYN 242
|
250 260
....*....|....*....|
7D06_B 250 TGSAEGPVEY------QFSH 263
Cdd:PRK13545 243 QMSVEERKDFreeqisQFQH 262
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
30-248 |
7.65e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 46.35 E-value: 7.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 30 DNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKdiaqmsrqelfaararMGMLFQSGALFTDMSVYE 109
Cdd:PRK13546 41 DDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE----------------VSVIAISAGLSGQLTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 110 NVAFpirahtklsenliaelvalKLESVGLRGTE--QLMP-----TEL-----------SGGMNRRVALARAIALDPDLI 171
Cdd:PRK13546 105 NIEF-------------------KMLCMGFKRKEikAMTPkiiefSELgefiyqpvkkySSGMRAKLGFSINITVNPDIL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
7D06_B 172 MYDEPFAGQDPIVKGVLTRLIRSLREAlDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELQAYASPFVKQF 248
Cdd:PRK13546 166 VIDEALSVGDQTFAQKCLDKIYEFKEQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPKYEAFLNDF 241
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
70-257 |
1.56e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 46.17 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 70 VLLDGKDIAQmsrqelfaararmgmlfqsgalFTDMSVYENVAFpiRAHTKLS--ENLIAELVaLK--------LESVGL 139
Cdd:COG0178 420 VKIGGKNIAE----------------------LTALSIDEALEF--FENLELTerEAEIAERI-LKeirsrlgfLVDVGL 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 140 ------RGTeqlmPTeLSGGMNRRVALARAI--AL-DpdlIMY--DEPFAGqdpivkgvL-----TRLIRSLREALDL-- 201
Cdd:COG0178 475 dyltldRSA----GT-LSGGEAQRIRLATQIgsGLvG---VLYvlDEPSIG--------LhqrdnDRLIETLKRLRDLgn 538
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
7D06_B 202 TTIIVSHDvPETLSIADYI------------YVVAegkiqgEGTPEELQAYASPFVKQFLTGSAEGPV 257
Cdd:COG0178 539 TVIVVEHD-EDTIRAADYIidigpgagehggEVVA------QGTPEEILKNPDSLTGQYLSGRKRIPV 599
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
13-74 |
1.93e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.55 E-value: 1.93e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
7D06_B 13 LIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDG 74
Cdd:PRK10636 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG 62
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
31-237 |
2.40e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 45.39 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 31 NISLNIRRGQITAIMGPSGTGKTTLL----------RLIGGQLVPDQGE-----------VLLDGKDIAQMSR------- 82
Cdd:TIGR00630 626 NITVSIPLGLFTCITGVSGSGKSTLIndtlypalanRLNGAKTVPGRYTsieglehldkvIHIDQSPIGRTPRsnpatyt 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 83 ------QELFA----ARAR--------------------------MGMLFQS----------GALFT------------- 103
Cdd:TIGR00630 706 gvfdeiRELFAetpeAKVRgytpgrfsfnvkggrceacqgdgvikIEMHFLPdvyvpcevckGKRYNretlevkykgkni 785
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 104 ----DMSVYENVAFpIRAHTKLSENLIAelvalkLESVGLrgteQLMP-----TELSGGMNRRVALARAI---ALDPDLI 171
Cdd:TIGR00630 786 advlDMTVEEAYEF-FEAVPSISRKLQT------LCDVGL----GYIRlgqpaTTLSGGEAQRIKLAKELskrSTGRTLY 854
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
7D06_B 172 MYDEPFAGQ--DPIVKgvLTRLIRSLREALDlTTIIVSH--DVPETlsiADYIYV------VAEGKIQGEGTPEEL 237
Cdd:TIGR00630 855 ILDEPTTGLhfDDIKK--LLEVLQRLVDKGN-TVVVIEHnlDVIKT---ADYIIDlgpeggDGGGTVVASGTPEEV 924
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
23-221 |
4.49e-05 |
|
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: 42.73 E-value: 4.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 23 RGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGgqlvpdqgeVLLDGKdiaqmsrqelfAARARMGMLFQSGalf 102
Cdd:cd03227 5 GRFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIG---------LALGGA-----------QSATRRRSGVKAG--- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 103 tdmsvyENVAFPIrahtklsenliAELValklesvglrgteqLMPTELSGGMNRRVALARAIAL----DPDLIMYDEPFA 178
Cdd:cd03227 62 ------CIVAAVS-----------AELI--------------FTRLQLSGGEKELSALALILALaslkPRPLYILDEIDR 110
|
170 180 190 200
....*....|....*....|....*....|....*....|...
7D06_B 179 GQDPIVKGVLTRLIRSLReALDLTTIIVSHDvPETLSIADYIY 221
Cdd:cd03227 111 GLDPRDGQALAEAILEHL-VKGAQVIVITHL-PELAELADKLI 151
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
150-249 |
1.46e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.28 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 150 LSGGMNRRVALARAIALDPDLIMY--DEPFAGQDPIVKGVLTRLIRSLREALDlTTIIVSHDvPETLSIADYIYVVAEGK 227
Cdd:PRK00635 477 LSGGEQERTALAKHLGAELIGITYilDEPSIGLHPQDTHKLINVIKKLRDQGN-TVLLVEHD-EQMISLADRIIDIGPGA 554
|
90 100
....*....|....*....|....*...
7D06_B 228 --IQGE----GTPEELQAYASPFVKQFL 249
Cdd:PRK00635 555 giFGGEvlfnGSPREFLAKSDSLTAKYL 582
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
14-176 |
1.61e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.92 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 14 IEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLR-----LIGG-----QLVPDQGEVLLDGKDIAQ---- 79
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRymamhAIDGipkncQILHVEQEVVGDDTTALQcvln 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 80 --MSRQELFAARARM---------------GMLFQSGALFTDM------SVYENVAFpIRAHTklSENLIAELVAlkles 136
Cdd:PLN03073 258 tdIERTQLLEEEAQLvaqqrelefetetgkGKGANKDGVDKDAvsqrleEIYKRLEL-IDAYT--AEARAASILA----- 329
|
170 180 190 200
....*....|....*....|....*....|....*....|...
7D06_B 137 vGLRGTEQLMPTE---LSGGMNRRVALARAIALDPDLIMYDEP 176
Cdd:PLN03073 330 -GLSFTPEMQVKAtktFSGGWRMRIALARALFIEPDLLLLDEP 371
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
27-208 |
2.62e-04 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 42.04 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 27 VIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGqLVPDQGEVLldgkdiAQMSRQELFAARARMGMlfqSGALFTDMS 106
Cdd:TIGR00954 466 VLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGE-LWPVYGGRL------TKPAKGKLFYVPQRPYM---TLGTLRDQI 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7D06_B 107 VYENVAFPIRAHTKLSENLIAELVALKLE-----SVGLRGTEQLMpTELSGGMNRRVALARAIALDPDLIMYDEPFAGQD 181
Cdd:TIGR00954 536 IYPDSSEDMKRRGLSDKDLEQILDNVQLThilerEGGWSAVQDWM-DVLSGGEKQRIAMARLFYHKPQFAILDECTSAVS 614
|
170 180
....*....|....*....|....*..
7D06_B 182 PIVKGVLTRLIRSLRealdLTTIIVSH 208
Cdd:TIGR00954 615 VDVEGYMYRLCREFG----ITLFSVSH 637
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
38-70 |
1.52e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 38.92 E-value: 1.52e-03
10 20 30
....*....|....*....|....*....|...
7D06_B 38 RGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEV 70
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLNALLPELVLATGEI 116
|
|
| COG1373 |
COG1373 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
25-63 |
1.72e-03 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440984 [Multi-domain] Cd Length: 405 Bit Score: 39.54 E-value: 1.72e-03
10 20 30
....*....|....*....|....*....|....*....
7D06_B 25 ERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQL 63
Cdd:COG1373 6 KRKILDKLLKLLDNRKAVVITGPRQVGKTTLLKQLAKEL 44
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
29-67 |
5.13e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 34.50 E-value: 5.13e-03
10 20 30
....*....|....*....|....*....|....*....
7D06_B 29 YDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQ 67
Cdd:pfam13555 12 FDGHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTLLVPAK 50
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
38-72 |
6.14e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 36.17 E-value: 6.14e-03
10 20 30
....*....|....*....|....*....|....*
7D06_B 38 RGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLL 72
Cdd:pfam13401 4 GAGILVLTGESGTGKTTLLRRLLEQLPEVRDSVVF 38
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
38-70 |
6.63e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 36.75 E-value: 6.63e-03
10 20 30
....*....|....*....|....*....|...
7D06_B 38 RGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEV 70
Cdd:pfam03193 105 KGKTTVLAGQSGVGKSTLLNALLPELDLRTGEI 137
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
44-71 |
6.69e-03 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 36.36 E-value: 6.69e-03
10 20
....*....|....*....|....*...
7D06_B 44 IMGPSGTGKTTLLRLIGGQLVPDQGEVL 71
Cdd:cd00009 24 LYGPPGTGKTTLARAIANELFRPGAPFL 51
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
37-88 |
6.70e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 37.07 E-value: 6.70e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
7D06_B 37 RRGQITAIMGPSGTGKTTLLRLIGGQLvPDQGEVLLdgkdIA--QMSRQELFAA 88
Cdd:COG3267 41 QGGGFVVLTGEVGTGKTTLLRRLLERL-PDDVKVAY----IPnpQLSPAELLRA 89
|
|
| |
