|
Name |
Accession |
Description |
Interval |
E-value |
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-255 |
1.40e-140 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 394.84 E-value: 1.40e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 7 QLKDVVKTVNEDTPEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSFL 86
Cdd:COG1101 3 ELKNLSKTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 87 SRVFQDPKLGTAPRMTVAENLLLAEKRGGHHHLVPRKLKGEMKRFKEITAKMNNNLDHRLNTATGSLSGGQRQALSFLMA 166
Cdd:COG1101 83 GRVFQDPMMGTAPSMTIEENLALAYRRGKRRGLRRGLTKKRRELFRELLATLGLGLENRLDTKVGLLSGGQRQALSLLMA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 167 TIKKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKISYDISGEDKQKLTKE 246
Cdd:COG1101 163 TLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRIILDVSGEEKKKLTVE 242
|
....*....
gi 927264579 247 ELLTFFNDI 255
Cdd:COG1101 243 DLLELFEEI 251
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
7-231 |
8.53e-54 |
|
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: 173.06 E-value: 8.53e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 7 QLKDVVKTVNEDtPEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSFL 86
Cdd:cd03255 2 ELKNLSKTYGGG-GEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 87 SR----VFQDPKLgtAPRMTVAENLLLAEkrgghhHLVPRKLKGEMKRFKEITAKMnnNLDHRLNTATGSLSGGQRQALS 162
Cdd:cd03255 81 RRhigfVFQSFNL--LPDLTALENVELPL------LLAGVPKKERRERAEELLERV--GLGDRLNHYPSELSGGQQQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 927264579 163 FLMATIKKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDAlKYGNRLLVLHQGKI 231
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-236 |
4.01e-53 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 171.38 E-value: 4.01e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 3 KTIFQLKDVVKTVNEDTpEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKR 82
Cdd:COG1136 2 SPLLELRNLTKSYGTGE-GEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 83 TSFLSR----VFQDPKLgtAPRMTVAENLLLAekrgghHHLVPRKLKGEMKRFKEITAKMNnnLDHRLNTATGSLSGGQR 158
Cdd:COG1136 81 ARLRRRhigfVFQFFNL--LPELTALENVALP------LLLAGVSRKERRERARELLERVG--LGDRLDHRPSQLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 159 Q------ALsflmatIKKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHlEDALKYGNRLLVLHQGKIS 232
Cdd:COG1136 151 QrvaiarAL------VNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRLRDGRIV 223
|
....
gi 927264579 233 YDIS 236
Cdd:COG1136 224 SDER 227
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
26-231 |
2.84e-52 |
|
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: 169.54 E-value: 2.84e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 26 LDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSF-LSRVFQDPKLgtAPRMTVA 104
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgIGRTFQIPRL--FPELTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 105 ENLLLAEKRGGHHHLVPRKLKGEMKRFKEITAKMNN--NLDHRLNTATGSLSGGQRQALSFLMATIKKPGILLLDEHTAA 182
Cdd:cd03219 94 ENVMVAAQARTGSGLLLARARREEREARERAEELLErvGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAG 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 927264579 183 LDPKTSQNLMDITdETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:cd03219 174 LNPEETEELAELI-RELRERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-248 |
5.02e-49 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 161.76 E-value: 5.02e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 4 TIFQLKDVVKTVNEDTPeelnILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRT 83
Cdd:COG3638 1 PMLELRNLSKRYPGGTP----ALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 84 SFLSR---VFQDPKLgtAPRMTVAENLLLAekRGGHH-------HLVPRKLKGE----MKRFkeitakmnnNLDHRLNTA 149
Cdd:COG3638 77 RLRRRigmIFQQFNL--VPRLSVLTNVLAG--RLGRTstwrsllGLFPPEDRERaleaLERV---------GLADKAYQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 150 TGSLSGGQRQ------ALsflmatIKKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRL 223
Cdd:COG3638 144 ADQLSGGQQQrvaiarAL------VQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRI 217
|
250 260
....*....|....*....|....*
gi 927264579 224 LVLHQGKISYDISGEDkqkLTKEEL 248
Cdd:COG3638 218 IGLRDGRVVFDGPPAE---LTDAVL 239
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
8-231 |
6.68e-49 |
|
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: 160.38 E-value: 6.68e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 8 LKDVVKTVNEDTpeelnILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTsfLS 87
Cdd:cd03259 3 LKGLSKTYGSVR-----ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRN--IG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 88 RVFQDPKLgtAPRMTVAENLLLAEKRGGhhhlVPRKLKGEmkRFKEITAKMNnnLDHRLNTATGSLSGGQRQALSFLMAT 167
Cdd:cd03259 76 MVFQDYAL--FPHLTVAENIAFGLKLRG----VPKAEIRA--RVRELLELVG--LEGLLNRYPHELSGGQQQRVALARAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 927264579 168 IKKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:cd03259 146 AREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-231 |
2.11e-46 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 153.82 E-value: 2.11e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 6 FQLKDVVKTVNEDTpeelnILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVV---KR 82
Cdd:COG4619 1 LELEGLSFRVGGKP-----ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPewrRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 83 TSFlsrVFQDPKLGtapRMTVAENLLLAEKRgghhhlvpRKLKGEMKRFKEITAKMNnnLDHR-LNTATGSLSGGQRQAL 161
Cdd:COG4619 76 VAY---VPQEPALW---GGTVRDNLPFPFQL--------RERKFDRERALELLERLG--LPPDiLDKPVERLSGGERQRL 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 162 SFLMATIKKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:COG4619 140 ALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
23-231 |
3.77e-46 |
|
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: 154.43 E-value: 3.77e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 23 LNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSF-LSRVFQDPKLgtAPRM 101
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLgIARTFQNPRL--FPEL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 102 TVAENLLLAEKRGGHHHLVP--RKLKGEMKRFKEITAKMNN-----NLDHRLNTATGSLSGGQRQALSFLMATIKKPGIL 174
Cdd:COG0411 95 TVLENVLVAAHARLGRGLLAalLRLPRARREEREARERAEEllervGLADRADEPAGNLSYGQQRRLEIARALATEPKLL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 927264579 175 LLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:COG0411 175 LLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-249 |
1.21e-45 |
|
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: 152.49 E-value: 1.21e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 6 FQLKDVVKTVNEDTPeelnILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSF 85
Cdd:COG1122 1 IELENLSFSYPGGTP----ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 86 LSRVFQDPK---LGTaprmTVAENLLLA-EKRGghhhlVPRKlkgEM-KRFKEITAKMnnNLDHRLNTATGSLSGGQRQ- 159
Cdd:COG1122 77 VGLVFQNPDdqlFAP----TVEEDVAFGpENLG-----LPRE---EIrERVEEALELV--GLEHLADRPPHELSGGQKQr 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 160 -ALSFLMATikKPGILLLDEHTAALDPKTSQNLMDITDEtIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKISYDisGE 238
Cdd:COG1122 143 vAIAGVLAM--EPEVLVLDEPTAGLDPRGRRELLELLKR-LNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVAD--GT 217
|
250
....*....|.
gi 927264579 239 DKQKLTKEELL 249
Cdd:COG1122 218 PREVFSDYELL 228
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-230 |
2.50e-45 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 151.08 E-value: 2.50e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 7 QLKDVVKTVNEDTPeelNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSFL 86
Cdd:cd03225 1 ELKNLSFSYPDGAR---PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 87 SRVFQDPK---LGTaprmTVAENLLLA-EKRGGHHHLVPRKLKGEMKRFkeitakmnnNLDHRLNTATGSLSGGQRQALS 162
Cdd:cd03225 78 GLVFQNPDdqfFGP----TVEEEVAFGlENLGLPEEEIEERVEEALELV---------GLEGLRDRSPFTLSGGQKQRVA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 927264579 163 FLMATIKKPGILLLDEHTAALDPKTSQNLMDITDEtIKEQNLTCLMITHHLEDALKYGNRLLVLHQGK 230
Cdd:cd03225 145 IAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKK-LKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-234 |
1.44e-44 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 150.03 E-value: 1.44e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 6 FQLKDVVKTVNEDTpeelNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSF 85
Cdd:cd03256 1 IEVENLSKTYPNGK----KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 86 LSR---VFQDPKLgtAPRMTVAENLLLAekRGGHHHLVpRKLKG-----EMKRFKEITAKMnnNLDHRLNTATGSLSGGQ 157
Cdd:cd03256 77 RRQigmIFQQFNL--IERLSVLENVLSG--RLGRRSTW-RSLFGlfpkeEKQRALAALERV--GLLDKAYQRADQLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 927264579 158 RQALSFLMATIKKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKISYD 234
Cdd:cd03256 150 QQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFD 226
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
25-231 |
2.39e-44 |
|
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: 149.81 E-value: 2.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSFLSRVFQDPklGTAPRMTVA 104
Cdd:COG1120 16 VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQEP--PAPFGLTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 105 ENLLLaekrGGHHHLvpRKLKGEMKRFKEIT----AKMnnNLDHRLNTATGSLSGGQRQALSFLMATIKKPGILLLDEHT 180
Cdd:COG1120 94 ELVAL----GRYPHL--GLFGRPSAEDREAVeealERT--GLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 927264579 181 AALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:COG1120 166 SHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRI 216
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
22-231 |
2.55e-44 |
|
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: 148.74 E-value: 2.55e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 22 ELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSF-LSRVFQDPKLgtAPR 100
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYVPEGRRI--FPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 101 MTVAENLLLAEKRGGHhhlvprklkgemKRFKEITAKMNN---NLDHRLNTATGSLSGGQRQALSFLMATIKKPGILLLD 177
Cdd:cd03224 90 LTVEENLLLGAYARRR------------AKRKARLERVYElfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 927264579 178 EHTAALDPKTSQNLMDITDEtIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:cd03224 158 EPSEGLAPKIVEEIFEAIRE-LRDEGVTILLVEQNARFALEIADRAYVLERGRV 210
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-231 |
1.71e-43 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 150.25 E-value: 1.71e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 1 MTKTIFQLKDVVKTVNEDTpeelnILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVV 80
Cdd:COG3842 1 MAMPALELENVSKRYGDVT-----ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 81 KR-TSFlsrVFQDPklgtA--PRMTVAENL---LlaEKRGghhhlVPRKlkgEMK-RFKEITAKMNnnLDHRLNTATGSL 153
Cdd:COG3842 76 KRnVGM---VFQDY----AlfPHLTVAENVafgL--RMRG-----VPKA---EIRaRVAELLELVG--LEGLADRYPHQL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 154 SGGQRQ------ALsflmatIKKPGILLLDEHTAALDPK----TSQNLMDItdetIKEQNLTCLMITHHLEDALKYGNRL 223
Cdd:COG3842 137 SGGQQQrvalarAL------APEPRVLLLDEPLSALDAKlreeMREELRRL----QRELGITFIYVTHDQEEALALADRI 206
|
....*...
gi 927264579 224 LVLHQGKI 231
Cdd:COG3842 207 AVMNDGRI 214
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
7-231 |
2.95e-43 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 146.36 E-value: 2.95e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 7 QLKDVVKTVNEDTpeelnILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMS--VVKRTS 84
Cdd:COG1131 2 EVRGLTKRYGDKT-----ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPaeVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 85 FlsrVFQDPKLgtAPRMTVAENLLLAekrGGHHHLVPRKLKgemKRFKEITAKMnnNLDHRLNTATGSLSGGQRQALSFL 164
Cdd:COG1131 77 Y---VPQEPAL--YPDLTVRENLRFF---ARLYGLPRKEAR---ERIDELLELF--GLTDAADRKVGTLSGGMKQRLGLA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 927264579 165 MATIKKPGILLLDEHTAALDPKTSQNLMDITDEtIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:COG1131 144 LALLHDPELLILDEPTSGLDPEARRELWELLRE-LAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRI 209
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
25-231 |
8.35e-43 |
|
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: 144.96 E-value: 8.35e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSFLSR---VFQDPklGTA--P 99
Cdd:cd03257 20 ALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRRKEiqmVFQDP--MSSlnP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 100 RMTVAEnlLLAEkrGGHHHLVPRKlKGEMKRFKEITAKMNNNLDHRLNTATGSLSGGQRQALSFLMATIKKPGILLLDEH 179
Cdd:cd03257 98 RMTIGE--QIAE--PLRIHGKLSK-KEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 927264579 180 TAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:cd03257 173 TSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-231 |
1.44e-42 |
|
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: 151.21 E-value: 1.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 1 MTKTIFQLKDVVKTVNEDTPEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVV 80
Cdd:COG1123 256 AAEPLLEVRNLSKRYPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 81 KRTSFLSR---VFQDPKLGTAPRMTVAEnlLLAEkrgghhhlvPRKLKGEMKRfKEITAKMNNNLDH-RLNTAT-----G 151
Cdd:COG1123 336 SLRELRRRvqmVFQDPYSSLNPRMTVGD--IIAE---------PLRLHGLLSR-AERRERVAELLERvGLPPDLadrypH 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 152 SLSGGQRQALSFLMATIKKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:COG1123 404 ELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRI 483
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
30-239 |
1.98e-42 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 144.13 E-value: 1.98e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 30 DLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTsfLSRVFQDPKLgtAPRMTVAENLLL 109
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERP--VSMLFQENNL--FPHLTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 110 AekrgghhhLVPR-KL-KGEMKRFKEITAKMNnnLDHRLNTATGSLSGGQRQ--ALS--FLMatiKKPgILLLDEHTAAL 183
Cdd:COG3840 95 G--------LRPGlKLtAEQRAQVEQALERVG--LAGLLDRLPGQLSGGQRQrvALArcLVR---KRP-ILLLDEPFSAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 927264579 184 DPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKISYDISGED 239
Cdd:COG3840 161 DPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAA 216
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
22-239 |
9.32e-42 |
|
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: 142.43 E-value: 9.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 22 ELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRT----SFLS---RVFqdpk 94
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIArlgiGYVPegrRIF---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 95 lgtaPRMTVAENLLLAEKRGGHHHLVPRKLKGEMKRF---KEitakmnnnldhRLNTATGSLSGGQRQALSF---LMAti 168
Cdd:COG0410 91 ----PSLTVEENLLLGAYARRDRAEVRADLERVYELFprlKE-----------RRRQRAGTLSGGEQQMLAIgraLMS-- 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 927264579 169 kKPGILLLDEHTAALDPKTSQNLMDITDEtIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKISYDISGED 239
Cdd:COG0410 154 -RPKLLLLDEPSLGLAPLIVEEIFEIIRR-LNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAE 222
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
26-231 |
1.25e-41 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 142.47 E-value: 1.25e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 26 LDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTsfLSRVFQDPKLgtAPRMTVAE 105
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRD--ISYVPQNYAL--FPHMTVYK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 106 NLLLAEKrgghHHLVPRKLKGemKRFKEITAKMNnnLDHRLNTATGSLSGGQRQALSFLMATIKKPGILLLDEHTAALDP 185
Cdd:cd03299 91 NIAYGLK----KRKVDKKEIE--RKVLEIAEMLG--IDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 927264579 186 KTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:cd03299 163 RTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKL 208
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
7-226 |
7.68e-41 |
|
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: 139.91 E-value: 7.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 7 QLKDVVKTVnEDTPEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSvvKRTSFl 86
Cdd:cd03293 2 EVRNVSKTY-GGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG--PDRGY- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 87 srVFQDPKLgtAPRMTVAENLLLAEKRGGhhhlVPRKLKGEmkRFKEITAKMNnnLDHRLNTATGSLSGGQRQALSFLMA 166
Cdd:cd03293 78 --VFQQDAL--LPWLTVLDNVALGLELQG----VPKAEARE--RAEELLELVG--LSGFENAYPHQLSGGMRQRVALARA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 167 TIKKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVL 226
Cdd:cd03293 146 LAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
25-231 |
4.55e-39 |
|
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: 133.68 E-value: 4.55e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITN--MSVVKRTSFlsrVFQDPKLGtaPRMT 102
Cdd:cd03230 15 ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKepEEVKRRIGY---LPEEPSLY--ENLT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 103 VAENLllaekrgghhhlvprklkgemkrfkeitakmnnnldhrlntatgSLSGGQRQALSFLMATIKKPGILLLDEHTAA 182
Cdd:cd03230 90 VRENL--------------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSG 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 927264579 183 LDPKTSQNLMDITDEtIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:cd03230 126 LDPESRREFWELLRE-LKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-230 |
5.09e-39 |
|
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: 133.85 E-value: 5.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 6 FQLKDVVKTVNEDTpeelnILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSF 85
Cdd:cd03229 1 LELKNVSKRYGQKT-----VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 86 --LSRVFQDPKLgtAPRMTVAENLLLAekrgghhhlvprklkgemkrfkeitakmnnnldhrlntatgsLSGGQRQALSF 163
Cdd:cd03229 76 rrIGMVFQDFAL--FPHLTVLENIALG------------------------------------------LSGGQQQRVAL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 927264579 164 LMATIKKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGK 230
Cdd:cd03229 112 ARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-235 |
6.00e-39 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 135.99 E-value: 6.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 1 MTKTIFQLKDVVKTVNEDTpEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSvv 80
Cdd:COG1116 3 AAAPALELRGVSKRFPTGG-GGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 81 KRTSFlsrVFQDPKLgtAPRMTVAENLLLA-EKRGghhhlVPRKLKGEmkRFKEITAKMNnnLDHRLNTATGSLSGGQRQ 159
Cdd:COG1116 80 PDRGV---VFQEPAL--LPWLTVLDNVALGlELRG-----VPKAERRE--RARELLELVG--LAGFEDAYPHQLSGGMRQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 927264579 160 ALSFLMATIKKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVL--HQGKISYDI 235
Cdd:COG1116 146 RVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLsaRPGRIVEEI 223
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
7-234 |
6.25e-39 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 134.79 E-value: 6.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 7 QLKDVVKTVNEDTPeelnILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSvVKRTSFL 86
Cdd:COG2884 3 RFENVSKRYPGGRE----ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLK-RREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 87 SR----VFQDPKLgtAPRMTVAENLLLAEKRGGHHhlvPRKLKgemKRFKEITAKMnnNLDHRLNTATGSLSGGQRQALS 162
Cdd:COG2884 78 RRrigvVFQDFRL--LPDRTVYENVALPLRVTGKS---RKEIR---RRVREVLDLV--GLSDKAKALPHELSGGEQQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 927264579 163 FLMATIKKPGILLLDEHTAALDPKTSQNLMDITDEtIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKISYD 234
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPETSWEIMELLEE-INRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRD 218
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
5-234 |
8.41e-39 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 135.12 E-value: 8.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 5 IFQLKDVVKTVNEDTpeelNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTS 84
Cdd:TIGR02315 1 MLEVENLSKVYPNGK----QALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 85 FLSR---VFQDPKLgtAPRMTVAENLLLAekRGGHHHLVPRKL----KGEMKRFKEITAKMNnnLDHRLNTATGSLSGGQ 157
Cdd:TIGR02315 77 LRRRigmIFQHYNL--IERLTVLENVLHG--RLGYKPTWRSLLgrfsEEDKERALSALERVG--LADKAYQRADQLSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 927264579 158 RQALSFLMATIKKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKISYD 234
Cdd:TIGR02315 151 QQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFD 227
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
7-249 |
1.71e-38 |
|
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: 135.27 E-value: 1.71e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 7 QLKDVVKTVNEDTPEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSFL 86
Cdd:TIGR04521 2 KLKNVSYIYQPGTPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 87 SRV---FQDPklgtaprmtvaENLLLAEkrgghhhLV-------PRKL---KGEMK-RFKEITAKMNnnLDHR-LNTATG 151
Cdd:TIGR04521 82 KKVglvFQFP-----------EHQLFEE-------TVykdiafgPKNLglsEEEAEeRVKEALELVG--LDEEyLERSPF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 152 SLSGGQ--RQALSFLMATikKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQG 229
Cdd:TIGR04521 142 ELSGGQmrRVAIAGVLAM--EPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKG 219
|
250 260
....*....|....*....|
gi 927264579 230 KISYDisGEDKQKLTKEELL 249
Cdd:TIGR04521 220 KIVLD--GTPREVFSDVDEL 237
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
28-234 |
4.85e-38 |
|
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: 132.23 E-value: 4.85e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 28 HVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTsfLSRVFQDPKLgtAPRMTVAENL 107
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP--VSMLFQENNL--FAHLTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 108 LLAekrgghhhLVPR-KLKGE-MKRFKEITAKMN-NNLDHRLntaTGSLSGGQRQALSFLMATIKKPGILLLDEHTAALD 184
Cdd:cd03298 92 GLG--------LSPGlKLTAEdRQAIEVALARVGlAGLEKRL---PGELSGGERQRVALARVLVRDKPVLLLDEPFAALD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 927264579 185 PKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKISYD 234
Cdd:cd03298 161 PALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQ 210
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
25-231 |
9.37e-38 |
|
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: 138.50 E-value: 9.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPT---SGQVIYKDKDITNMSVVKRTSFLSRVFQDPKLGTAPrM 101
Cdd:COG1123 21 AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRRIGMVFQDPMTQLNP-V 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 102 TVAENLLLAEKRGGhhhlVPRKlkgEMK-RFKEITAKMNnnLDHRLNTATGSLSGGQRQALSFLMATIKKPGILLLDEHT 180
Cdd:COG1123 100 TVGDQIAEALENLG----LSRA---EARaRVLELLEAVG--LERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPT 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 927264579 181 AALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:COG1123 171 TALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRI 221
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
7-231 |
9.46e-38 |
|
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: 132.24 E-value: 9.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 7 QLKDVVKTVNEDTpeelnILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSFL 86
Cdd:cd03261 2 ELRGLTKSFGGRT-----VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 87 SR---VFQDPKLGTAprMTVAEN--LLLAEkrgghHHLVPRKLKGEMKRFKeITAKmnnNLDHRLNTATGSLSGGQRQAL 161
Cdd:cd03261 77 RRmgmLFQSGALFDS--LTVFENvaFPLRE-----HTRLSEEEIREIVLEK-LEAV---GLRGAEDLYPAELSGGMKKRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 162 SFLMATIKKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:cd03261 146 ALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKI 215
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
25-231 |
1.22e-37 |
|
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: 130.25 E-value: 1.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSFLSRVFQdpklgtaprmtva 104
Cdd:cd03214 14 VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 105 enlllAEKRGGHHHLVPRKLkgemkrfkeitakmnnnldhrlntatGSLSGGQRQALSFLMATIKKPGILLLDEHTAALD 184
Cdd:cd03214 81 -----ALELLGLAHLADRPF--------------------------NELSGGERQRVLLARALAQEPPILLLDEPTSHLD 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 927264579 185 PKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:cd03214 130 IAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
25-252 |
1.84e-37 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 131.75 E-value: 1.84e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSvvKRTSFLsrvfqdPKLGTAPR---M 101
Cdd:COG1121 21 VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRAR--RRIGYV------PQRAEVDWdfpI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 102 TVAENLLLAekRGGHHHLVPRKLKGEMKRFKEITAKMnnNLDHRLNTATGSLSGGQRQ------ALsflmatIKKPGILL 175
Cdd:COG1121 93 TVRDVVLMG--RYGRRGLFRRPSRADREAVDEALERV--GLEDLADRPIGELSGGQQQrvllarAL------AQDPDLLL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 927264579 176 LDEHTAALDPKTSQNLMDITDEtIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKISYdisGEDKQKLTKEELLTFF 252
Cdd:COG1121 163 LDEPFAGVDAATEEALYELLRE-LRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAH---GPPEEVLTPENLSRAY 235
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
28-234 |
2.57e-37 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 131.24 E-value: 2.57e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 28 HVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTsfLSRVFQDPKLgtAPRMTVAENL 107
Cdd:PRK10771 17 RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRP--VSMLFQENNL--FSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 108 LLaekrGGHHHLvprKLKGEMKR-FKEITAKMNnnLDHRLNTATGSLSGGQRQALSFLMATIKKPGILLLDEHTAALDPK 186
Cdd:PRK10771 93 GL----GLNPGL---KLNAAQREkLHAIARQMG--IEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 927264579 187 TSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKISYD 234
Cdd:PRK10771 164 LRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWD 211
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-231 |
1.03e-36 |
|
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: 129.71 E-value: 1.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 1 MTKTIFQLKDVVKTVNEDTpeelnILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVV 80
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRV-----VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 81 KRTSFLSR---VFQDPKLGTAprMTVAENLLLAEKRggHHHLvPRKLKGEMkrfkeITAKMNN-NLDHRLNTATGSLSGG 156
Cdd:COG1127 76 ELYELRRRigmLFQGGALFDS--LTVFENVAFPLRE--HTDL-SEAEIREL-----VLEKLELvGLPGAADKMPSELSGG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 927264579 157 QRQALSFLMATIKKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:COG1127 146 MRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKI 220
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
6-249 |
5.43e-36 |
|
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: 134.96 E-value: 5.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 6 FQLKDVVKTVNEDTPeelNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSF 85
Cdd:COG2274 474 IELENVSFRYPGDSP---PVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQ 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 86 LSRVFQDPKL--GTaprmtVAENLLLAEKRGGHHHLVpRKLKgeMKRFKEITAKMNNNLDHRLNTATGSLSGGQRQALSF 163
Cdd:COG2274 551 IGVVLQDVFLfsGT-----IRENITLGDPDATDEEII-EAAR--LAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAI 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 164 LMATIKKPGILLLDEHTAALDPKTSQNLMditdETIKE--QNLTCLMITHHLEdALKYGNRLLVLHQGKISYDisGedkq 241
Cdd:COG2274 623 ARALLRNPRILILDEATSALDAETEAIIL----ENLRRllKGRTVIIIAHRLS-TIRLADRIIVLDKGRIVED--G---- 691
|
....*...
gi 927264579 242 klTKEELL 249
Cdd:COG2274 692 --THEELL 697
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-230 |
1.03e-35 |
|
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: 124.66 E-value: 1.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 7 QLKDVVKTVNEDTpeelnILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSFL 86
Cdd:cd00267 1 EIENLSFRYGGRT-----ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 87 SRVFQdpklgtaprmtvaenlllaekrgghhhlvprklkgemkrfkeitakmnnnldhrlntatgsLSGGQRQALSFLMA 166
Cdd:cd00267 76 GYVPQ-------------------------------------------------------------LSGGQRQRVALARA 94
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 927264579 167 TIKKPGILLLDEHTAALDPKTSQNLMDITDEtIKEQNLTCLMITHHLEDALKYGNRLLVLHQGK 230
Cdd:cd00267 95 LLLNPDLLLLDEPTSGLDPASRERLLELLRE-LAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
8-231 |
2.47e-35 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 125.77 E-value: 2.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 8 LKDVVKTVnEDTPEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSFLS 87
Cdd:cd03258 4 LKNVSKVF-GDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 88 R---VFQDPKLGTAPrmTVAENLLLaekrgghhhlvPRKLKGEMKrfKEITAKMNN-----NLDHRLNTATGSLSGGQRQ 159
Cdd:cd03258 83 RigmIFQHFNLLSSR--TVFENVAL-----------PLEIAGVPK--AEIEERVLEllelvGLEDKADAYPAQLSGGQKQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 927264579 160 ALSFLMATIKKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:cd03258 148 RVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
7-231 |
3.83e-35 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 128.27 E-value: 3.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 7 QLKDVVKTVNEDTpeelnILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRtsFL 86
Cdd:COG3839 5 ELENVSKSYGGVE-----ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDR--NI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 87 SRVFQDPKLgtAPRMTVAENLLLAEKRgghhhlvpRKL-KGEM-KRFKEITAKMNnnLDHRLNTATGSLSGGQRQ----- 159
Cdd:COG3839 78 AMVFQSYAL--YPHMTVYENIAFPLKL--------RKVpKAEIdRRVREAAELLG--LEDLLDRKPKQLSGGQRQrvalg 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 927264579 160 -ALsflmatIKKPGILLLDEHTAALDPKtsqnLMDITDETIK----EQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:COG3839 146 rAL------VREPKVFLLDEPLSNLDAK----LRVEMRAEIKrlhrRLGTTTIYVTHDQVEAMTLADRIAVMNDGRI 212
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
25-231 |
9.86e-35 |
|
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: 124.92 E-value: 9.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSFLSRVFQDPKLGTAPRMTVA 104
Cdd:COG1124 20 VLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDPYASLHPRHTVD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 105 EnlLLAEkrgghhhlvPRKLKGEMKRFKEITAKMNN-NLDHRLNTAT-GSLSGGQRQALSFLMATIKKPGILLLDEHTAA 182
Cdd:COG1124 100 R--ILAE---------PLRIHGLPDREERIAELLEQvGLPPSFLDRYpHQLSGGQRQRVAIARALILEPELLLLDEPTSA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 927264579 183 LDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:COG1124 169 LDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRI 217
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
25-231 |
1.51e-34 |
|
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: 123.89 E-value: 1.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTsfLSRVFQDPKLgtAPRMTVA 104
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRP--VNTVFQNYAL--FPHLTVF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 105 ENLLLAEKRgghhhlvpRKL-KGEMKRFKEITAKMNNNLDHRlNTATGSLSGGQRQALSFLMATIKKPGILLLDEHTAAL 183
Cdd:cd03300 91 ENIAFGLRL--------KKLpKAEIKERVAEALDLVQLEGYA-NRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGAL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 927264579 184 DPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:cd03300 162 DLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
25-230 |
3.31e-34 |
|
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: 120.95 E-value: 3.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSFLSRVFQDPKLgtaPRMTVA 104
Cdd:cd03228 17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAYVPQDPFL---FSGTIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 105 ENLLlaekrgghhhlvprklkgemkrfkeitakmnnnldhrlntatgslSGGQRQALSFLMATIKKPGILLLDEHTAALD 184
Cdd:cd03228 94 ENIL---------------------------------------------SGGQRQRIAIARALLRDPPILILDEATSALD 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 927264579 185 PKTSQNLMditdETIKE--QNLTCLMITHHLEdALKYGNRLLVLHQGK 230
Cdd:cd03228 129 PETEALIL----EALRAlaKGKTVIVIAHRLS-TIRDADRIIVLDDGR 171
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
19-249 |
7.43e-34 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 122.92 E-value: 7.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 19 TPEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVK--RtSFLSRVFQDPK-- 94
Cdd:TIGR04520 11 PESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWeiR-KKVGMVFQNPDnq 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 95 -LGTaprmTVAENLllA---EKRGghhhlVPRKlkgEM-KRFKEITAKMNnnLDHRLNTATGSLSGGQRQ--ALSFLMAT 167
Cdd:TIGR04520 90 fVGA----TVEDDV--AfglENLG-----VPRE---EMrKRVDEALKLVG--MEDFRDREPHLLSGGQKQrvAIAGVLAM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 168 ikKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKyGNRLLVLHQGKISYDisGEDKQKLTKEE 247
Cdd:TIGR04520 154 --RPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAE--GTPREIFSQVE 228
|
..
gi 927264579 248 LL 249
Cdd:TIGR04520 229 LL 230
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
20-231 |
5.17e-33 |
|
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: 125.64 E-value: 5.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 20 PEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSFLSRVFQDPKLgtaP 99
Cdd:COG4988 347 PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYL---F 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 100 RMTVAENLLLAEKRGGHHHLVpRKLkgEMKRFKEITAKMNNNLDHRLNTATGSLSGGQRQALSFLMATIKKPGILLLDEH 179
Cdd:COG4988 424 AGTIRENLRLGRPDASDEELE-AAL--EAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEP 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 927264579 180 TAALDPKTSQNLMDitdeTIKE--QNLTCLMITHHLEDaLKYGNRLLVLHQGKI 231
Cdd:COG4988 501 TAHLDAETEAEILQ----ALRRlaKGRTVILITHRLAL-LAQADRILVLDDGRI 549
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
26-245 |
7.22e-33 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 124.75 E-value: 7.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 26 LDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKrtsflSR------VFQDPKLgtAP 99
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRD-----AQaagiaiIHQELNL--VP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 100 RMTVAENLLLA-EKRGGhhHLVPRKlkgEM-KRFKEITAKMNNNLDhrLNTATGSLSGGQRQ------ALSflmatiKKP 171
Cdd:COG1129 93 NLSVAENIFLGrEPRRG--GLIDWR---AMrRRARELLARLGLDID--PDTPVGDLSVAQQQlveiarALS------RDA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 927264579 172 GILLLDEHTAALDPKTSQNLMDITDEtIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI--SYDISGEDKQKLTK 245
Cdd:COG1129 160 RVLILDEPTASLTEREVERLFRIIRR-LKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLvgTGPVAELTEDELVR 234
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
26-181 |
1.27e-32 |
|
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: 116.59 E-value: 1.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 26 LDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSFLSRVFQDPKLGtaPRMTVAE 105
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLF--PRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 927264579 106 NLLLAekrGGHHHLVPRKLKGEMKRFKEiTAKMNNNLDHRLNTATGSLSGGQRQALSFLMATIKKPGILLLDEHTA 181
Cdd:pfam00005 79 NLRLG---LLLKGLSKREKDARAEEALE-KLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
24-231 |
1.65e-32 |
|
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: 118.02 E-value: 1.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 24 NILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSvvKRTSFLsrvfqdPKLGTAPR--- 100
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER--KRIGYV------PQRRSIDRdfp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 101 MTVAENLLLAekRGGHHHLVPRKLKGEMKRFKEITAK--MNNNLDHRLntatGSLSGGQRQALSFLMATIKKPGILLLDE 178
Cdd:cd03235 85 ISVRDVVLMG--LYGHKGLFRRLSKADKAKVDEALERvgLSELADRQI----GELSGGQQQRVLLARALVQDPDLLLLDE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 927264579 179 HTAALDPKTSQNLMDITDEtIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:cd03235 159 PFAGVDPKTQEDIYELLRE-LRREGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
27-230 |
1.69e-32 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 119.32 E-value: 1.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 27 DHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMS--VVKRTSfLSRVFQDPKLgtAPRMTVA 104
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPghQIARMG-VVRTFQHVRL--FREMTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 105 ENLLLAEkrggHHHLVPRKLKGEMK----RFKEITA---------KMnnNLDHRLNTATGSLSGGQRQALSFLMATIKKP 171
Cdd:PRK11300 99 ENLLVAQ----HQQLKTGLFSGLLKtpafRRAESEAldraatwleRV--GLLEHANRQAGNLAYGQQRRLEIARCMVTQP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 927264579 172 GILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGK 230
Cdd:PRK11300 173 EILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
25-255 |
6.09e-32 |
|
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: 117.27 E-value: 6.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSfLSRVFQDPklGTAPRMTVA 104
Cdd:COG4555 16 ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQ-IGVLPDER--GLYDRLTVR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 105 ENLLLAekrGGHHHLVPRKLKgemKRFKEITAKMnnNLDHRLNTATGSLSGGQRQALSFLMATIKKPGILLLDEHTAALD 184
Cdd:COG4555 93 ENIRYF---AELYGLFDEELK---KRIEELIELL--GLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLD 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 927264579 185 PKTSQNLMDITdETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKISYDISGEDKQKLTKEELL--TFFNDI 255
Cdd:COG4555 165 VMARRLLREIL-RALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEENLedAFVALI 236
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
20-231 |
7.04e-32 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 122.57 E-value: 7.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 20 PEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSFLSRVFQDPKLGTAp 99
Cdd:COG4987 345 GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDT- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 100 rmTVAENLLLAE------------KRGGHHHLVprklkgemkrfkeitakmnNNLDHRLNTATGS----LSGGQRQALSF 163
Cdd:COG4987 424 --TLRENLRLARpdatdeelwaalERVGLGDWL-------------------AALPDGLDTWLGEggrrLSGGERRRLAL 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 927264579 164 LMATIKKPGILLLDEHTAALDPKTSQNLMDITDETIKEQnlTCLMITHHLEdALKYGNRLLVLHQGKI 231
Cdd:COG4987 483 ARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLA-GLERMDRILVLEDGRI 547
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
7-231 |
9.35e-32 |
|
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: 116.20 E-value: 9.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 7 QLKDVVKTVNEDTpeelnILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTsfL 86
Cdd:cd03301 2 ELENVTKRFGNVT-----ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRD--I 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 87 SRVFQDPKLgtAPRMTVAENLLLaekrgghhhlvPRKLKGEMKRfkEITAKMNN-----NLDHRLNTATGSLSGGQRQAL 161
Cdd:cd03301 75 AMVFQNYAL--YPHMTVYDNIAF-----------GLKLRKVPKD--EIDERVREvaellQIEHLLDRKPKQLSGGQRQRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 162 SFLMATIKKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:cd03301 140 ALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
7-231 |
1.07e-31 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 116.07 E-value: 1.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 7 QLKDVVKTVNEDTPeelNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDI-TNMSVVKRTsf 85
Cdd:cd03263 2 QIRNLTKTYKKGTK---PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIrTDRKAARQS-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 86 LSRVFQDPKLgtAPRMTVAENLLL-AEKRGGHHHLVPRKLKGEMKRFkeitakmnnNLDHRLNTATGSLSGGQRQALSFL 164
Cdd:cd03263 77 LGYCPQFDAL--FDELTVREHLRFyARLKGLPKSEIKEEVELLLRVL---------GLTDKANKRARTLSGGMKRKLSLA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 927264579 165 MATIKKPGILLLDEHTAALDPKTSQNLMDITDETIKeqNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:cd03263 146 IALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKL 210
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
26-231 |
3.30e-31 |
|
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: 115.51 E-value: 3.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 26 LDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTsfLSRVFQDPKLgtAPRMTVAE 105
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERN--VGFVFQHYAL--FRHMTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 106 NL---LLAEKRGghhhlvPRKLKGEMKRfkeitaKMNN-----NLDHRLNTATGSLSGGQRQALSFLMATIKKPGILLLD 177
Cdd:cd03296 94 NVafgLRVKPRS------ERPPEAEIRA------KVHEllklvQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 927264579 178 EHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:cd03296 162 EPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
26-245 |
3.39e-31 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 120.13 E-value: 3.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 26 LDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDK--DITN----------MsvvkrtsflsrVFQDP 93
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvRIRSprdaialgigM-----------VHQHF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 94 KLgtAPRMTVAENLLLAEKRGGHHHLvprKLKGEMKRFKEITAKMNNNLDhrLNTATGSLSGGQRQALSFLMATIKKPGI 173
Cdd:COG3845 90 ML--VPNLTVAENIVLGLEPTKGGRL---DRKAARARIRELSERYGLDVD--PDAKVEDLSVGEQQRVEILKALYRGARI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 927264579 174 LLLDEHTAALDPKTSQNLMDITDEtIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI--SYDISGEDKQKLTK 245
Cdd:COG3845 163 LILDEPTAVLTPQEADELFEILRR-LAAEGKSIIFITHKLREVMAIADRVTVLRRGKVvgTVDTAETSEEELAE 235
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
7-249 |
8.20e-31 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 116.78 E-value: 8.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 7 QLKDVVKTVNEDTpeelnILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDI-TNMSVVKR-TS 84
Cdd:COG1118 4 EVRNISKRFGSFT-----LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRERrVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 85 FlsrVFQDPKLgtAPRMTVAENLLLaekrgGHHHLVPRKlkgemkrfKEITAKMNNNLD--------HRLNTAtgsLSGG 156
Cdd:COG1118 79 F---VFQHYAL--FPHMTVAENIAF-----GLRVRPPSK--------AEIRARVEELLElvqleglaDRYPSQ---LSGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 157 QRQ--ALSFLMATikKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKISyd 234
Cdd:COG1118 138 QRQrvALARALAV--EPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIE-- 213
|
250
....*....|....*
gi 927264579 235 isgedkQKLTKEELL 249
Cdd:COG1118 214 ------QVGTPDEVY 222
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
7-249 |
9.31e-31 |
|
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: 113.86 E-value: 9.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 7 QLKDVVKTVNEDTPeelnILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSFL 86
Cdd:cd03254 4 EFENVNFSYDEKKP----VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 87 SRVFQDPKLGTAprmTVAENLLL------------AEKRGGHHHLVpRKLKgemkrfkeitakmnNNLDHRLNTATGSLS 154
Cdd:cd03254 80 GVVLQDTFLFSG---TIMENIRLgrpnatdeevieAAKEAGAHDFI-MKLP--------------NGYDTVLGENGGNLS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 155 GGQRQALSFLMATIKKPGILLLDEHTAALDPKTSQNLMDITDETIKeqNLTCLMITHHLeDALKYGNRLLVLHQGKIsyd 234
Cdd:cd03254 142 QGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRL-STIKNADKILVLDDGKI--- 215
|
250
....*....|....*
gi 927264579 235 isgedKQKLTKEELL 249
Cdd:cd03254 216 -----IEEGTHDELL 225
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
26-233 |
1.97e-30 |
|
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: 113.33 E-value: 1.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 26 LDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDIT-----NMSVVKRTSFLsrvfqdpklgtaPR 100
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITepgpdRMVVFQNYSLL------------PW 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 101 MTVAENLLLAEKRgghhhLVPRKLKGEMKRFKEITAKMNNnLDHRLNTATGSLSGGQRQALSFLMATIKKPGILLLDEHT 180
Cdd:TIGR01184 69 LTVRENIALAVDR-----VLPDLSKSERRAIVEEHIALVG-LTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPF 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 927264579 181 AALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKISY 233
Cdd:TIGR01184 143 GALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAAN 195
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
29-234 |
2.19e-30 |
|
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: 112.39 E-value: 2.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 29 VDLDIhEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKD-------KDItNMSVVKRTsfLSRVFQDPKLgtAPRM 101
Cdd:cd03297 17 IDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrKKI-NLPPQQRK--IGLVFQQYAL--FPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 102 TVAENLLLAekrgghhhlVPRKLKGEMK-RFKEITAKMNnnLDHRLNTATGSLSGGQRQALSFLMATIKKPGILLLDEHT 180
Cdd:cd03297 91 NVRENLAFG---------LKRKRNREDRiSVDELLDLLG--LDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 927264579 181 AALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKISYD 234
Cdd:cd03297 160 SALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYI 213
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
8-250 |
3.69e-30 |
|
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: 112.78 E-value: 3.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 8 LKDVVKTVNEDTPeelnILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSFLS 87
Cdd:cd03295 3 FENVTKRYGGGKK----AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 88 RVFQdpKLGTAPRMTVAENLllaekrgghhHLVPrKLKGEMK-----RFKEITAKMNNNLDHRLNTATGSLSGGQRQALS 162
Cdd:cd03295 79 YVIQ--QIGLFPHMTVEENI----------ALVP-KLLKWPKekireRADELLALVGLDPAEFADRYPHELSGGQQQRVG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 163 FLMATIKKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKISydisgedkQK 242
Cdd:cd03295 146 VARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIV--------QV 217
|
....*...
gi 927264579 243 LTKEELLT 250
Cdd:cd03295 218 GTPDEILR 225
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
20-231 |
6.16e-30 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 117.19 E-value: 6.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 20 PEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSvvkRTSFLSR---VFQDPKLG 96
Cdd:COG1132 350 PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLT---LESLRRQigvVPQDTFLF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 97 TaprMTVAENLLLAE------------KRGGHHHLVprklkgemkrfkeitAKMNNNLDHRLNTATGSLSGGQRQALSFL 164
Cdd:COG1132 427 S---GTIRENIRYGRpdatdeeveeaaKAAQAHEFI---------------EALPDGYDTVVGERGVNLSGGQRQRIAIA 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 927264579 165 MATIKKPGILLLDEHTAALDPKTSQNLMditdETIKE--QNLTCLMITHHL---EDAlkygNRLLVLHQGKI 231
Cdd:COG1132 489 RALLKDPPILILDEATSALDTETEALIQ----EALERlmKGRTTIVIAHRLstiRNA----DRILVLDDGRI 552
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
25-226 |
8.98e-30 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 110.65 E-value: 8.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRP---TSGQVIYKDKDITNMSVVKRtsflsRV---FQDPKLgtA 98
Cdd:COG4136 16 LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQR-----RIgilFQDDLL--F 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 99 PRMTVAENLLLAekrgghhhlVPRKLKGEMKRFKEITAKMNNNLDHRLNTATGSLSGGQRQALSFLMATIKKPGILLLDE 178
Cdd:COG4136 89 PHLSVGENLAFA---------LPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 927264579 179 HTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGnRLLVL 226
Cdd:COG4136 160 PFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAAG-RVLDL 206
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
12-231 |
9.01e-30 |
|
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: 110.81 E-value: 9.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 12 VKTVNEDTPEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSFLSrvfQ 91
Cdd:cd03226 2 IENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSIGYVM---Q 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 92 DP--KLGTAprmTVAENLLLAEKRGghhHLVPRKLKGEMKRFKEITAKmnnnLDHRLntatgSLSGGQRQALSFLMATIK 169
Cdd:cd03226 79 DVdyQLFTD---SVREELLLGLKEL---DAGNEQAETVLKDLDLYALK----ERHPL-----SLSGGQKQRLAIAAALLS 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 927264579 170 KPGILLLDEHTAALDPKTSQNLMDITDEtIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:cd03226 144 GKDLLIFDEPTSGLDYKNMERVGELIRE-LAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-231 |
1.14e-29 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 110.70 E-value: 1.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 6 FQLKDVVKTVNEdtpeeLNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITN-----MSVV 80
Cdd:cd03262 1 IEIKNLHKSFGD-----FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkkniNELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 81 KRTSFlsrVFQDPKLgtAPRMTVAENLLLAekrgghhhlvPRKLKGEMK-----RFKEITAKMnnNLDHRLNTATGSLSG 155
Cdd:cd03262 76 QKVGM---VFQQFNL--FPHLTVLENITLA----------PIKVKGMSKaeaeeRALELLEKV--GLADKADAYPAQLSG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 927264579 156 GQRQALSFLMATIKKPGILLLDEHTAALDPKTSQNLMDITDEtIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:cd03262 139 GQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKD-LAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-231 |
2.60e-29 |
|
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: 110.22 E-value: 2.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 1 MTKTIFQLKDVVKTVNEDTpEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVV 80
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGA-GELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 81 KRTSFLSR----VFQDPKLgtAPRMTVAENLLLaekrgghhhlvPRKLKGE---MKRFKEITAKMNnnLDHRLNTATGSL 153
Cdd:COG4181 83 ARARLRARhvgfVFQSFQL--LPTLTALENVML-----------PLELAGRrdaRARARALLERVG--LGHRLDHYPAQL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 154 SGG--QRQALSflMATIKKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGnRLLVLHQGKI 231
Cdd:COG4181 148 SGGeqQRVALA--RAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCD-RVLRLRAGRL 224
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-234 |
4.06e-29 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 112.73 E-value: 4.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 1 MTKTIFQLKDVVKTVNEDTpeelnILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVV 80
Cdd:PRK09452 10 SLSPLVELRGISKSFDGKE-----VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 81 KRtsFLSRVFQDPKLgtAPRMTVAENL---LLAEKrgghhhlVPrklKGEMKRFKEITAKMnNNLDHRLNTATGSLSGGQ 157
Cdd:PRK09452 85 NR--HVNTVFQSYAL--FPHMTVFENVafgLRMQK-------TP---AAEITPRVMEALRM-VQLEEFAQRKPHQLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 927264579 158 RQALSFLMATIKKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKISYD 234
Cdd:PRK09452 150 QQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQD 226
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
6-230 |
7.21e-29 |
|
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: 108.34 E-value: 7.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 6 FQLKDVVKTVNEDTpeelnILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNmsvvKRTSF 85
Cdd:COG4133 3 LEAENLSCRRGERL-----LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD----AREDY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 86 LSRV-FQDPKLGTAPRMTVAENLLLAEKRGGhhhlvprkLKGEMKRFKEITAKMnnNLDHRLNTATGSLSGGQRQALSFL 164
Cdd:COG4133 74 RRRLaYLGHADGLKPELTVRENLRFWAALYG--------LRADREAIDEALEAV--GLAGLADLPVRQLSAGQKRRVALA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 927264579 165 MATIKKPGILLLDEHTAALDPKTSQNLMDITDETiKEQNLTCLMITHHLEDALkyGNRLLVLHQGK 230
Cdd:COG4133 144 RLLLSPAPLWLLDEPFTALDAAGVALLAELIAAH-LARGGAVLLTTHQPLELA--AARVLDLGDFK 206
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
16-234 |
1.17e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 109.75 E-value: 1.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 16 NEDTPEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDIT----NMSVVKRTSFLsrVFQ 91
Cdd:PRK13637 13 MEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkkvKLSDIRKKVGL--VFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 92 DPklgtaprmtvaENLLLAEKRGGHHHLVPRKL---KGEM-KRFKEITAKMNNNLDHRLNTATGSLSGGQRQALSFLMAT 167
Cdd:PRK13637 91 YP-----------EYQLFEETIEKDIAFGPINLglsEEEIeNRVKRAMNIVGLDYEDYKDKSPFELSGGQKRRVAIAGVV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 927264579 168 IKKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKISYD 234
Cdd:PRK13637 160 AMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQ 226
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-231 |
1.99e-28 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 108.95 E-value: 1.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 1 MTKTIFQLKDVVKTVNEDtpeELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSV- 79
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDA---ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVw 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 80 -VKRTsfLSRVFQDPK---LGTAPRMTVAENLllaEKRGghhhlVPRKlkgEM-KRFKEITAK--MNNNLDHRlntaTGS 152
Cdd:PRK13635 78 dVRRQ--VGMVFQNPDnqfVGATVQDDVAFGL---ENIG-----VPRE---EMvERVDQALRQvgMEDFLNRE----PHR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 153 LSGGQRQ--ALSFLMATikKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKyGNRLLVLHQGK 230
Cdd:PRK13635 141 LSGGQKQrvAIAGVLAL--QPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGE 217
|
.
gi 927264579 231 I 231
Cdd:PRK13635 218 I 218
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-231 |
2.47e-28 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 107.65 E-value: 2.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 6 FQLKDVVKTVNEDTpeelnILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGG-----NLRPTSGQVIYKDKDITNMSV- 79
Cdd:cd03260 1 IELRDLNVYYGDKH-----ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKDIYDLDVd 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 80 ---VKRTsfLSRVFQDPklgTAPRMTVAENLLLAEKRGGhhhlvpRKLKGEMKRFKE-------ITAKMNNNLDHRlnta 149
Cdd:cd03260 76 vleLRRR--VGMVFQKP---NPFPGSIYDNVAYGLRLHG------IKLKEELDERVEealrkaaLWDEVKDRLHAL---- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 150 tgSLSGGQRQALSFLMATIKKPGILLLDEHTAALDPKTSQNLmditDETIKE--QNLTCLMITHHLEDALKYGNRLLVLH 227
Cdd:cd03260 141 --GLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKI----EELIAElkKEYTIVIVTHNMQQAARVADRTAFLL 214
|
....
gi 927264579 228 QGKI 231
Cdd:cd03260 215 NGRL 218
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
7-231 |
3.49e-28 |
|
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: 106.72 E-value: 3.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 7 QLKDVVKTVNEDTPEelniLDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSvVKRTSFL 86
Cdd:cd03292 2 EFINVTKTYPNGTAA----LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLR-GRAIPYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 87 SR----VFQDPKLgtAPRMTVAENLLLAEKRGGH-HHLVPRKLKGEMKRFkeitakmnnNLDHRLNTATGSLSGGQRQAL 161
Cdd:cd03292 77 RRkigvVFQDFRL--LPDRNVYENVAFALEVTGVpPREIRKRVPAALELV---------GLSHKHRALPAELSGGEQQRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 162 SFLMATIKKPGILLLDEHTAALDPKTSQNLMDITdETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:cd03292 146 AIARAIVNSPTILIADEPTGNLDPDTTWEIMNLL-KKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-252 |
3.64e-28 |
|
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: 107.48 E-value: 3.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 4 TIFQLKDVvkTVN-EDTPeelnILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIykdkditnmsvvkr 82
Cdd:COG1119 2 PLLELRNV--TVRrGGKT----ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDV-------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 83 tsflsRVFqDPKLGtapRMTVAEnlllAEKRGGH-----HHLVPRKLKGE----------MKRFKEITAKMNN------- 140
Cdd:COG1119 62 -----RLF-GERRG---GEDVWE----LRKRIGLvspalQLRFPRDETVLdvvlsgffdsIGLYREPTDEQRErarelle 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 141 --NLDHRLNTATGSLSGGQRQ------ALsflmatIKKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHH 212
Cdd:COG1119 129 llGLAHLADRPFGTLSQGEQRrvliarAL------VKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHH 202
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 927264579 213 LEDALKYGNRLLVLHQGKISYDisGEDKQKLTKEELLTFF 252
Cdd:COG1119 203 VEEIPPGITHVLLLKDGRVVAA--GPKEEVLTSENLSEAF 240
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
20-234 |
8.38e-28 |
|
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: 105.75 E-value: 8.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 20 PEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSFLSRVFQDPKL--GT 97
Cdd:cd03245 14 NQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQDVTLfyGT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 98 -----APRMTVA--ENLLLAEKRGGHHHLVPRKLKGemkrfkeitakmnnnLDHRLNTATGSLSGGQRQALSFLMATIKK 170
Cdd:cd03245 94 lrdniTLGAPLAddERILRAAELAGVTDFVNKHPNG---------------LDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 927264579 171 PGILLLDEHTAALDPKTSQNLMDITDETIKEQnlTCLMITHHLEdALKYGNRLLVLHQGKISYD 234
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGDK--TLIIITHRPS-LLDLVDRIIVMDSGRIVAD 219
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
25-231 |
1.23e-27 |
|
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: 105.70 E-value: 1.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRT----SFL---SRVFQdpklgt 97
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRArlgiGYLpqeASIFR------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 98 apRMTVAENLLLA-EKRGghhhlVPRKLKgeMKRFKEITAKMnnNLDHRLNTATGSLSGGQRQALSFLMATIKKPGILLL 176
Cdd:cd03218 89 --KLTVEENILAVlEIRG-----LSKKER--EEKLEELLEEF--HITHLRKSKASSLSGGERRRVEIARALATNPKFLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 927264579 177 DEHTAALDPKTSQNLMDITDEtIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:cd03218 158 DEPFAGVDPIAVQDIQKIIKI-LKDRGIGVLITDHNVRETLSITDRAYIIYEGKV 211
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
7-246 |
2.76e-27 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 107.09 E-value: 2.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 7 QLKDVVKTVnEDTPEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIggNL--RPTSGQVIYKDKDITNMS------ 78
Cdd:COG1135 3 ELENLSKTF-PTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCI--NLleRPTSGSVLVDGVDLTALSerelra 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 79 VVKRTSFlsrVFQDPKLgtAPRMTVAENLLLAEKRGGhhhlVPRklkgemkrfKEITAKMNN-----NLDHRLNTATGSL 153
Cdd:COG1135 80 ARRKIGM---IFQHFNL--LSSRTVAENVALPLEIAG----VPK---------AEIRKRVAEllelvGLSDKADAYPSQL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 154 SGGQRQ------ALsflmATikKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLH 227
Cdd:COG1135 142 SGGQKQrvgiarAL----AN--NPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLE 215
|
250 260
....*....|....*....|....
gi 927264579 228 QGKIS-----YDISGEDKQKLTKE 246
Cdd:COG1135 216 NGRIVeqgpvLDVFANPQSELTRR 239
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
25-239 |
3.64e-27 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 104.53 E-value: 3.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTsflsrvfqdpKLGTA------ 98
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERA----------RAGIAyvpqgr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 99 ---PRMTVAENLLL-AEKRGGHHHLVPRK-------LKgEMKrfkeitakmnnnldHRLNtatGSLSGGQRQALSFLMAT 167
Cdd:TIGR03410 85 eifPRLTVEENLLTgLAALPRRSRKIPDEiyelfpvLK-EML--------------GRRG---GDLSGGQQQQLAIARAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 927264579 168 IKKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKISYDISGED 239
Cdd:TIGR03410 147 VTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDE 218
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
25-231 |
7.75e-27 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 104.47 E-value: 7.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSFLSRVFQDPKLgTAPrMTVA 104
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSL-SFP-FTVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 105 ENLLLaekrGGHHHlvprklKGEMKRFKEITAKMNNNLD-----HRLNTAtgsLSGGQRQ------ALSFLMATIKKPGI 173
Cdd:PRK13548 95 EVVAM----GRAPH------GLSRAEDDALVAAALAQVDlahlaGRDYPQ---LSGGEQQrvqlarVLAQLWEPDGPPRW 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 927264579 174 LLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:PRK13548 162 LLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRL 219
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
28-255 |
7.80e-27 |
|
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: 104.65 E-value: 7.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 28 HVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMS-----VVKRTSFlSRVFQdpKLGTAPRMT 102
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkelrELRRKKI-SMVFQ--SFALLPHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 103 VAENLLLA-EKRGghhhlVPRKLKGEMKRfkEITAKMnnNLDHRLNTATGSLSGGQRQALSFLMATIKKPGILLLDEHTA 181
Cdd:cd03294 119 VLENVAFGlEVQG-----VPRAEREERAA--EALELV--GLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 182 ALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKISydisgedkQKLTKEELLT---------FF 252
Cdd:cd03294 190 ALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLV--------QVGTPEEILTnpandyvreFF 261
|
...
gi 927264579 253 NDI 255
Cdd:cd03294 262 RGV 264
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
8-234 |
8.40e-27 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 104.01 E-value: 8.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 8 LKDVVKTVNEDTPEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQViykdkdITNMSVvkrTSFLS 87
Cdd:COG1134 24 LKELLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV------EVNGRV---SALLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 88 rvfqdpkLGTA--PRMTVAENLLLaekRGGhhhlvprkLKGeMKRfKEITAKMNN-----NLDHRLNTATGSLSGGQRQA 160
Cdd:COG1134 95 -------LGAGfhPELTGRENIYL---NGR--------LLG-LSR-KEIDEKFDEivefaELGDFIDQPVKTYSSGMRAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 927264579 161 LSFLMATIKKPGILLLDEHTAALDP---KTSQNLMditdETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKISYD 234
Cdd:COG1134 155 LAFAVATAVDPDILLVDEVLAVGDAafqKKCLARI----RELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMD 227
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
22-238 |
4.18e-26 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 101.88 E-value: 4.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 22 ELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVK--RTSFL-----SRVFQdpk 94
Cdd:PRK11614 17 KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKimREAVAivpegRRVFS--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 95 lgtapRMTVAENLLLaekrgGHHHLVPRKLKGEMKRFKEITAKmnnnLDHRLNTATGSLSGGQRQALSFLMATIKKPGIL 174
Cdd:PRK11614 94 -----RMTVEENLAM-----GGFFAERDQFQERIKWVYELFPR----LHERRIQRAGTMSGGEQQMLAIGRALMSQPRLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 927264579 175 LLDEHTAALDPKTSQNLMDiTDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKISYDISGE 238
Cdd:PRK11614 160 LLDEPSLGLAPIIIQQIFD-TIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGD 222
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
22-231 |
5.20e-26 |
|
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: 103.59 E-value: 5.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 22 ELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRP---TSGQVIYKDKDITNMSVVKRTSFLSR----VFQDPk 94
Cdd:COG0444 17 VVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELRKIRGReiqmIFQDP- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 95 lGTA--PRMTV----AENLLLaekrgghHHLVPRKlkGEMKRFKEITAKMN-NNLDHRLNTATGSLSGGQRQALSFLMAT 167
Cdd:COG0444 96 -MTSlnPVMTVgdqiAEPLRI-------HGGLSKA--EARERAIELLERVGlPDPERRLDRYPHELSGGMRQRVMIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 927264579 168 IKKPGILLLDEHTAALDPkTSQ----NLMditDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:COG0444 166 ALEPKLLIADEPTTALDV-TIQaqilNLL---KDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRI 229
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
8-231 |
5.81e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 102.79 E-value: 5.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 8 LKDVVKTVNEDTPEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSFLS 87
Cdd:PRK13634 5 FQKVEHRYQYKTPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLKPLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 88 R----VFQDP--KLGTAprmTVAENLLLAEKRGGhhhlVPRKlkGEMKRFKEITAKMNnnLDHRLNTATG-SLSGGQ--R 158
Cdd:PRK13634 85 KkvgiVFQFPehQLFEE---TVEKDICFGPMNFG----VSEE--DAKQKAREMIELVG--LPEELLARSPfELSGGQmrR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 927264579 159 QALSFLMATikKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:PRK13634 154 VAIAGVLAM--EPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTV 224
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
25-231 |
5.93e-26 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 101.61 E-value: 5.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMS-----VVKRTSFlsrVFQDPKLgtAP 99
Cdd:COG1126 16 VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKkdinkLRRKVGM---VFQQFNL--FP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 100 RMTVAENLLLAekrgghhhlvPRKLKGeMKRfKEITAKMNNNLD-----HRLNTATGSLSGGQRQ------ALSflMati 168
Cdd:COG1126 91 HLTVLENVTLA----------PIKVKK-MSK-AEAEERAMELLErvglaDKADAYPAQLSGGQQQrvaiarALA--M--- 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 927264579 169 kKPGILLLDEHTAALDPktsqnlmditdETIKE----------QNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:COG1126 154 -EPKVMLFDEPTSALDP-----------ELVGEvldvmrdlakEGMTMVVVTHEMGFAREVADRVVFMDGGRI 214
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
5-234 |
6.32e-26 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 101.71 E-value: 6.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 5 IFQLKDVVKTVNEDTpeelnILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTS 84
Cdd:PRK09493 1 MIEFKNVSKHFGPTQ-----VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 85 FLS--RVFQDPKLgtAPRMTVAENLLLAekrgghhhlvPRKLKGEMKR-----FKEITAKMNnnLDHRLNTATGSLSGGQ 157
Cdd:PRK09493 76 RQEagMVFQQFYL--FPHLTALENVMFG----------PLRVRGASKEeaekqARELLAKVG--LAERAHHYPSELSGGQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 927264579 158 RQALSFLMATIKKPGILLLDEHTAALDPKTSQNLMDITdETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKISYD 234
Cdd:PRK09493 142 QQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVM-QDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAED 217
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-231 |
1.48e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 101.37 E-value: 1.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 1 MTKTIFQLKDVVKTVNEDTPEELNildHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVV 80
Cdd:PRK13648 3 DKNSIIVFKNVSFQYQSDASFTLK---DVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 81 KRTSFLSRVFQDPK---LGTAPRMTVAENLllaekrggHHHLVPRKlkgEMKRFKEITAKMNNNLDHRlNTATGSLSGGQ 157
Cdd:PRK13648 80 KLRKHIGIVFQNPDnqfVGSIVKYDVAFGL--------ENHAVPYD---EMHRRVSEALKQVDMLERA-DYEPNALSGGQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 927264579 158 RQALSFLMATIKKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKyGNRLLVLHQGKI 231
Cdd:PRK13648 148 KQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTV 220
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
8-256 |
1.58e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 102.09 E-value: 1.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 8 LKDVVKTVNEDTPEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQV--IYKDKDITNMSVVKRTSF 85
Cdd:PRK13651 5 VKNIVKIFNKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewIFKDEKNKKKTKEKEKVL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 86 LSRVFQDPKL-------GTAPRMTV----AENLLLAEKRGGHHHLVPRKLKGEMKRFKEITAKMNN--NLDHR-LNTATG 151
Cdd:PRK13651 85 EKLVIQKTRFkkikkikEIRRRVGVvfqfAEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIElvGLDESyLQRSPF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 152 SLSGGQ--RQALSFLMATikKPGILLLDEHTAALDPKTSQNLMDITDEtIKEQNLTCLMITHHLEDALKYGNRLLVLHQG 229
Cdd:PRK13651 165 ELSGGQkrRVALAGILAM--EPDFLVFDEPTAGLDPQGVKEILEIFDN-LNKQGKTIILVTHDLDNVLEWTKRTIFFKDG 241
|
250 260 270
....*....|....*....|....*....|....*.
gi 927264579 230 KI-----SYDISGEDK----QKLTKEELLTFFNDIQ 256
Cdd:PRK13651 242 KIikdgdTYDILSDNKflieNNMEPPKLLNFVNKLE 277
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
25-231 |
2.55e-25 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 100.32 E-value: 2.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVvKRtsflSRVFQDPKLgtAPRMTVA 104
Cdd:COG4525 22 ALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGA-DR----GVVFQKDAL--LPWLNVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 105 ENLLLAEKRGGhhhlVPRKlkGEMKRFKEITAKMNnnLDHRLNTATGSLSGGQRQALSFLMATIKKPGILLLDEHTAALD 184
Cdd:COG4525 95 DNVAFGLRLRG----VPKA--ERRARAEELLALVG--LADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 927264579 185 PKTSQN----LMDITDETIKeqnlTCLMITHHLEDALKYGNRLLVL--HQGKI 231
Cdd:COG4525 167 ALTREQmqelLLDVWQRTGK----GVFLITHSVEEALFLATRLVVMspGPGRI 215
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
25-231 |
3.14e-25 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 100.26 E-value: 3.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSF---LSRVFQDPKLGTAPRM 101
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAFrrdVQLVFQDSPSAVNPRM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 102 TVAEnlLLAEKRgghHHLVPRKLKGEMKRFKEITAKMNNNLDHrLNTATGSLSGGQRQALSFLMATIKKPGILLLDEHTA 181
Cdd:TIGR02769 106 TVRQ--IIGEPL---RHLTSLDESEQKARIAELLDMVGLRSED-ADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVS 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 927264579 182 ALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:TIGR02769 180 NLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-249 |
3.85e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 100.31 E-value: 3.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 1 MTKTIFQLKDVvktvNEDTPEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDK--DITNMS 78
Cdd:PRK13636 1 MEDYILKVEEL----NYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 79 VVKRTSFLSRVFQDP--KLGTAprmTVAE-------NLLLAEKRgghhhlVPRKLKGEMKRfkeitakmnNNLDHRLNTA 149
Cdd:PRK13636 77 LMKLRESVGMVFQDPdnQLFSA---SVYQdvsfgavNLKLPEDE------VRKRVDNALKR---------TGIEHLKDKP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 150 TGSLSGGQRQALSFLMATIKKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQG 229
Cdd:PRK13636 139 THCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEG 218
|
250 260
....*....|....*....|
gi 927264579 230 KISYDisGEDKQKLTKEELL 249
Cdd:PRK13636 219 RVILQ--GNPKEVFAEKEML 236
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
24-231 |
4.46e-25 |
|
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: 98.51 E-value: 4.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 24 NILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITnMSVVKRTSFLSRvfqdpKLGTAPRMTV 103
Cdd:cd03269 14 TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD-IAARNRIGYLPE-----ERGLYPKMKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 104 AENLL-LAEKRGGHHHLVPRKLKGEMKRFkEITAKMNNNLDhrlntatgSLSGGQRQALSFLMATIKKPGILLLDEHTAA 182
Cdd:cd03269 88 IDQLVyLAQLKGLKKEEARRRIDEWLERL-ELSEYANKRVE--------ELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 927264579 183 LDPKTSQNLMDITDEtIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:cd03269 159 LDPVNVELLKDVIRE-LARAGKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
26-234 |
4.63e-25 |
|
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: 98.59 E-value: 4.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 26 LDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITN--MSVVKRTSFLSrvfqdPKLGTAPRMTV 103
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKepAEARRRLGFVS-----DSTGLYDRLTA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 104 AENLllaEKRGGHHHLVPRKLKGemkRFKEITAKMNnnLDHRLNTATGSLSGGQRQALSFLMATIKKPGILLLDEHTAAL 183
Cdd:cd03266 96 RENL---EYFAGLYGLKGDELTA---RLEELADRLG--MEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 927264579 184 DPKTSQNLMDITDEtIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKISYD 234
Cdd:cd03266 168 DVMATRALREFIRQ-LRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
26-231 |
5.12e-25 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 97.11 E-value: 5.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 26 LDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVK-RTSFLSRVFQdpklgtaprmtva 104
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIAMVYQ------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 105 enlllaekrgghhhlvprklkgemkrfkeitakmnnnldhrlntatgsLSGGQRQALSFLMATIKKPGILLLDEHTAALD 184
Cdd:cd03216 83 ------------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALT 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 927264579 185 PKTSQNLMDITDEtIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:cd03216 115 PAEVERLFKVIRR-LRAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
26-231 |
5.78e-25 |
|
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: 98.60 E-value: 5.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 26 LDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIykdkdITNMSVVKRTSFLSR----VFQDPKLGtaPRM 101
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRAT-----VAGHDVVREPREVRRrigiVFQDLSVD--DEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 102 TVAENLLLAEKRGGHHHLVPRKLKGEMKRFKEITAKMnnnldHRLntaTGSLSGGQRQALSFLMATIKKPGILLLDEHTA 181
Cdd:cd03265 89 TGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAA-----DRL---VKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 927264579 182 ALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
25-234 |
9.20e-25 |
|
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: 97.65 E-value: 9.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGdFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRtSFLSRVFQDPklGTAPRMTVA 104
Cdd:cd03264 15 ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLR-RRIGYLPQEF--GVYPNFTVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 105 ENL-LLAEKRGGHHhlvprklKGEMKRFKEITAKMNnnLDHRLNTATGSLSGGQRQALSFLMATIKKPGILLLDEHTAAL 183
Cdd:cd03264 91 EFLdYIAWLKGIPS-------KEVKARVDEVLELVN--LGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 927264579 184 DPKtsqnlmditdETIKEQNL--------TCLMITHHLEDALKYGNRLLVLHQGKISYD 234
Cdd:cd03264 162 DPE----------ERIRFRNLlselgedrIVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
26-230 |
9.70e-25 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 101.07 E-value: 9.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 26 LDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTsfLSRVFQDPKLgtAPRMTVAE 105
Cdd:PRK11607 35 VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRP--INMMFQSYAL--FPHMTVEQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 106 NLLLAEKRGghhhlvpRKLKGEMK-RFKEITAkmnnnLDHRLNTAT---GSLSGGQRQALSFLMATIKKPGILLLDEHTA 181
Cdd:PRK11607 111 NIAFGLKQD-------KLPKAEIAsRVNEMLG-----LVHMQEFAKrkpHQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 927264579 182 ALDPKTSQNL-MDITDeTIKEQNLTCLMITHHLEDALKYGNRLLVLHQGK 230
Cdd:PRK11607 179 ALDKKLRDRMqLEVVD-ILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
7-246 |
1.76e-24 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 99.88 E-value: 1.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 7 QLKDVVKTVNEDTPEeLNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSFL 86
Cdd:PRK11153 3 ELKNISKVFPQGGRT-IHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 87 SRV---FQDPKLgTAPRmTVAENLLLaekrgghhhlvPRKLKGEMKrfKEITAKMNNNLD-----HRLNTATGSLSGGQR 158
Cdd:PRK11153 82 RQIgmiFQHFNL-LSSR-TVFDNVAL-----------PLELAGTPK--AEIKARVTELLElvglsDKADRYPAQLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 159 QALSFLMATIKKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI-----SY 233
Cdd:PRK11153 147 QRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLveqgtVS 226
|
250
....*....|...
gi 927264579 234 DISGEDKQKLTKE 246
Cdd:PRK11153 227 EVFSHPKHPLTRE 239
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
13-231 |
2.32e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 101.46 E-value: 2.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 13 KTVNEDTP-----EELNILDH--------VDLDIHEGDFITILGSNGAGKSTLFNTIGGNLrPTSGQVIYKDKDITNMSV 79
Cdd:PRK11174 340 KELASNDPvtieaEDLEILSPdgktlagpLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDP 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 80 VKRTSFLSRVFQDPKLgtaPRMTVAENLLLaekrgGHHHLVPRKLKGEMKR--FKEITAKMNNNLDHRLNTATGSLSGGQ 157
Cdd:PRK11174 419 ESWRKHLSWVGQNPQL---PHGTLRDNVLL-----GNPDASDEQLQQALENawVSEFLPLLPQGLDTPIGDQAAGLSVGQ 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 927264579 158 RQALSFLMATIKKPGILLLDEHTAALDPKTSQNLMditdETIKE--QNLTCLMITHHLEDaLKYGNRLLVLHQGKI 231
Cdd:PRK11174 491 AQRLALARALLQPCQLLLLDEPTASLDAHSEQLVM----QALNAasRRQTTLMVTHQLED-LAQWDQIWVMQDGQI 561
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
25-231 |
2.37e-24 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 97.41 E-value: 2.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRT----SFL---SRVFQdpklgt 97
Cdd:COG1137 18 VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRArlgiGYLpqeASIFR------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 98 apRMTVAENLLLA-EKRGghhhlVPRklkgemkrfKEITAKMNN-----NLDHRLNTATGSLSGGQRQALSFLMATIKKP 171
Cdd:COG1137 92 --KLTVEDNILAVlELRK-----LSK---------KEREERLEElleefGITHLRKSKAYSLSGGERRRVEIARALATNP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 927264579 172 GILLLDEHTAALDPKTSQNLMDITdETIKEQNLTCLmIT-HHLEDALKYGNRLLVLHQGKI 231
Cdd:COG1137 156 KFILLDEPFAGVDPIAVADIQKII-RHLKERGIGVL-ITdHNVRETLGICDRAYIISEGKV 214
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
20-231 |
2.39e-24 |
|
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: 96.79 E-value: 2.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 20 PEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSFLSRVFQDPKLGTAp 99
Cdd:cd03244 14 PNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQDPVLFSG- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 100 rmTVAENLllaekrGGHHHLVPRKLKG--EMKRFKEITAKMNNNLDHRLNTATGSLSGGQRQALSFLMATIKKPGILLLD 177
Cdd:cd03244 93 --TIRSNL------DPFGEYSDEELWQalERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 927264579 178 EHTAALDPKTSQNLMditdETIKEQ--NLTCLMITHHLEDALKYgNRLLVLHQGKI 231
Cdd:cd03244 165 EATASVDPETDALIQ----KTIREAfkDCTVLTIAHRLDTIIDS-DRILVLDKGRV 215
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
9-231 |
3.19e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 97.85 E-value: 3.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 9 KDVV-KTVNEDTPEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKD---KDITNMSVVKRTS 84
Cdd:PRK13633 8 KNVSyKYESNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtSDEENLWDIRNKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 85 FLsrVFQDPK---LGTAPRMTVA---ENLLLAEKRgghhhlVPRKLKGEMKRfkeitAKMNNNLDHrlntATGSLSGGQR 158
Cdd:PRK13633 88 GM--VFQNPDnqiVATIVEEDVAfgpENLGIPPEE------IRERVDESLKK-----VGMYEYRRH----APHLLSGGQK 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 927264579 159 QALSFLMATIKKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKyGNRLLVLHQGKI 231
Cdd:PRK13633 151 QRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKV 222
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
25-231 |
5.01e-24 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 96.72 E-value: 5.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMS---------VVKRTSFLSRVFqdpkl 95
Cdd:COG4559 16 LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSpwelarrraVLPQHSSLAFPF----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 96 gtaprmTVAENLLLaekrGGHHHLVPRKLKGEMKRfkEITAKMnnNLDHRLNTATGSLSGGQRQ------ALSFLMATIK 169
Cdd:COG4559 91 ------TVEEVVAL----GRAPHGSSAAQDRQIVR--EALALV--GLAHLAGRSYQTLSGGEQQrvqlarVLAQLWEPVD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 927264579 170 -KPGILLLDEHTAALDPKTSQNLMDITDEtIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:COG4559 157 gGPRWLFLDEPTSALDLAHQHAVLRLARQ-LARRGGGVVAVLHDLNLAAQYADRILLLHQGRL 218
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
19-249 |
5.02e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 97.37 E-value: 5.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 19 TPEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSFLSRVFQDPK---L 95
Cdd:PRK13632 18 PNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIFQNPDnqfI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 96 GTAPRMTVAENLllaEKRgghhhLVPRKlkgEMKRFKEITAK---MNNNLDHRlntaTGSLSGGQRQ--ALSFLMATikK 170
Cdd:PRK13632 98 GATVEDDIAFGL---ENK-----KVPPK---KMKDIIDDLAKkvgMEDYLDKE----PQNLSGGQKQrvAIASVLAL--N 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 927264579 171 PGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKyGNRLLVLHQGKISYdiSGEDKQKLTKEELL 249
Cdd:PRK13632 161 PEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIA--QGKPKEILNNKEIL 236
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
20-231 |
2.37e-23 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 98.64 E-value: 2.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 20 PEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSFLSRVFQDPKLGTAp 99
Cdd:TIGR02203 342 GRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFND- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 100 rmTVAENLLLAEKRGGHHHLVPRKLkgEMKRFKEITAKMNNNLDHRLNTATGSLSGGQRQALSFLMATIKKPGILLLDEH 179
Cdd:TIGR02203 421 --TIANNIAYGRTEQADRAEIERAL--AAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEA 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 927264579 180 TAALDPKTSQNLMDITDETIkeQNLTCLMITHHLEdALKYGNRLLVLHQGKI 231
Cdd:TIGR02203 497 TSALDNESERLVQAALERLM--QGRTTLVIAHRLS-TIEKADRIVVMDDGRI 545
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-231 |
2.87e-23 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 96.71 E-value: 2.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 1 MTKTIF-QLKDVVKTVNEDTpeelnILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSV 79
Cdd:PRK11432 1 MTQKNFvVLKNITKRFGSNT-----VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 80 VKRTsfLSRVFQDPKLgtAPRMTVAENLLLAEKRGGhhhlVPrklKGEMK-RFKEITAKMNnnLDHRLNTATGSLSGGQR 158
Cdd:PRK11432 76 QQRD--ICMVFQSYAL--FPHMSLGENVGYGLKMLG----VP---KEERKqRVKEALELVD--LAGFEDRYVDQISGGQQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 927264579 159 QALSFLMATIKKPGILLLDEHTAALDpktsQNLMDITDETIKE-Q---NLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:PRK11432 143 QRVALARALILKPKVLLFDEPLSNLD----ANLRRSMREKIRElQqqfNITSLYVTHDQSEAFAVSDTVIVMNKGKI 215
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
20-216 |
3.72e-23 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 92.87 E-value: 3.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 20 PEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVI-------YKDKDITNmsvVKRTSFLsrVFQD 92
Cdd:TIGR01166 2 PGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLidgepldYSRKGLLE---RRQRVGL--VFQD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 93 PklgtaprmtvaENLLLAEKRGGHHHLVPRKLKGEMKrfkEITAKMNNNL-----DHRLNTATGSLSGGQRQALSFLMAT 167
Cdd:TIGR01166 77 P-----------DDQLFAADVDQDVAFGPLNLGLSEA---EVERRVREALtavgaSGLRERPTHCLSGGEKKRVAIAGAV 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 927264579 168 IKKPGILLLDEHTAALDPKTSQNLMDITDEtIKEQNLTCLMITHHLEDA 216
Cdd:TIGR01166 143 AMRPDVLLLDEPTAGLDPAGREQMLAILRR-LRAEGMTVVISTHDVDLA 190
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
26-234 |
7.67e-23 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 93.17 E-value: 7.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 26 LDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVI------YKDKDitnmSVVKRTSFlsrVFqdpklgtAP 99
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRvaglvpWKRRK----KFLRRIGV---VF-------GQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 100 RMTVAENLLLAEKRGGHHH---LVPRKLKgemKRFKEITAKMNnnLDHRLNTATGSLSGGQRQALSFLMATIKKPGILLL 176
Cdd:cd03267 103 KTQLWWDLPVIDSFYLLAAiydLPPARFK---KRLDELSELLD--LEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 927264579 177 DEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKISYD 234
Cdd:cd03267 178 DEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYD 235
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
26-231 |
9.74e-23 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 95.17 E-value: 9.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 26 LDhVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSG------QVIYKDKDITNMSVVKRtsflsR---VFQDPKLg 96
Cdd:COG4148 16 LD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGrirlggEVLQDSARGIFLPPHRR-----RigyVFQEARL- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 97 tAPRMTVAENLLLAEKRGGhhhlvprklKGEMK-RFKEITAKMNnnLDHRLNTATGSLSGGQRQ------ALsflmatIK 169
Cdd:COG4148 89 -FPHLSVRGNLLYGRKRAP---------RAERRiSFDEVVELLG--IGHLLDRRPATLSGGERQrvaigrAL------LS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 927264579 170 KPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:COG4148 151 SPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRV 212
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
8-236 |
1.31e-22 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 93.20 E-value: 1.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 8 LKDVVKTVNEDTpeelnILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQV------IYKDKDITNMsvvk 81
Cdd:PRK11247 15 LNAVSKRYGERT-----VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELlagtapLAEAREDTRL---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 82 rtsflsrVFQDPKLgtAPRMTVAENLLLAekrgghhhlvprkLKGEMkRFKEITAKMNNNLDHRLNTATGSLSGGQRQAL 161
Cdd:PRK11247 86 -------MFQDARL--LPWKKVIDNVGLG-------------LKGQW-RDAALQALAAVGLADRANEWPAALSGGQKQRV 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 927264579 162 SFLMATIKKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKISYDIS 236
Cdd:PRK11247 143 ALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLT 217
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
8-231 |
1.55e-22 |
|
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: 92.29 E-value: 1.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 8 LKDVVKTVNEDTPeelNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSFLS 87
Cdd:cd03251 3 FKNVTFRYPGDGP---PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 88 RVFQDPKLGTAprmTVAENLLLAeKRGGHHHLVPRKLKgeMKRFKEITAKMNNNLDHRLNTATGSLSGGQRQALSFLMAT 167
Cdd:cd03251 80 LVSQDVFLFND---TVAENIAYG-RPGATREEVEEAAR--AANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 927264579 168 IKKPGILLLDEHTAALDPKTSQNLMDITDETIKeqNLTCLMITHHL---EDAlkygNRLLVLHQGKI 231
Cdd:cd03251 154 LKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLstiENA----DRIVVLEDGKI 214
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
8-249 |
1.82e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 93.27 E-value: 1.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 8 LKDVVKTVNEDTPEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSFLS 87
Cdd:PRK13649 5 LQNVSYTYQAGTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 88 R----VFQDPKlgtapRMTVAENLLLAEKRGGHHHLVPRKLKGEMKRFKEITAKMNNNLdhrLNTATGSLSGGQ--RQAL 161
Cdd:PRK13649 85 KkvglVFQFPE-----SQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESL---FEKNPFELSGGQmrRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 162 SFLMATikKPGILLLDEHTAALDPKTSQNLMDITDEtIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKISydISGEDKQ 241
Cdd:PRK13649 157 AGILAM--EPKILVLDEPTAGLDPKGRKELMTLFKK-LHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLV--LSGKPKD 231
|
....*...
gi 927264579 242 KLTKEELL 249
Cdd:PRK13649 232 IFQDVDFL 239
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-231 |
2.66e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 92.28 E-value: 2.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGG--NLRP---TSGQVIYKDKDITNMSVVKRTSFLSRVFQDPKlgTAP 99
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRliELYPearVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPN--PIP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 100 RMTVAENLLLAEKRgghHHLVprKLKGEM-KRFKEI--TAKMNNNLDHRLNTATGSLSGGQRQALSFLMATIKKPGILLL 176
Cdd:PRK14247 96 NLSIFENVALGLKL---NRLV--KSKKELqERVRWAleKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 927264579 177 DEHTAALDPKTSQNLMDITDETIKEqnLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
24-231 |
2.82e-22 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 95.58 E-value: 2.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 24 NILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSFLSRVFQDPKLGTAprmTV 103
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSG---SI 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 104 AENLLLAEKRGGHHHLVPRKLkgemkRFKEITA---KMNNNLDHRLNTATGSLSGGQRQALSFLMATIKKPGILLLDEHT 180
Cdd:TIGR01193 565 LENLLLGAKENVSQDEIWAAC-----EIAEIKDdieNMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDEST 639
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 927264579 181 AALDPKTSQ----NLMDITDETIkeqnltcLMITHHLEDAlKYGNRLLVLHQGKI 231
Cdd:TIGR01193 640 SNLDTITEKkivnNLLNLQDKTI-------IFVAHRLSVA-KQSDKIIVLDHGKI 686
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
20-229 |
3.04e-22 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 93.62 E-value: 3.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 20 PEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKR---TSFLSRVFQDPKLG 96
Cdd:PRK15079 31 PKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravRSDIQMIFQDPLAS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 97 TAPRMTVAEnlLLAEKRGGHHhlvPRKLKGEMK-RFKEITAKMnNNLDHRLNTATGSLSGGQRQALSFLMATIKKPGILL 175
Cdd:PRK15079 111 LNPRMTIGE--IIAEPLRTYH---PKLSRQEVKdRVKAMMLKV-GLLPNLINRYPHEFSGGQCQRIGIARALILEPKLII 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 927264579 176 LDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQG 229
Cdd:PRK15079 185 CDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLG 238
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
25-213 |
3.29e-22 |
|
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: 95.12 E-value: 3.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMS---VVKRTSFLSrvfQDPKLGTAprm 101
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDqdeVRRRVSVCA---QDAHLFDT--- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 102 TVAENLLLAEKRGGHHHLVpRKLkgEMKRFKEITAKMNNNLDHRLNTATGSLSGGQRQALSFLMATIKKPGILLLDEHTA 181
Cdd:TIGR02868 424 TVRENLRLARPDATDEELW-AAL--ERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTE 500
|
170 180 190
....*....|....*....|....*....|...
gi 927264579 182 ALDPKTSQNLM-DITDETikeQNLTCLMITHHL 213
Cdd:TIGR02868 501 HLDAETADELLeDLLAAL---SGRTVVLITHHL 530
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
8-234 |
3.49e-22 |
|
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: 91.05 E-value: 3.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 8 LKDVVKTVNEDTPEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQViykdkdITNMSVvkrTSFLs 87
Cdd:cd03220 20 LKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV------TVRGRV---SSLL- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 88 rvfqDPKLGTAPRMTVAENLLLaekRGGhhhlvprkLKGeMKRfKEITAKMN-----NNLDHRLNTATGSLSGGQRQALS 162
Cdd:cd03220 90 ----GLGGGFNPELTGRENIYL---NGR--------LLG-LSR-KEIDEKIDeiiefSELGDFIDLPVKTYSSGMKARLA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 927264579 163 FLMATIKKPGILLLDEHTAALDPKTSQNLMDITDEtIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKISYD 234
Cdd:cd03220 153 FAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRE-LLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
25-231 |
4.30e-22 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 91.23 E-value: 4.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIggNL--RPTSGQV-IYKDK-DITNMSVVKRTSFLSR----VFQDPKLG 96
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVL--NLleMPRSGTLnIAGNHfDFSKTPSDKAIRELRRnvgmVFQQYNLW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 97 taPRMTVAENLLLAekrgghhhlvPRKLKG-----EMKRFKEITAKMnnnldhRLNTATGS----LSGGQRQALSFLMAT 167
Cdd:PRK11124 95 --PHLTVQQNLIEA----------PCRVLGlskdqALARAEKLLERL------RLKPYADRfplhLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 927264579 168 IKKPGILLLDEHTAALDPKTSQNLMDITDEtIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDPEITAQIVSIIRE-LAETGITQVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
26-231 |
4.55e-22 |
|
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: 95.08 E-value: 4.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 26 LDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDI-TNMSVVKRTsflsrvfqdpkLGTAPRmtva 104
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDAVRQS-----------LGMCPQ---- 1010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 105 ENLLLAEKRGGHHHLVPRKLKGemKRFKEITAKM-----NNNLDHRLNTATGSLSGGQRQALSFLMATIKKPGILLLDEH 179
Cdd:TIGR01257 1011 HNILFHHLTVAEHILFYAQLKG--RSWEEAQLEMeamleDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEP 1088
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 927264579 180 TAALDPKTSQNLMDITDETikEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:TIGR01257 1089 TSGVDPYSRRSIWDLLLKY--RSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
26-217 |
5.59e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 89.99 E-value: 5.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 26 LDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQViykdkditnmsVVKRTSFLSRVFQDPKLGTAPRMTVAE 105
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----------RRAGGARVAYVPQRSEVPDSLPLTVRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 106 nlLLAEKRGGHHHLVpRKLKGEMKRfkEITAKMN----NNLDHRlntATGSLSGGQRQALSFLMATIKKPGILLLDEHTA 181
Cdd:NF040873 77 --LVAMGRWARRGLW-RRLTRDDRA--AVDDALErvglADLAGR---QLGELSGGQRQRALLAQGLAQEADLLLLDEPTT 148
|
170 180 190
....*....|....*....|....*....|....*.
gi 927264579 182 ALDPKTSQNLMDITDEtIKEQNLTCLMITHHLEDAL 217
Cdd:NF040873 149 GLDAESRERIIALLAE-EHARGATVVVVTHDLELVR 183
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
3-211 |
5.97e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 90.54 E-value: 5.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 3 KTIFQLKDVVKTVNEDTpeelnILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKR 82
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAK-----ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 83 TSFLSRVFQDPKL-GTaprmTVAENLLLA-EKRggHHHLVPRKLKGEMKRFkeitakmnnNL-DHRLNTATGSLSGGQRQ 159
Cdd:PRK10247 80 RQQVSYCAQTPTLfGD----TVYDNLIFPwQIR--NQQPDPAIFLDDLERF---------ALpDTILTKNIAELSGGEKQ 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 927264579 160 ALSFLMATIKKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITH 211
Cdd:PRK10247 145 RISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTH 196
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
25-231 |
6.38e-22 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 92.84 E-value: 6.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKR-TSFlsrVFQDPKLGTapRMTV 103
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRkVGF---VFQHYALFR--HMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 104 AENLLLAEKrgghhhLVPRKLKGEMKRFKEITAKMNN--NLDHRLNTATGSLSGGQRQALSFLMATIKKPGILLLDEHTA 181
Cdd:PRK10851 92 FDNIAFGLT------VLPRRERPNAAAIKAKVTQLLEmvQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 927264579 182 ALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:PRK10851 166 ALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
25-231 |
6.48e-22 |
|
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: 90.68 E-value: 6.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIggnLR---PTSGQVIYKDKDITNMSVVKRTSFLSRVFQDPKLGTaprM 101
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLL---ERfydPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVLFD---G 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 102 TVAENLLLAekrgghhhlvprKLKGEMKRFKEITAKMN-----NNLDHRLNTATG----SLSGGQRQALSFLMATIKKPG 172
Cdd:cd03249 92 TIAENIRYG------------KPDATDEEVEEAAKKANihdfiMSLPDGYDTLVGergsQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 927264579 173 ILLLDEHTAALDPKTSQNLMDITDETIKeqNLTCLMITHHLEdALKYGNRLLVLHQGKI 231
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLS-TIRNADLIAVLQNGQV 215
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
7-231 |
9.00e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 91.38 E-value: 9.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 7 QLKDVVKTVNEDTPEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSFL 86
Cdd:PRK13646 4 RFDNVSYTYQKGTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 87 SR----VFQDPklgtaprmtvaENLLLAEKRGGHHHLVPRKLKGEMKRFKEITAKMNNNLDHRLNTATGS---LSGGQRQ 159
Cdd:PRK13646 84 RKrigmVFQFP-----------ESQLFEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSpfqMSGGQMR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 927264579 160 ALSFLMATIKKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:PRK13646 153 KIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
20-231 |
1.36e-21 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 88.52 E-value: 1.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 20 PEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRtSFLSRVFQDPKLgtap 99
Cdd:cd03247 12 EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALS-SLISVLNQRPYL---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 100 rmtvaenlllaekrgghhhlvprklkgemkrfkeITAKMNNNLDHRLntatgslSGGQRQALSFLMATIKKPGILLLDEH 179
Cdd:cd03247 87 ----------------------------------FDTTLRNNLGRRF-------SGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 927264579 180 TAALDPKTSQNLMDITDETIKEQnlTCLMITHHLEdALKYGNRLLVLHQGKI 231
Cdd:cd03247 126 TVGLDPITERQLLSLIFEVLKDK--TLIWITHHLT-GIEHMDKILFLENGKI 174
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
25-231 |
1.46e-21 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 90.52 E-value: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSF---LSRVFQDPKLGTAPRM 101
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFrrdIQMVFQDSISAVNPRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 102 TVAEnlLLAEKRgghHHLVPRKLKGEMKRFKEITAKMNNNLDHrLNTATGSLSGGQRQALSFLMATIKKPGILLLDEHTA 181
Cdd:PRK10419 107 TVRE--IIREPL---RHLLSLDKAERLARASEMLRAVDLDDSV-LDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVS 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 927264579 182 ALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:PRK10419 181 NLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
25-231 |
1.97e-21 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 89.69 E-value: 1.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIggNL--RPTSGQVIYKDK--DITNMSVVKRTSFLSR----VFQDPKLG 96
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSSLLRVL--NLleTPDSGQLNIAGHqfDFSQKPSEKAIRLLRQkvgmVFQQYNLW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 97 taPRMTVAENLLLAekrgghhhlvPRKLKGEMK-----RFKEITAKMNnnLDHRLNTATGSLSGGQRQALSFLMATIKKP 171
Cdd:COG4161 95 --PHLTVMENLIEA----------PCKVLGLSKeqareKAMKLLARLR--LTDKADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 172 GILLLDEHTAALDPKTSQNLMDITDEtIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:COG4161 161 QVLLFDEPTAALDPEITAQVVEIIRE-LSQTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
24-253 |
2.47e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 89.69 E-value: 2.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 24 NILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMS---VVKRTSFLsrvfqdPKLGTAPR 100
Cdd:PRK11231 16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSsrqLARRLALL------PQHHLTPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 101 -MTVAEnlLLAEKRGGHHHLVPRkLKGEMKRFkeITAKMNN-NLDHRLNTATGSLSGGQRQALSFLMATIKKPGILLLDE 178
Cdd:PRK11231 90 gITVRE--LVAYGRSPWLSLWGR-LSAEDNAR--VNQAMEQtRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 927264579 179 HTAALDPKTSQNLMDITDEtIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKISYDisGEDKQKLTKEELLTFFN 253
Cdd:PRK11231 165 PTTYLDINHQVELMRLMRE-LNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQ--GTPEEVMTPGLLRTVFD 236
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
5-231 |
2.65e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 90.14 E-value: 2.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 5 IFQLKDVVKTVNEDTpeelNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDIT--NMSVVKR 82
Cdd:PRK13639 1 ILETRDLKYSYPDGT----EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydKKSLLEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 83 TSFLSRVFQDPKLGT-APrmTVAENLLLAekrgghhhlvPRKLKGEM----KRFKEITAKMNnnLDHRLNTATGSLSGGQ 157
Cdd:PRK13639 77 RKTVGIVFQNPDDQLfAP--TVEEDVAFG----------PLNLGLSKeeveKRVKEALKAVG--MEGFENKPPHHLSGGQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 927264579 158 --RQALSFLMATikKPGILLLDEHTAALDPKTSQNLMDITDEtIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:PRK13639 143 kkRVAIAGILAM--KPEIIVLDEPTSGLDPMGASQIMKLLYD-LNKEGITIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
20-256 |
3.60e-21 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 88.70 E-value: 3.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 20 PEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDitnMSVVKRTSF---LSRVFQDPKLG 96
Cdd:cd03252 12 PDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHD---LALADPAWLrrqVGVVLQENVLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 97 TAprmTVAENLLLAEKRGGHHHLV-PRKLKGEmkrfKEITAKMNNNLDHRLNTATGSLSGGQRQALSFLMATIKKPGILL 175
Cdd:cd03252 89 NR---SIRDNIALADPGMSMERVIeAAKLAGA----HDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 176 LDEHTAALDPKTS----QNLMDITDetikeqNLTCLMITHHLEdALKYGNRLLVLHQGKISYDisGEDKQKLTKEELLTF 251
Cdd:cd03252 162 FDEATSALDYESEhaimRNMHDICA------GRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQ--GSHDELLAENGLYAY 232
|
....*
gi 927264579 252 FNDIQ 256
Cdd:cd03252 233 LYQLQ 237
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
16-250 |
4.38e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 90.29 E-value: 4.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 16 NEDTPEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKD------------------KDITNM 77
Cdd:PRK13631 32 DEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyigdkknnhelitnpysKKIKNF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 78 SVVKRTsfLSRVFQDPKLGTApRMTVAENLLLAekrgghhhlvPRKLKGEMKRFKEITAKMNNNL---DHRLNTATGSLS 154
Cdd:PRK13631 112 KELRRR--VSMVFQFPEYQLF-KDTIEKDIMFG----------PVALGVKKSEAKKLAKFYLNKMgldDSYLERSPFGLS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 155 GGQ--RQALSFLMATikKPGILLLDEHTAALDPKTSQNLMDITDETiKEQNLTCLMITHHLEDALKYGNRLLVLHQGKIS 232
Cdd:PRK13631 179 GGQkrRVAIAGILAI--QPEILIFDEPTAGLDPKGEHEMMQLILDA-KANNKTVFVITHTMEHVLEVADEVIVMDKGKIL 255
|
250
....*....|....*...
gi 927264579 233 ydISGEDKQKLTKEELLT 250
Cdd:PRK13631 256 --KTGTPYEIFTDQHIIN 271
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
19-231 |
6.01e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 89.12 E-value: 6.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 19 TPEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDIT----NMSVVKRTSFLSRVFQdpk 94
Cdd:PRK13641 16 TPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKKLRKKVSLVFQ--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 95 lgtAPRMTVAENLLLAEKRGGhhhlvPRKLKGEMKRFKEITAKMNNNL---DHRLNTATGSLSGGQ--RQALSFLMATik 169
Cdd:PRK13641 93 ---FPEAQLFENTVLKDVEFG-----PKNFGFSEDEAKEKALKWLKKVglsEDLISKSPFELSGGQmrRVAIAGVMAY-- 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 927264579 170 KPGILLLDEHTAALDPKTSQNLMDITDETIKEQNlTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:PRK13641 163 EPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGH-TVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
25-231 |
6.20e-21 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 86.50 E-value: 6.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSFLSRVFQDPKLGTAprmTVA 104
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQDDELFSG---SIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 105 ENLLlaekrgghhhlvprklkgemkrfkeitakmnnnldhrlntatgslSGGQRQALSFLMATIKKPGILLLDEHTAALD 184
Cdd:cd03246 94 ENIL---------------------------------------------SGGQRQRLGLARALYGNPRILVLDEPNSHLD 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 927264579 185 PKTSQNLMDITdETIKEQNLTCLMITHHLEdALKYGNRLLVLHQGKI 231
Cdd:cd03246 129 VEGERALNQAI-AALKAAGATRIVIAHRPE-TLASADRILVLEDGRV 173
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-234 |
6.55e-21 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 88.53 E-value: 6.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 3 KTIFQLKDVVKTVNEDtpeelNILDHVDLDIHEGDFITILGSNGAGKSTLfntiggnLRPTSGqVIYKDKDITNM----- 77
Cdd:PRK09984 2 QTIIRVEKLAKTFNQH-----QALHAVDLNIHHGEMVALLGPSGSGKSTL-------LRHLSG-LITGDKSAGSHiellg 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 78 SVVKRTSFLSR-----------VFQDPKLgtAPRMTVAENLLLAEKRGGHHHLVPRKLKGEMKRFKEITAKMNNNLDHRL 146
Cdd:PRK09984 69 RTVQREGRLARdirksrantgyIFQQFNL--VNRLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQALTRVGMVHFA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 147 NTATGSLSGGQRQALSFLMATIKKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVL 226
Cdd:PRK09984 147 HQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVAL 226
|
....*...
gi 927264579 227 HQGKISYD 234
Cdd:PRK09984 227 RQGHVFYD 234
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
22-215 |
8.71e-21 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 87.49 E-value: 8.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 22 ELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDK----DITN------MSVVKRT-----SFL 86
Cdd:COG4778 23 RLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQaspreiLALRRRTigyvsQFL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 87 sRVFqdpklgtaPRMT----VAENLLL-------AEKRGGH--HHL-VPRKLkgemkrfkeitakmnnnldHRLNTATgs 152
Cdd:COG4778 103 -RVI--------PRVSaldvVAEPLLErgvdreeARARAREllARLnLPERL-------------------WDLPPAT-- 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 927264579 153 LSGGQRQALSFLMATIKKPGILLLDEHTAALDPKTSQNLMDITDEtIKEQNLTCLMITHHLED 215
Cdd:COG4778 153 FSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEE-AKARGTAIIGIFHDEEV 214
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
12-231 |
1.64e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 87.74 E-value: 1.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 12 VKTVNEDTPEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRT-SFLSRVF 90
Cdd:PRK13644 4 LENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIrKLVGIVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 91 QDPKLGTAPRmTVAENLLLAEKrggHHHLVPRKLKGEMKRfkeitAKMNNNLDHRLNTATGSLSGGQRQALSFLMATIKK 170
Cdd:PRK13644 84 QNPETQFVGR-TVEEDLAFGPE---NLCLPPIEIRKRVDR-----ALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTME 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 927264579 171 PGILLLDEHTAALDPKTSQNLMditdETIK---EQNLTCLMITHHLEDaLKYGNRLLVLHQGKI 231
Cdd:PRK13644 155 PECLIFDEVTSMLDPDSGIAVL----ERIKklhEKGKTIVYITHNLEE-LHDADRIIVMDRGKI 213
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
2-231 |
2.14e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 87.48 E-value: 2.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 2 TKTIFQLKDVvkTVNEDTPEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVK 81
Cdd:PRK13650 1 MSNIIEVKNL--TFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 82 RTSFLSRVFQDPK---LGTAPRMTVAENLllaEKRG-GHHHLVPR-----KLKGeMKRFKEitakmnnnldhrlnTATGS 152
Cdd:PRK13650 79 IRHKIGMVFQNPDnqfVGATVEDDVAFGL---ENKGiPHEEMKERvnealELVG-MQDFKE--------------REPAR 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 927264579 153 LSGGQRQALSFLMATIKKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLeDALKYGNRLLVLHQGKI 231
Cdd:PRK13650 141 LSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDL-DEVALSDRVLVMKNGQV 218
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
25-246 |
2.47e-20 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 87.35 E-value: 2.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMS---VVKRTSFLSRVFQDPKlgtapRM 101
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYAskeVARRIGLLAQNATTPG-----DI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 102 TVAEnlLLAEKRGGHHHLVPRKLKGEMKrfkEITAKMN-NNLDHRLNTATGSLSGGQRQALSFLMATIKKPGILLLDEHT 180
Cdd:PRK10253 97 TVQE--LVARGRYPHQPLFTRWRKEDEE---AVTKAMQaTGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 927264579 181 AALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKISYDisGEDKQKLTKE 246
Cdd:PRK10253 172 TWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQ--GAPKEIVTAE 235
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
26-216 |
2.52e-20 |
|
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: 89.65 E-value: 2.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 26 LDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSFLSRVFQDPKLGTAprmTVAE 105
Cdd:TIGR02857 338 LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAG---TIAE 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 106 NLLLAeKRGGHHHLVPRKLkgEMKRFKEITAKMNNNLDHRLNTATGSLSGGQRQALSFLMATIKKPGILLLDEHTAALDP 185
Cdd:TIGR02857 415 NIRLA-RPDASDAEIREAL--ERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDA 491
|
170 180 190
....*....|....*....|....*....|.
gi 927264579 186 KTSQNLMDITDETIkeQNLTCLMITHHLEDA 216
Cdd:TIGR02857 492 ETEAEVLEALRALA--QGRTVLLVTHRLALA 520
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
25-233 |
4.04e-20 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 85.79 E-value: 4.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRP---TSGQVIYKDKDITNMSVVKRTSFLSrvfQDPKLgtAPRM 101
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKPDQFQKCVAYVR---QDDIL--LPGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 102 TVAENLLLAEkrgghHHLVPRKLKGEMKRFKEITAKMNNNLDHRL-NTATGSLSGGQRQALSFLMATIKKPGILLLDEHT 180
Cdd:cd03234 97 TVRETLTYTA-----ILRLPRKSSDAIRKKRVEDVLLRDLALTRIgGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 927264579 181 AALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKISY 233
Cdd:cd03234 172 SGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVY 224
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
24-236 |
4.47e-20 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 85.64 E-value: 4.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 24 NILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSFLSR----VFQDPKLgtAP 99
Cdd:PRK11629 23 DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQklgfIYQFHHL--LP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 100 RMTVAENLLLAEKRGGhhhlvpRKLKGEMKRFKEITAKMnnNLDHRLNTATGSLSGGQRQALSFLMATIKKPGILLLDEH 179
Cdd:PRK11629 101 DFTALENVAMPLLIGK------KKPAEINSRALEMLAAV--GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 927264579 180 TAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDAlKYGNRLLVLHQGKISYDIS 236
Cdd:PRK11629 173 TGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLA-KRMSRQLEMRDGRLTAELS 228
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
19-231 |
4.92e-20 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 88.59 E-value: 4.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 19 TPEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIggnLR--PTSGQVIYKDKDITNMSVVKRTSFLSR---VFQDP 93
Cdd:COG4172 295 TVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLAL---LRliPSEGEIRFDGQDLDGLSRRALRPLRRRmqvVFQDP 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 94 kLGT-APRMTVAEnlLLAEkrGGHHHLVPRKLKGEMKRFKEITAKMNnnldhrLNTATGS-----LSGGQRQALSFLMAT 167
Cdd:COG4172 372 -FGSlSPRMTVGQ--IIAE--GLRVHGPGLSAAERRARVAEALEEVG------LDPAARHrypheFSGGQRQRIAIARAL 440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 927264579 168 IKKPGILLLDEHTAALDpKTSQN-----LMDITdetiKEQNLTCLMITHHLE--DALkyGNRLLVLHQGKI 231
Cdd:COG4172 441 ILEPKLLVLDEPTSALD-VSVQAqildlLRDLQ----REHGLAYLFISHDLAvvRAL--AHRVMVMKDGKV 504
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-231 |
1.62e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 85.55 E-value: 1.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 5 IFQLKDVVKTVNEDTpeelnILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITnMSVVKRTS 84
Cdd:COG4152 1 MLELKGLTKRFGDKT-----AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD-PEDRRRIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 85 FL--SRvfqdpklGTAPRMTVAENLL-LAEKRGGHHHLVPRKLKGEMKRFkeitakmnnNLDHRLNTATGSLSGGQRQAL 161
Cdd:COG4152 75 YLpeER-------GLYPKMKVGEQLVyLARLKGLSKAEAKRRADEWLERL---------GLGDRANKKVEELSKGNQQKV 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 162 SFLMATIKKPGILLLDEHTAALDPKTSQNLMDITDEtIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:COG4152 139 QLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRE-LAAKGTTVIFSSHQMELVEELCDRIVIINKGRK 207
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
26-231 |
1.67e-19 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 85.94 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 26 LDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSFLSR---VFQDPKLGTAPRMT 102
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLRRRmqmVFQDPYASLNPRMT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 103 V----AENLLLaekrgghHHLVPRKlkGEMKRFKEITAKMnnnldhRLNTATGS-----LSGGQRQ------ALSFlmat 167
Cdd:COG4608 114 VgdiiAEPLRI-------HGLASKA--ERRERVAELLELV------GLRPEHADrypheFSGGQRQrigiarALAL---- 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 927264579 168 ikKPGILLLDEHTAALDpKTSQ----NL-MDITDetikEQNLTCLMITH------HLEDalkygnRLLVLHQGKI 231
Cdd:COG4608 175 --NPKLIVCDEPVSALD-VSIQaqvlNLlEDLQD----ELGLTYLFISHdlsvvrHISD------RVAVMYLGKI 236
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
26-231 |
2.03e-19 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 86.94 E-value: 2.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 26 LDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSFLSRVFQDPKLGTaprMTVAE 105
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFN---RSIED 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 106 NL------------LLAEKRGGHHHLVPRKLKGemkrfkeitakmnnnldhrLNTATG----SLSGGQRQALSFLMATIK 169
Cdd:PRK13657 428 NIrvgrpdatdeemRAAAERAQAHDFIERKPDG-------------------YDTVVGergrQLSGGERQRLAIARALLK 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 927264579 170 KPGILLLDEHTAALDPKTSQNLMDITDETIKeqNLTCLMITHHLEdALKYGNRLLVLHQGKI 231
Cdd:PRK13657 489 DPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLS-TVRNADRILVFDNGRV 547
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
22-231 |
4.76e-19 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 84.93 E-value: 4.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 22 ELNI---LDHVDLDIHE---GDFIT-ILGSNGAGKSTLFNTIGGNLRPTSG------QVIYKDKDITNMSVVKRTsfLSR 88
Cdd:PRK11144 3 ELNFkqqLGDLCLTVNLtlpAQGITaIFGRSGAGKTSLINAISGLTRPQKGrivlngRVLFDAEKGICLPPEKRR--IGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 89 VFQDPKLgtAPRMTVAENLLLAekrgghhhlvprkLKGEMK-RFKEITAKMNnnLDHRLNTATGSLSGGQRQALSFLMAT 167
Cdd:PRK11144 81 VFQDARL--FPHYKVRGNLRYG-------------MAKSMVaQFDKIVALLG--IEPLLDRYPGSLSGGEKQRVAIGRAL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 927264579 168 IKKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:PRK11144 144 LTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKV 207
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
31-231 |
4.81e-19 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 85.47 E-value: 4.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 31 LDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVK----RTSFLSRVFQDPKLgtAPRMTVAEN 106
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevRRKKIAMVFQSFAL--MPHMTVLDN 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 107 LLLAEKRGGhhhlvprkLKGEMKRFKEITAKMNNNLDHRLNTATGSLSGGQRQALSFLMATIKKPGILLLDEHTAALDPK 186
Cdd:PRK10070 127 TAFGMELAG--------INAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 927264579 187 TSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:PRK10070 199 IRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
8-250 |
5.34e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 83.90 E-value: 5.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 8 LKDVVKTVNEDTPEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDI-TNMSVVKRTSFL 86
Cdd:PRK13645 9 LDNVSYTYAKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpANLKKIKEVKRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 87 SR----VFQDPKL----GTAPRMTVAENLLLAEKRGGHHHLVPRKLKgeMKRFKEITAKmnnnldhrlnTATGSLSGGQ- 157
Cdd:PRK13645 89 RKeiglVFQFPEYqlfqETIEKDIAFGPVNLGENKQEAYKKVPELLK--LVQLPEDYVK----------RSPFELSGGQk 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 158 -RQALSFLMATIKKpgILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKIsYDIs 236
Cdd:PRK13645 157 rRVALAGIIAMDGN--TLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKV-ISI- 232
|
250
....*....|....
gi 927264579 237 GEDKQKLTKEELLT 250
Cdd:PRK13645 233 GSPFEIFSNQELLT 246
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
22-231 |
5.86e-19 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 83.48 E-value: 5.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 22 ELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDIT-------NMSVVKRTSF------LSR 88
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgQLKVADKNQLrllrtrLTM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 89 VFQDPKLGTapRMTVAENLLLAekrgghhhlvPRKLKGEMK---RFKEITAKMNNNLDHRLNTATGS-LSGGQRQALSFL 164
Cdd:PRK10619 97 VFQHFNLWS--HMTVLENVMEA----------PIQVLGLSKqeaRERAVKYLAKVGIDERAQGKYPVhLSGGQQQRVSIA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 927264579 165 MATIKKPGILLLDEHTAALDPKTSQNLMDITdETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:PRK10619 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIM-QQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
24-235 |
6.91e-19 |
|
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: 81.88 E-value: 6.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 24 NILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSvvkrtSFLSRV---FQDPklGTAPR 100
Cdd:cd03268 14 RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNI-----EALRRIgalIEAP--GFYPN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 101 MTVAENLLLaekrgghHHLVPRKLKGEMKRFKEITakmnnNLDHRLNTATGSLSGGQRQALSFLMATIKKPGILLLDEHT 180
Cdd:cd03268 87 LTARENLRL-------LARLLGIRKKRIDEVLDVV-----GLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 927264579 181 AALDPKTSQNLMDITdETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKISYDI 235
Cdd:cd03268 155 NGLDPDGIKELRELI-LSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
25-231 |
7.22e-19 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 81.80 E-value: 7.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGN--LRPTSGQVIYKDKDITNMSVVKRTS---FLSrvFQDPklgtap 99
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERARlgiFLA--FQYP------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 100 rmtvaenlllaekrgghhhlvprklkgemkrfKEITAKMNNNLDHRLNTatgSLSGGQRQALSFLMATIKKPGILLLDEH 179
Cdd:cd03217 87 --------------------------------PEIPGVKNADFLRYVNE---GFSGGEKKRNEILQLLLLEPDLAILDEP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 927264579 180 TAALDpktSQNLMDITD--ETIKEQNLTCLMITHHlEDALKY--GNRLLVLHQGKI 231
Cdd:cd03217 132 DSGLD---IDALRLVAEviNKLREEGKSVLIITHY-QRLLDYikPDRVHVLYDGRI 183
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
26-250 |
7.46e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 85.35 E-value: 7.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 26 LDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVvkRTSFLSRV---FQDpkLGTAPRMT 102
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFAST--TAALAAGVaiiYQE--LHLVPEMT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 103 VAENLLLAE--KRGGhhhLVPRKLKgeMKRFKEITAKMNNNLDHrlNTATGSLSGGQRQALSFLMATIKKPGILLLDEHT 180
Cdd:PRK11288 96 VAENLYLGQlpHKGG---IVNRRLL--NYEAREQLEHLGVDIDP--DTPLKYLSIGQRQMVEIAKALARNARVIAFDEPT 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 181 AALDPKTSQNLMDITDEtIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKisYDISGEDKQKLTKEELLT 250
Cdd:PRK11288 169 SSLSAREIEQLFRVIRE-LRAEGRVILYVSHRMEEIFALCDAITVFKDGR--YVATFDDMAQVDRDQLVQ 235
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-231 |
1.13e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 84.73 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 8 LKDVVKTVNEDTpeelnILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIyKDKDItnmsvvkRTSFLS 87
Cdd:COG0488 1 LENLSKSFGGRP-----LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVS-IPKGL-------RIGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 88 rvfQDPKLGtaPRMTVAENLLlaekrGGHHHLvpRKLkgeMKRFKEITAKMNN---------------------NLDHR- 145
Cdd:COG0488 68 ---QEPPLD--DDLTVLDTVL-----DGDAEL--RAL---EAELEELEAKLAEpdedlerlaelqeefealggwEAEARa 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 146 -------------LNTATGSLSGGQR------QALsflmatIKKPGILLLDEHTaaldpktsqNLMDItdETIK--EQNL 204
Cdd:COG0488 133 eeilsglgfpeedLDRPVSELSGGWRrrvalaRAL------LSEPDLLLLDEPT---------NHLDL--ESIEwlEEFL 195
|
250 260 270
....*....|....*....|....*....|....
gi 927264579 205 -----TCLMITH--HLEDALkyGNRLLVLHQGKI 231
Cdd:COG0488 196 knypgTVLVVSHdrYFLDRV--ATRILELDRGKL 227
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
29-231 |
1.29e-18 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 82.28 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 29 VDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDK-----DITNMSVVKRtSFLSR-----VFQDPKLGTa 98
Cdd:PRK11701 25 VSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAER-RRLLRtewgfVHQHPRDGL- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 99 pRMTV------AENLLLAekrGGHHHLVPRKLKGEMKRFKEITAKmnnnldhRLNTATGSLSGGQRQALSFLMATIKKPG 172
Cdd:PRK11701 103 -RMQVsaggniGERLMAV---GARHYGDIRATAGDWLERVEIDAA-------RIDDLPTTFSGGMQQRLQIARNLVTHPR 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 927264579 173 ILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:PRK11701 172 LVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRV 230
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
39-250 |
2.23e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 82.16 E-value: 2.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 39 ITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSFLSRVFQDPK---LGTAPRMTVA---ENLLLAEK 112
Cdd:PRK13652 33 IAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPDdqiFSPTVEQDIAfgpINLGLDEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 113 RGGHHHLVPRKLKGemkrfkeitakmnnnLDHRLNTATGSLSGGQRQALSFLMATIKKPGILLLDEHTAALDPKTSQNLM 192
Cdd:PRK13652 113 TVAHRVSSALHMLG---------------LEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELI 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 927264579 193 DITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKISydISGEDKQKLTKEELLT 250
Cdd:PRK13652 178 DFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIV--AYGTVEEIFLQPDLLA 233
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
8-232 |
2.59e-18 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 83.16 E-value: 2.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 8 LKDVVKTVNEDTpeelnILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTsfLS 87
Cdd:PRK11000 6 LRNVTKAYGDVV-----ISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERG--VG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 88 RVFQDPKLgtAPRMTVAENLLLAekrgghhhlvpRKLKGEMKRfkEITAKMNN-----NLDHRLNTATGSLSGGQRQALS 162
Cdd:PRK11000 79 MVFQSYAL--YPHLSVAENMSFG-----------LKLAGAKKE--EINQRVNQvaevlQLAHLLDRKPKALSGGQRQRVA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 927264579 163 FLMATIKKPGILLLDEHTAALDPKTSQNlMDItdETIK-EQNLTCLMI--THHLEDALKYGNRLLVLHQGKIS 232
Cdd:PRK11000 144 IGRTLVAEPSVFLLDEPLSNLDAALRVQ-MRI--EISRlHKRLGRTMIyvTHDQVEAMTLADKIVVLDAGRVA 213
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
25-230 |
2.70e-18 |
|
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: 80.21 E-value: 2.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQViykdkditnmSVVKRTSFLSrvfQDPKLgtaPRMTVA 104
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV----------SVPGSIAYVS---QEPWI---QNGTIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 105 ENLLLAEKRgghhhlvprklkgEMKRFKE-ITA----KMNNNLDHRLNTATG----SLSGGQRQALSFLMATIKKPGILL 175
Cdd:cd03250 84 ENILFGKPF-------------DEERYEKvIKAcalePDLEILPDGDLTEIGekgiNLSGGQKQRISLARAVYSDADIYL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 927264579 176 LDEHTAALDPKTSQNLMD--ITDETIKeqNLTCLMITHHLEdALKYGNRLLVLHQGK 230
Cdd:cd03250 151 LDDPLSAVDAHVGRHIFEncILGLLLN--NKTRILVTHQLQ-LLPHADQIVVLDNGR 204
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
7-231 |
3.76e-18 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 80.90 E-value: 3.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 7 QLKDVVKTVNEDTpeelnILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMS---VVKRT 83
Cdd:COG4604 3 EIKNVSKRYGGKV-----VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPsreLAKRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 84 SFLSrvfQDPKLGTapRMTVAEnlLLAEKRGGHHhlvprklKGEMKrfKEITAKMNNNLD--------HR-LNTatgsLS 154
Cdd:COG4604 78 AILR---QENHINS--RLTVRE--LVAFGRFPYS-------KGRLT--AEDREIIDEAIAyldledlaDRyLDE----LS 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 927264579 155 GGQRQaLSFL-MATIKKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:COG4604 138 GGQRQ-RAFIaMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRV 214
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-248 |
6.79e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 82.38 E-value: 6.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 3 KTIFQLKDVvkTVNEDTPEELniLDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKR 82
Cdd:COG3845 255 EVVLEVENL--SVRDDRGVPA--LKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRER 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 83 TSF-LSRVFQDP-KLGTAPRMTVAENLLLaekrgGHHHLvPRKLKGEMKRFKEI---TAKMNNNLDHR---LNTATGSLS 154
Cdd:COG3845 331 RRLgVAYIPEDRlGRGLVPDMSVAENLIL-----GRYRR-PPFSRGGFLDRKAIrafAEELIEEFDVRtpgPDTPARSLS 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 155 GG--QRqalsFLMA--TIKKPGILLLDEHTAALDPKTS----QNLMDitdetIKEQNLTCLMITHHLEDALKYGNRLLVL 226
Cdd:COG3845 405 GGnqQK----VILAreLSRDPKLLIAAQPTRGLDVGAIefihQRLLE-----LRDAGAAVLLISEDLDEILALSDRIAVM 475
|
250 260
....*....|....*....|..
gi 927264579 227 HQGKISYDISGEDkqkLTKEEL 248
Cdd:COG3845 476 YEGRIVGEVPAAE---ATREEI 494
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
22-212 |
7.39e-18 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 78.94 E-value: 7.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 22 ELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSFLSRVFQDpklGTAPRM 101
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLP---GLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 102 TVAENLllaekrgghhHLVPRKLKGEMKRFKEITAKMNnnLDHRLNTATGSLSGGQRQALSFLMATIKKPGILLLDEHTA 181
Cdd:TIGR01189 89 SALENL----------HFWAAIHGGAQRTIEDALAAVG--LTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170 180 190
....*....|....*....|....*....|.
gi 927264579 182 ALDPKTSQNLMDITDETIKEQNLTcLMITHH 212
Cdd:TIGR01189 157 ALDKAGVALLAGLLRAHLARGGIV-LLTTHQ 186
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
5-231 |
2.40e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 79.39 E-value: 2.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 5 IFQLKDVVKTVNEDTPEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTS 84
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 85 FLSR----VFQDPKlGTAPRMTVAENLLLAEKRGGHHHLVPRKLKGEMKRFKEITAKMnnnldhrLNTATGSLSGGQRQA 160
Cdd:PRK13643 81 PVRKkvgvVFQFPE-SQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEF-------WEKSPFELSGGQMRR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 927264579 161 LSFLMATIKKPGILLLDEHTAALDPKTSQNLMDITdETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:PRK13643 153 VAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLF-ESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHI 222
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
24-250 |
2.95e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.48 E-value: 2.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 24 NILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSF-LSRVFQDPKLgtAPRMT 102
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLgIYLVPQEPLL--FPNLS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 103 VAENLLLAekrgghhhlVPRKlKGEMKRFKEITAKMNNNLDhrLNTATGSLSGGQRQALSFLMATIKKPGILLLDEHTAA 182
Cdd:PRK15439 103 VKENILFG---------LPKR-QASMQKMKQLLAALGCQLD--LDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTAS 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 927264579 183 LDPKTSQNLMDITDEtIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKISydISGEDKQkLTKEELLT 250
Cdd:PRK15439 171 LTPAETERLFSRIRE-LLAQGVGIVFISHKLPEIRQLADRISVMRDGTIA--LSGKTAD-LSTDDIIQ 234
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
12-233 |
3.06e-17 |
|
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: 77.21 E-value: 3.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 12 VKTVNEDTPEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRP--TSGQVIYKDKDITNMSVVKRTSFlsrV 89
Cdd:cd03213 11 VTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDKRSFRKIIGY---V 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 90 FQDPKLgtAPRMTVAENLLLAEKrgghhhlvprkLKGemkrfkeitakmnnnldhrlntatgsLSGGQRQALSFLMATIK 169
Cdd:cd03213 88 PQDDIL--HPTLTVRETLMFAAK-----------LRG--------------------------LSGGERKRVSIALELVS 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 927264579 170 KPGILLLDEHTAALDPKTSQNLMDiTDETIKEQNLTCLMITHHL-EDALKYGNRLLVLHQGKISY 233
Cdd:cd03213 129 NPSLLFLDEPTSGLDSSSALQVMS-LLRRLADTGRTIICSIHQPsSEIFELFDKLLLLSQGRVIY 192
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
21-248 |
3.58e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 80.54 E-value: 3.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 21 EELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNM-----SVVKRTSFlSRVFQDPKL 95
Cdd:PRK10535 19 EQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLdadalAQLRREHF-GFIFQRYHL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 96 gtAPRMTVAENLLLAEKRGGhhhlVPRKLKgeMKRFKEITAKMnnNLDHRLNTATGSLSGGQRQALSFLMATIKKPGILL 175
Cdd:PRK10535 98 --LSHLTAAQNVEVPAVYAG----LERKQR--LLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVIL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 927264579 176 LDEHTAALDPKTSQNLMDITDEtIKEQNLTCLMITHHLEDALKyGNRLLVLHQGKISYDISGEDKQKLTKEEL 248
Cdd:PRK10535 168 ADEPTGALDSHSGEEVMAILHQ-LRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRNPPAQEKVNVAGGTE 238
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-230 |
3.62e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 79.08 E-value: 3.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 1 MTKTIFQLKDVVKTVNEDTpeelnILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVV 80
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKL-----VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 81 KRtsflSRVFQDPKLGTA-PRMTVAENLLLAEKRGGHHHLVPRKLKGEMKRFkeitAKMNNNLDHRLntatGSLSGGQRQ 159
Cdd:PRK13537 78 AR----QRVGVVPQFDNLdPDFTVRENLLVFGRYFGLSAAAARALVPPLLEF----AKLENKADAKV----GELSGGMKR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 927264579 160 ALSFLMATIKKPGILLLDEHTAALDPKtSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGK 230
Cdd:PRK13537 146 RLTLARALVNDPDVLVLDEPTTGLDPQ-ARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
22-248 |
3.83e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 79.89 E-value: 3.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 22 ELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSFLSRVFQDPKLG--TAP 99
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLSfeFDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 100 RMTVaenlllaeKRGGHHHLVPRKLKGEMKRFKEITAKMNNNLDHRLNTATGSLSGGQRQALSFLMATIKKPGILLLDEH 179
Cdd:PRK09536 95 RQVV--------EMGRTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEP 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 927264579 180 TAALDPKTSQNLMDITdETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKISydISGEDKQKLTKEEL 248
Cdd:PRK09536 167 TASLDINHQVRTLELV-RRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVR--AAGPPADVLTADTL 232
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
22-231 |
4.20e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 78.60 E-value: 4.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 22 ELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSFLSRVFQDPKlGTAPRM 101
Cdd:PRK13642 19 DVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPD-NQFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 102 TVAENLLLAEKRGGhhhlVPRKlkgEM-KRFKEITAKMNNnLDHRlNTATGSLSGGQRQALSFLMATIKKPGILLLDEHT 180
Cdd:PRK13642 98 TVEDDVAFGMENQG----IPRE---EMiKRVDEALLAVNM-LDFK-TREPARLSGGQKQRVAVAGIIALRPEIIILDEST 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 927264579 181 AALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKyGNRLLVLHQGKI 231
Cdd:PRK13642 169 SMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEI 218
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
25-187 |
4.83e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 76.84 E-value: 4.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSFLSrvfqdPKLGTAPRMTVA 104
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG-----HRNAMKPALTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 105 ENLLL-AEKRGGHHHLVPRKLkgemKRFkeitakmnnNLDHRLNTATGSLSGGQ--RQALSFLMATiKKPgILLLDEHTA 181
Cdd:PRK13539 92 ENLEFwAAFLGGEELDIAAAL----EAV---------GLAPLAHLPFGYLSAGQkrRVALARLLVS-NRP-IWILDEPTA 156
|
....*.
gi 927264579 182 ALDPKT 187
Cdd:PRK13539 157 ALDAAA 162
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
7-231 |
5.46e-17 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 79.12 E-value: 5.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 7 QLKDVVKTVNEDTPeelnILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTsfL 86
Cdd:PRK11650 5 KLQAVRKSYDGKTQ----VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRD--I 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 87 SRVFQDPKLgtAPRMTVAENLLLAEK-RGghhhlVPrklKGEMKRFKEITAKMnNNLDHRLNTATGSLSGGQRQALSFLM 165
Cdd:PRK11650 79 AMVFQNYAL--YPHMSVRENMAYGLKiRG-----MP---KAEIEERVAEAARI-LELEPLLDRKPRELSGGQRQRVAMGR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 927264579 166 ATIKKPGILLLDEHTAALDPKtsqnL---MDItdETIKEQ---NLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:PRK11650 148 AIVREPAVFLFDEPLSNLDAK----LrvqMRL--EIQRLHrrlKTTSLYVTHDQVEAMTLADRVVVMNGGVA 213
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-249 |
7.37e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 77.39 E-value: 7.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLR------PTSGQVIYKDKDITNMSVVKRTSFLSRVFQDPKlgTA 98
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPN--PF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 99 PRMTVAENLLLAEKRGGhhhlvpRKLKGEMKRFKEITAK---MNNNLDHRLNTATGSLSGGQRQALSFLMATIKKPGILL 175
Cdd:PRK14246 103 PHLSIYDNIAYPLKSHG------IKEKREIKKIVEECLRkvgLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 927264579 176 LDEHTAALDPKTSQNLMDITDETIKEqnLTCLMITHHLEDALKYGNRLLVLHQGKI-----SYDISGEDKQKLTKEELL 249
Cdd:PRK14246 177 MDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELvewgsSNEIFTSPKNELTEKYVI 253
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-231 |
8.02e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 79.48 E-value: 8.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 20 PEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDIT---------NMSVVKRtsflsRV- 89
Cdd:PRK11160 350 DQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIAdyseaalrqAISVVSQ-----RVh 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 90 -FQDpklgtaprmTVAENLLLAEKRGGHHHLVprklkgemkrfkEITAKMN-NNL---DHRLNTATGS----LSGGQRQA 160
Cdd:PRK11160 425 lFSA---------TLRDNLLLAAPNASDEALI------------EVLQQVGlEKLledDKGLNAWLGEggrqLSGGEQRR 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 927264579 161 LSFLMATIKKPGILLLDEHTAALDPKTSQNLMDITDETIkeQNLTCLMITHHLEdALKYGNRLLVLHQGKI 231
Cdd:PRK11160 484 LGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA--QNKTVLMITHRLT-GLEQFDRICVMDNGQI 551
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
8-231 |
8.17e-17 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 77.10 E-value: 8.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 8 LKDVVKTVNEDTpeelnILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDI-TNMSVVKRTSFL 86
Cdd:PRK11264 6 VKNLVKKFHGQT-----VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdTARSLSQQKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 87 SR-------VFQDPKLgtAPRMTVAENLLLAekrgghhhlvPRKLKGE-----MKRFKEITAKMnnNLDHRLNTATGSLS 154
Cdd:PRK11264 81 RQlrqhvgfVFQNFNL--FPHRTVLENIIEG----------PVIVKGEpkeeaTARARELLAKV--GLAGKETSYPRRLS 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 927264579 155 GGQRQALSFLMATIKKPGILLLDEHTAALDPKTSQNLMDiTDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:PRK11264 147 GGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLN-TIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
22-231 |
9.23e-17 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 77.15 E-value: 9.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 22 ELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIggNL--RPTSGQVIYKDKDI------------TNMSVVKRT-SFL 86
Cdd:COG4598 20 DLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCI--NLleTPDSGEIRVGGEEIrlkpdrdgelvpADRRQLQRIrTRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 87 SRVFQDPKLGtaPRMTVAENLLLAekrgghhhlvPRKLKGEMKrfKEITAKMNNNLD-----HRLNTATGSLSGGQRQAL 161
Cdd:COG4598 98 GMVFQSFNLW--SHMTVLENVIEA----------PVHVLGRPK--AEAIERAEALLAkvglaDKRDAYPAHLSGGQQQRA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 927264579 162 SFLMATIKKPGILLLDEHTAALDP-------KTSQNLmditdetiKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:COG4598 164 AIARALAMEPEVMLFDEPTSALDPelvgevlKVMRDL--------AEEGRTMLVVTHEMGFARDVSSHVVFLHQGRI 232
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-231 |
1.21e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 78.95 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 3 KTIFQLKDVVKTVNEDTpeelnILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVI--------YKDKDI 74
Cdd:COG0488 313 KKVLELEGLSKSYGDKT-----LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKlgetvkigYFDQHQ 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 75 TNMSvvkrtsflsrvfqdpklgtaPRMTVAENLllaekRGGHHHLVPRKLKGEMKRFkeitakmnnNLD-HRLNTATGSL 153
Cdd:COG0488 388 EELD--------------------PDKTVLDEL-----RDGAPGGTEQEVRGYLGRF---------LFSgDDAFKPVGVL 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 154 SGGQRQALSFLMATIKKPGILLLDEHTAALDPKTSQNLmditdetikEQNL-----TCLMITH--HLEDALkyGNRLLVL 226
Cdd:COG0488 434 SGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEAL---------EEALddfpgTVLLVSHdrYFLDRV--ATRILEF 502
|
....*
gi 927264579 227 HQGKI 231
Cdd:COG0488 503 EDGGV 507
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
24-231 |
1.24e-16 |
|
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: 76.36 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 24 NILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSFLSRVFQDPK--------- 94
Cdd:cd03248 28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPVlfarslqdn 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 95 ----LGTAPRMTVAEnllLAEKRGGHHHLvprklkgemkrfkeitAKMNNNLDHRLNTATGSLSGGQRQALSFLMATIKK 170
Cdd:cd03248 108 iaygLQSCSFECVKE---AAQKAHAHSFI----------------SELASGYDTEVGEKGSQLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 927264579 171 PGILLLDEHTAALDPKTSQNLMDITDETikEQNLTCLMITHHLEdALKYGNRLLVLHQGKI 231
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDW--PERRTVLVIAHRLS-TVERADQILVLDGGRI 226
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
26-231 |
1.37e-16 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 78.69 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 26 LDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYK--DK--DITNMSVVKR---TSFLSRVFQDPKLgtA 98
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgDEwvDMTKPGPDGRgraKRYIGILHQEYDL--Y 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 99 PRMTVAENLLLAekrgghhhlVPRKLKGEMKRFKE-ITAKMNNNLDHR----LNTATGSLSGGQRQALSFLMATIKKPGI 173
Cdd:TIGR03269 378 PHRTVLDNLTEA---------IGLELPDELARMKAvITLKMVGFDEEKaeeiLDKYPDELSEGERHRVALAQVLIKEPRI 448
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 927264579 174 LLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:TIGR03269 449 VILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-222 |
1.78e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 76.35 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 1 MTKTIFQLKDVVKTVNEDtpeelNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIG--GNLRP---TSGQVIYKDKDI- 74
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKK-----KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPevtITGSIVYNGHNIy 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 75 -TNMSVVKRTSFLSRVFQDPKlgTAPrMTVAENLLLAEKRGGHH------HLVPRKLKGemkrfkeitAKMNNNLDHRLN 147
Cdd:PRK14239 76 sPRTDTVDLRKEIGMVFQQPN--PFP-MSIYENVVYGLRLKGIKdkqvldEAVEKSLKG---------ASIWDEVKDRLH 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 927264579 148 TATGSLSGGQRQALSFLMATIKKPGILLLDEHTAALDPKTSQNLMDiTDETIKEQnLTCLMITHHLEDALKYGNR 222
Cdd:PRK14239 144 DSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEE-TLLGLKDD-YTMLLVTRSMQQASRISDR 216
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
26-251 |
2.30e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 77.05 E-value: 2.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 26 LDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQV------IYKDkditnmsvvkRTSFLSR---VF------ 90
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVrvlgyvPFKR----------RKEFARRigvVFgqrsql 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 91 -QDpklgtaprMTVAENLLLaekrggHHHL--VPRKlkgemkRFKEITAKMNN--NLDHRLNTATGSLSGGQRQALSFLM 165
Cdd:COG4586 108 wWD--------LPAIDSFRL------LKAIyrIPDA------EYKKRLDELVEllDLGELLDTPVRQLSLGQRMRCELAA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 166 ATIKKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKISYDISGED-KQKLT 244
Cdd:COG4586 168 ALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEElKERFG 247
|
....*..
gi 927264579 245 KEELLTF 251
Cdd:COG4586 248 PYKTIVL 254
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-231 |
2.65e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 76.38 E-value: 2.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 1 MTKTIFQLKDVVKTVnEDTPEElnILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQviykDKDIT--NMS 78
Cdd:PRK13640 1 MKDNIVEFKHVSFTY-PDSKKP--ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNP----NSKITvdGIT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 79 VVKRTSFLSR-----VFQDPK---LGTAPRMTVAENLllaEKRGghhhlVPRKlkgEMKRfkeITAKMNNNLD--HRLNT 148
Cdd:PRK13640 74 LTAKTVWDIRekvgiVFQNPDnqfVGATVGDDVAFGL---ENRA-----VPRP---EMIK---IVRDVLADVGmlDYIDS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 149 ATGSLSGGQRQ--ALSFLMATikKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDAlKYGNRLLVL 226
Cdd:PRK13640 140 EPANLSGGQKQrvAIAGILAV--EPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVL 216
|
....*
gi 927264579 227 HQGKI 231
Cdd:PRK13640 217 DDGKL 221
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
2-231 |
3.00e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 75.98 E-value: 3.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 2 TKTIFQLKDVVKTVNEDTpeelnILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSvvk 81
Cdd:PRK10575 8 SDTTFALRNVSFRVPGRT-----LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWS--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 82 RTSFLSRVFQDPK-LGTAPRMTVAEnlLLAEKRGGHHHLVPRKLKGEMKRFKE-ITAKMNNNLDHRLntaTGSLSGGQRQ 159
Cdd:PRK10575 80 SKAFARKVAYLPQqLPAAEGMTVRE--LVAIGRYPWHGALGRFGAADREKVEEaISLVGLKPLAHRL---VDSLSGGERQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 927264579 160 ALSFLMATIKKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:PRK10575 155 RAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEM 226
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
25-231 |
3.88e-16 |
|
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: 74.96 E-value: 3.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIggnLR---PTSGQVIYKDKDITNmsvVKRTSFLSR---VFQDPKLGTA 98
Cdd:cd03253 16 VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLL---FRfydVSSGSILIDGQDIRE---VTLDSLRRAigvVPQDTVLFND 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 99 prmTVAENLLL------------AEKRGGHHhlvprklkGEMKRFKEitakmnnnldhRLNTATGS----LSGGQRQALS 162
Cdd:cd03253 90 ---TIGYNIRYgrpdatdeevieAAKAAQIH--------DKIMRFPD-----------GYDTIVGErglkLSGGEKQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 927264579 163 FLMATIKKPGILLLDEHTAALDPKTSQNLMDITDETIKeqNLTCLMITHHLE---DALKygnrLLVLHQGKI 231
Cdd:cd03253 148 IARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLStivNADK----IIVLKDGRI 213
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
26-238 |
5.07e-16 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 74.53 E-value: 5.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 26 LDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVvKRTSFLSR----VFQDPKLgtAPRM 101
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKN-REVPFLRRqigmIFQDHHL--LMDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 102 TVAENLLLAekrgghhhLVPRKLKGEMKRfKEITAKMNNN--LDHRLNTATgSLSGGQRQALSFLMATIKKPGILLLDEH 179
Cdd:PRK10908 95 TVYDNVAIP--------LIIAGASGDDIR-RRVSAALDKVglLDKAKNFPI-QLSGGEQQRVGIARAVVNKPAVLLADEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 927264579 180 TAALDPKTSQNLMDITDEtIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKISYDISGE 238
Cdd:PRK10908 165 TGNLDDALSEGILRLFEE-FNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGGVGGE 222
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-250 |
5.33e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 76.89 E-value: 5.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 1 MTKTIFQLKDVVKTVNEdtpeeLNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGnLRPT---SGQVIYKDKDITNM 77
Cdd:PRK13549 1 MMEYLLEMKNITKTFGG-----VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEIIFEGEELQAS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 78 SVvKRTSFLSRVFQDPKLGTAPRMTVAENLLLAEK--RGGHHHLvprklkGEM-KRFKEITAKMNnnLDHRLNTATGSLS 154
Cdd:PRK13549 75 NI-RDTERAGIAIIHQELALVKELSVLENIFLGNEitPGGIMDY------DAMyLRAQKLLAQLK--LDINPATPVGNLG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 155 GGQRQALSFLMATIKKPGILLLDEHTAALDPKTSQNLMDITDEtIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKisyD 234
Cdd:PRK13549 146 LGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRD-LKAHGIACIYISHKLNEVKAISDTICVIRDGR---H 221
|
250
....*....|....*.
gi 927264579 235 ISGEDKQKLTKEELLT 250
Cdd:PRK13549 222 IGTRPAAGMTEDDIIT 237
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-231 |
8.85e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 74.49 E-value: 8.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNT------------IGGNLRpTSGQVIYkDKDITNMSVVKRTSFlsrVFQD 92
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrllelneearVEGEVR-LFGRNIY-SPDVDPIEVRREVGM---VFQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 93 PKlgTAPRMTVAENLLLAEKRGGhhhLV-PRKLKGEMKRFKEITAKMNNNLDHRLNTATGSLSGGQRQALSFLMATIKKP 171
Cdd:PRK14267 94 PN--PFPHLTIYDNVAIGVKLNG---LVkSKKELDERVEWALKKAALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 172 GILLLDEHTAALDPKTSQNLMDITDETIKEqnLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:PRK14267 169 KILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKL 226
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
7-250 |
9.22e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 76.70 E-value: 9.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 7 QLKDVVKTVNEDTPEelnILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSFL 86
Cdd:PLN03130 1239 KFEDVVLRYRPELPP---VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVL 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 87 SRVFQDPKLGTAprmTVAENLllaeKRGGHHHLVPRKLKGEMKRFKEITAKMNNNLDHRLNTATGSLSGGQRQALSFLMA 166
Cdd:PLN03130 1316 GIIPQAPVLFSG---TVRFNL----DPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARA 1388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 167 TIKKPGILLLDEHTAALDPKTSQnlmdITDETIKEQNLTCLM--ITHHLEDALKyGNRLLVLHQGKI-SYDisgedkqkl 243
Cdd:PLN03130 1389 LLRRSKILVLDEATAAVDVRTDA----LIQKTIREEFKSCTMliIAHRLNTIID-CDRILVLDAGRVvEFD--------- 1454
|
....*..
gi 927264579 244 TKEELLT 250
Cdd:PLN03130 1455 TPENLLS 1461
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
25-231 |
9.29e-16 |
|
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: 76.52 E-value: 9.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSFLSRVFQDPKLGTAP-RMTV 103
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSlRMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 104 AENLLLAEKRgghhhlVPRKLkgEMKRFKEITAKMNNNLDHRLNTATGSLSGGQRQALSFLMATIKKPGILLLDEHTAAL 183
Cdd:TIGR00957 1381 DPFSQYSDEE------VWWAL--ELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAV 1452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 927264579 184 DPKTSqnlmDITDETIKEQNLTC--LMITHHLEDALKYgNRLLVLHQGKI 231
Cdd:TIGR00957 1453 DLETD----NLIQSTIRTQFEDCtvLTIAHRLNTIMDY-TRVIVLDKGEV 1497
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-231 |
1.20e-15 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 73.92 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 1 MTKTIFQLKDVVKTvnedtpEELNI-------LDHVDLDIHEGDFITILGSNGAGKSTL---FN----TIGGNlRpTSGQ 66
Cdd:COG1117 1 MTAPASTLEPKIEV------RNLNVyygdkqaLKDINLDIPENKVTALIGPSGCGKSTLlrcLNrmndLIPGA-R-VEGE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 67 VIYKDKDI--TNMSVVKrtsfLSR----VFQDPklgtAP-RMTVAENLLLAEKRGGHH------HLVPRKLKG-----EM 128
Cdd:COG1117 73 ILLDGEDIydPDVDVVE----LRRrvgmVFQKP----NPfPKSIYDNVAYGLRLHGIKskseldEIVEESLRKaalwdEV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 129 KrfkeitakmnnnldHRLNTATGSLSGGQRQ------ALsflmATikKPGILLLDEHTAALDPKTSQNLmditDETIKE- 201
Cdd:COG1117 145 K--------------DRLKKSALGLSGGQQQrlciarAL----AV--EPEVLLMDEPTSALDPISTAKI----EELILEl 200
|
250 260 270
....*....|....*....|....*....|.
gi 927264579 202 -QNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:COG1117 201 kKDYTIVIVTHNMQQAARVSDYTAFFYLGEL 231
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-223 |
1.24e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 73.66 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 2 TKTIFQLKDVVKTVNEDTpEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVK 81
Cdd:PRK10584 3 AENIVEVHHLKKSVGQGE-HELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 82 RTSFLSR----VFQDPKLgtAPRMTVAENLLLaekrgghhhlvPRKLKGEMKRFKEITAKM---NNNLDHRLNTATGSLS 154
Cdd:PRK10584 82 RAKLRAKhvgfVFQSFML--IPTLNALENVEL-----------PALLRGESSRQSRNGAKAlleQLGLGKRLDHLPAQLS 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 927264579 155 GGQRQALSFLMATIKKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRL 223
Cdd:PRK10584 149 GGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRL 217
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
26-249 |
1.28e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 75.83 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 26 LDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRT----SFLSRvfqDPK-LGTAPR 100
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIragiAYVPE---DRKgEGLVLD 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 101 MTVAENLLLAE-KRGGHHHLVPRklkgemKRFKEITAKMNNNLD---HRLNTATGSLSGG--QRQALSFLMATikKPGIL 174
Cdd:COG1129 345 LSIRENITLASlDRLSRGGLLDR------RRERALAEEYIKRLRiktPSPEQPVGNLSGGnqQKVVLAKWLAT--DPKVL 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 927264579 175 LLDEHTAALDPKTSQNLMDITDEtIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKISYDISGEDkqkLTKEELL 249
Cdd:COG1129 417 ILDEPTRGIDVGAKAEIYRLIRE-LAAEGKAVIVISSELPELLGLSDRILVMREGRIVGELDREE---ATEEAIM 487
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
32-230 |
1.32e-15 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 75.15 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 32 DIHEGDFITILGSNGAGKS-TLFNTIG---GNLRpTSGQVIYKDKDITNMSVVK----RTSFLSRVFQDPKLGTAPRMTV 103
Cdd:PRK09473 38 SLRAGETLGIVGESGSGKSqTAFALMGllaANGR-IGGSATFNGREILNLPEKElnklRAEQISMIFQDPMTSLNPYMRV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 104 AENLLLAekrgghhhLVPRKLKGEMKRFKEiTAKMnnnLD--------HRLNTATGSLSGGQRQALSFLMATIKKPGILL 175
Cdd:PRK09473 117 GEQLMEV--------LMLHKGMSKAEAFEE-SVRM---LDavkmpearKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLI 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 927264579 176 LDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGK 230
Cdd:PRK09473 185 ADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 239
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-250 |
1.40e-15 |
|
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: 75.63 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 5 IFQLKDVVKTVNEdtpeeLNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGnLRPT---SGQVIYKDKDITnMSVVK 81
Cdd:TIGR02633 1 LLEMKGIVKTFGG-----VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHgtwDGEIYWSGSPLK-ASNIR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 82 RTSFLSRVFQDPKLGTAPRMTVAENLLLAEK---RGG--HHHLVPRKLKGEMKRFKeiTAKMNNNLdhrlntATGSLSGG 156
Cdd:TIGR02633 74 DTERAGIVIIHQELTLVPELSVAENIFLGNEitlPGGrmAYNAMYLRAKNLLRELQ--LDADNVTR------PVGDYGGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 157 QRQALSFLMATIKKPGILLLDEHTAALDPKTSQNLMDITDEtIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKisyDIS 236
Cdd:TIGR02633 146 QQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRD-LKAHGVACVYISHKLNEVKAVCDTICVIRDGQ---HVA 221
|
250
....*....|....
gi 927264579 237 GEDKQKLTKEELLT 250
Cdd:TIGR02633 222 TKDMSTMSEDDIIT 235
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
20-231 |
1.52e-15 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 72.83 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 20 PEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSFLSRVFQDPKL--GT 97
Cdd:cd03369 18 PDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQDPTLfsGT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 98 aprmtvaenlllaekrgghhhlvprkLKGEMKRFKEITAKmnnNLDHRLNTATG--SLSGGQRQALSFLMATIKKPGILL 175
Cdd:cd03369 98 --------------------------IRSNLDPFDEYSDE---EIYGALRVSEGglNLSQGQRQLLCLARALLKRPRVLV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 927264579 176 LDEHTAALDPKTSQNLmditDETIKE--QNLTCLMITHHLEDALKYgNRLLVLHQGKI 231
Cdd:cd03369 149 LDEATASIDYATDALI----QKTIREefTNSTILTIAHRLRTIIDY-DKILVMDAGEV 201
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
7-231 |
2.14e-15 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 75.22 E-value: 2.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 7 QLKDVVKTVnedtpEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGG--NLRPTSGQVIYKDKDITNMSVVKRTS 84
Cdd:TIGR03269 2 EVKNLTKKF-----DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYHVALCEKCGYVERPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 85 FLSRvfQDPKLGTAPRM----------------------------------TVAENLLLAEKRGGHhhlvprKLKGEMKR 130
Cdd:TIGR03269 77 KVGE--PCPVCGGTLEPeevdfwnlsdklrrrirkriaimlqrtfalygddTVLDNVLEALEEIGY------EGKEAVGR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 131 FKEITAKMNnnLDHRLNTATGSLSGGQRQALSFLMATIKKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMIT 210
Cdd:TIGR03269 149 AVDLIEMVQ--LSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTS 226
|
250 260
....*....|....*....|.
gi 927264579 211 HHLEDALKYGNRLLVLHQGKI 231
Cdd:TIGR03269 227 HWPEVIEDLSDKAIWLENGEI 247
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
25-230 |
2.57e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 74.10 E-value: 2.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQviykdkdITNMSV-VKRTSFLSRVfqdpKLGTAPRM-- 101
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGK-------ITVLGVpVPARARLARA----RIGVVPQFdn 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 102 -----TVAENLLLAekrGGHHHLVPRKLKGEMKRFKEItAKMNNNLDHRLntatGSLSGGQRQALSFLMATIKKPGILLL 176
Cdd:PRK13536 125 ldlefTVRENLLVF---GRYFGMSTREIEAVIPSLLEF-ARLESKADARV----SDLSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 927264579 177 DEHTAALDPKtSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGK 230
Cdd:PRK13536 197 DEPTTGLDPH-ARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
3-231 |
3.79e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 72.90 E-value: 3.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 3 KTIFQLKDVVKTVNEDT----PEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMS 78
Cdd:PRK15112 2 ETLLEVRNLSKTFRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 79 VVKRTSFLSRVFQDPKLGTAPRMTVAENLllaekrgghhhLVPRKLKGEM---KRFKEI--TAKMNNNLDHRLNTATGSL 153
Cdd:PRK15112 82 YSYRSQRIRMIFQDPSTSLNPRQRISQIL-----------DFPLRLNTDLepeQREKQIieTLRQVGLLPDHASYYPHML 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 927264579 154 SGGQRQALSFLMATIKKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:PRK15112 151 APGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEV 228
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
29-246 |
5.02e-15 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 74.24 E-value: 5.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 29 VDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSFLSRVFQDPKL--------GTAPR 100
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLfdqllgpeGKPAN 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 101 MTVAENLLlaekrgghHHLvprklkgemkrfkeitaKMNNNL---DHRLntATGSLSGGQRQALSFLMATIKKPGILLLD 177
Cdd:PRK10522 422 PALVEKWL--------ERL-----------------KMAHKLeleDGRI--SNLKLSKGQKKRLALLLALAEERDILLLD 474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 178 EHTAALDPKTSQNLMDITDETIKEQNLTCLMITHhlEDA-LKYGNRLLVLHQGKISyDISGEDKQKLTKE 246
Cdd:PRK10522 475 EWAADQDPHFRREFYQVLLPLLQEMGKTIFAISH--DDHyFIHADRLLEMRNGQLS-ELTGEERDAASRD 541
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-213 |
5.66e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 72.38 E-value: 5.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLF------NTIGGNLRPTS-----GQVIYKDKdiTNMSVVKRTsfLSRVFQDP 93
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLkclnrmNELESEVRVEGrveffNQNIYERR--VNLNRLRRQ--VSMVHPKP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 94 KLGTaprMTVAENLLLAEKRGGHHhlvPRKLKGEMKRFKEITAKMNNNLDHRLNTATGSLSGGQRQALSFLMATIKKPGI 173
Cdd:PRK14258 98 NLFP---MSVYDNVAYGVKIVGWR---PKLEIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 927264579 174 LLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHL 213
Cdd:PRK14258 172 LLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNL 211
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-231 |
9.42e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 72.05 E-value: 9.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGG-NLRPT----SGQVIYKDKDITNM-SVVKRTSFLSRVFQDPKlgTA 98
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRmNDKVSgyrySGDVLLGGRSIFNYrDVLEFRRRVGMLFQRPN--PF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 99 PrMTVAENLLLAEKRgghHHLVPRKLKGEMKRFKEITAKMNNNLDHRLNTATGSLSGGQRQALSFLMATIKKPGILLLDE 178
Cdd:PRK14271 114 P-MSIMDNVLAGVRA---HKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDE 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 927264579 179 HTAALDPKTSQNLmditDETIKE--QNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:PRK14271 190 PTSALDPTTTEKI----EEFIRSlaDRLTVIIVTHNLAQAARISDRAALFFDGRL 240
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
25-231 |
1.01e-14 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 73.24 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSvvkRTSF------LSrvfQDPKL--G 96
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWD---REELgrhigyLP---QDVELfdG 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 97 TaprmtVAEN-----------LLLAEKRGGHHHLVprklkgemkrfkeitAKMNNNLDHRLNTATGSLSGGQRQALSFLM 165
Cdd:COG4618 421 T-----IAENiarfgdadpekVVAAAKLAGVHEMI---------------LRLPDGYDTRIGEGGARLSGGQRQRIGLAR 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 927264579 166 ATIKKPGILLLDEHTAALDPKTSQNLMD-ItdETIKEQNLTCLMITHHLEdALKYGNRLLVLHQGKI 231
Cdd:COG4618 481 ALYGDPRLVVLDEPNSNLDDEGEAALAAaI--RALKARGATVVVITHRPS-LLAAVDKLLVLRDGRV 544
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
25-231 |
1.38e-14 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 72.83 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSFLSRVFQDPKL--------- 95
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLfsgsvreni 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 96 GTAPRMTVAENLLLAEKRGGHHHLVprklkgemkrfkeitAKMNNNLDHRLNTATGSLSGGQRQALSFLMATIKKPGILL 175
Cdd:TIGR00958 576 AYGLTDTPDEEIMAAAKAANAHDFI---------------MEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLI 640
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 927264579 176 LDEHTAALDPKTSQNLMditdETIKEQNLTCLMITHHLEDALKyGNRLLVLHQGKI 231
Cdd:TIGR00958 641 LDEATSALDAECEQLLQ----ESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSV 691
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
25-231 |
3.53e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 71.67 E-value: 3.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMS-VVKRTSfLSRVFQDPKLGTAprmTV 103
Cdd:PRK10790 356 VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLShSVLRQG-VAMVQQDPVVLAD---TF 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 104 AENLLLAekRGGHHHLVPRKLkgEMKRFKEITAKMNNNLDHRLNTATGSLSGGQRQALSFLMATIKKPGILLLDEHTAAL 183
Cdd:PRK10790 432 LANVTLG--RDISEEQVWQAL--ETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANI 507
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 927264579 184 DPKTSQNLMDITdETIKEQNlTCLMITHHLEDALKyGNRLLVLHQGKI 231
Cdd:PRK10790 508 DSGTEQAIQQAL-AAVREHT-TLVVIAHRLSTIVE-ADTILVLHRGQA 552
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
20-232 |
5.78e-14 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 70.84 E-value: 5.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 20 PEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNmsvVKRTSFLSRVF---QDPKLG 96
Cdd:TIGR01842 328 GGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQ---WDRETFGKHIGylpQDVELF 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 97 TAprmTVAENL------------LLAEKRGGHHHLVprklkgemkrfkeitAKMNNNLDHRLNTATGSLSGGQRQALSFL 164
Cdd:TIGR01842 405 PG---TVAENIarfgenadpekiIEAAKLAGVHELI---------------LRLPDGYDTVIGPGGATLSGGQRQRIALA 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 927264579 165 MATIKKPGILLLDEHTAALDPKTSQNLMD-ITDetIKEQNLTCLMITHHLEdALKYGNRLLVLHQGKIS 232
Cdd:TIGR01842 467 RALYGDPKLVVLDEPNSNLDEEGEQALANaIKA--LKARGITVVVITHRPS-LLGCVDKILVLQDGRIA 532
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
25-229 |
8.73e-14 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 68.96 E-value: 8.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTsflsrVFQDPKLgtAPRMTVA 104
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGV-----VFQNEGL--LPWRNVQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 105 ENLLLAEKRGGhhhlVPRKLKGEMKRfkEITAKMN-NNLDHRLntaTGSLSGGQRQALSFLMATIKKPGILLLDEHTAAL 183
Cdd:PRK11248 89 DNVAFGLQLAG----VEKMQRLEIAH--QMLKKVGlEGAEKRY---IWQLSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 927264579 184 DPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQG 229
Cdd:PRK11248 160 DAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
26-249 |
1.06e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 68.99 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 26 LDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSFLSRVFQDPKlGTAPRMTVAE 105
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDPD-DQVFSSTVWD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 106 NLLLAekrgghhhlvPRKL---KGEMKRFKEITAKMNNNLDHRlNTATGSLSGGQ--RQALSFLMATikKPGILLLDEHT 180
Cdd:PRK13647 100 DVAFG----------PVNMgldKDEVERRVEEALKAVRMWDFR-DKPPYHLSYGQkkRVAIAGVLAM--DPDVIVLDEPM 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 927264579 181 AALDPKTSQNLMDITDEtIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKIsydISGEDKQKLTKEELL 249
Cdd:PRK13647 167 AYLDPRGQETLMEILDR-LHNQGKTVIVATHDVDLAAEWADQVIVLKEGRV---LAEGDKSLLTDEDIV 231
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
26-238 |
1.67e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 69.43 E-value: 1.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 26 LDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSF-LSRVFQDpkLGTAPRMTVA 104
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGIIYQE--LSVIDELTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 105 ENLLLAEkrgghhhLVPRKLKG----EMKRFKEITAKMNNNLDHR--LNTATGSLSGGQRQALSFLMATIKKPGILLLDE 178
Cdd:PRK09700 99 ENLYIGR-------HLTKKVCGvniiDWREMRVRAAMMLLRVGLKvdLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 179 HTAALDPKTSQNLMDITDEtIKEQNLTCLMITHHLEDALKYGNRLLVLHQGkiSYDISGE 238
Cdd:PRK09700 172 PTSSLTNKEVDYLFLIMNQ-LRKEGTAIVYISHKLAEIRRICDRYTVMKDG--SSVCSGM 228
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
26-229 |
1.88e-13 |
|
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: 70.04 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 26 LDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDI-TNMSVVKRTsflsrvfqdpkLGTAPRMTVA 104
Cdd:TIGR01257 1955 VDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISDVHQN-----------MGYCPQFDAI 2023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 105 ENLLlaekRGGHHHLVPRKLKG----EMKRFKEITAKmNNNLDHRLNTATGSLSGGQRQALSFLMATIKKPGILLLDEHT 180
Cdd:TIGR01257 2024 DDLL----TGREHLYLYARLRGvpaeEIEKVANWSIQ-SLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPT 2098
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 927264579 181 AALDPKTSQNLMDITDETIKEQNlTCLMITHHLEDALKYGNRLLVLHQG 229
Cdd:TIGR01257 2099 TGMDPQARRMLWNTIVSIIREGR-AVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
25-231 |
2.80e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 67.23 E-value: 2.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRT-SFLSRVFQDPKLGTapRMTV 103
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARArRGIGYLPQEASIFR--RLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 104 AENLLLAEKrgghhhlVPRKLKGEMK--RFKEITAKMnnNLDHRLNTATGSLSGGQRQALSFLMATIKKPGILLLDEHTA 181
Cdd:PRK10895 96 YDNLMAVLQ-------IRDDLSAEQRedRANELMEEF--HIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 927264579 182 ALDPKTSQNLMDITdETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:PRK10895 167 GVDPISVIDIKRII-EHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHL 215
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
27-185 |
3.24e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 69.00 E-value: 3.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 27 DHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQ--VIYKDKDITNMSVVKRTSFLSRVFQdpkLGTapRMTVA 104
Cdd:NF033858 283 DHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEawLFGQPVDAGDIATRRRVGYMSQAFS---LYG--ELTVR 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 105 ENLLLaekrggHHHL-------VPRKLKGEMKRFkeitakmnnNLDHRLNTATGSLSGGQRQALSFLMATIKKPGILLLD 177
Cdd:NF033858 358 QNLEL------HARLfhlpaaeIAARVAEMLERF---------DLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILD 422
|
....*...
gi 927264579 178 EHTAALDP 185
Cdd:NF033858 423 EPTSGVDP 430
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
36-250 |
3.30e-13 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 67.17 E-value: 3.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 36 GDFITILGSNGAGKSTLFNTIGGnLRPTSGQVIYKDKDITNMSVV---KRTSFLSRvfQDPklgTAPRMTVAENLLLaek 112
Cdd:COG4138 22 GELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNGRPLSDWSAAelaRHRAYLSQ--QQS---PPFAMPVFQYLAL--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 113 rGGHHHLVPRKLKGEMkrfKEITAKMnnNLDHRLNTATGSLSGGQRQALSfLMATIKK--PGI------LLLDEHTAALD 184
Cdd:COG4138 93 -HQPAGASSEAVEQLL---AQLAEAL--GLEDKLSRPLTQLSGGEWQRVR-LAAVLLQvwPTInpegqlLLLDEPMNSLD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 927264579 185 pKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKISydISGEDKQKLTkEELLT 250
Cdd:COG4138 166 -VAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLV--ASGETAEVMT-PENLS 227
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
6-229 |
3.31e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 68.68 E-value: 3.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 6 FQLKDVvkTVneDTPEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGnLRP-TSGQVIYKDKDitnmsvvkRTS 84
Cdd:COG4178 363 LALEDL--TL--RTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG-LWPyGSGRIARPAGA--------RVL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 85 FLSrvfQDPKL------------GTAPRMTVAEnLLLAEKRGGHHHLVPRkLKGEmkrfkeitakmnNNLDHRLntatgs 152
Cdd:COG4178 430 FLP---QRPYLplgtlreallypATAEAFSDAE-LREALEAVGLGHLAER-LDEE------------ADWDQVL------ 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 927264579 153 lSGGQRQALSFLMATIKKPGILLLDEHTAALDPKTSQNLMditdETIKEQ--NLTCLMITHHlEDALKYGNRLLVLHQG 229
Cdd:COG4178 487 -SLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALY----QLLREElpGTTVISVGHR-STLAAFHDRVLELTGD 559
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
25-217 |
4.25e-13 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 67.10 E-value: 4.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMS------VVKRTSFLsrvFQDPKLGTa 98
Cdd:PRK11831 22 IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSrsrlytVRKRMSML---FQSGALFT- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 99 pRMTVAENLLLAEKRggHHHLVPRKLKGE-MKRFKEITAKMNNNLdhrlntATGSLSGG--QRQALSFLMATikKPGILL 175
Cdd:PRK11831 98 -DMNVFDNVAYPLRE--HTQLPAPLLHSTvMMKLEAVGLRGAAKL------MPSELSGGmaRRAALARAIAL--EPDLIM 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 927264579 176 LDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDAL 217
Cdd:PRK11831 167 FDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVL 208
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
26-230 |
1.03e-12 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 67.12 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 26 LDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGnLRPT---SGQVIYkDKDITNMSVVKRTSFLSRVFQDPKLGTAPRMT 102
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHgsyEGEILF-DGEVCRFKDIRDSEALGIVIIHQELALIPYLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 103 VAENLLLaekrgGHhhlvPRKLKG------EMKRFKEITAKMNnnLDHRLNTATGSLSGGQRQ------ALSflmatiKK 170
Cdd:NF040905 95 IAENIFL-----GN----ERAKRGvidwneTNRRARELLAKVG--LDESPDTLVTDIGVGKQQlveiakALS------KD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 171 PGILLLDEHTAALDPKTSQNLMDITDEtIKEQNLTCLMITHHLEDALKYGNRLLVLHQGK 230
Cdd:NF040905 158 VKLLILDEPTAALNEEDSAALLDLLLE-LKAQGITSIIISHKLNEIRRVADSITVLRDGR 216
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
25-231 |
1.13e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 67.04 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTlfnTIGGNLR--PTSGQVIYKDKDITNMSVVKRTSFLSR---VFQDPKLGTAP 99
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKST---TGLALLRliNSQGEIWFDGQPLHNLNRRQLLPVRHRiqvVFQDPNSSLNP 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 100 RMTVAEnlLLAEKRGGHHhlvpRKLKGEMKRFKEITAKMNNNLD----HRLNTAtgsLSGGQRQALSFLMATIKKPGILL 175
Cdd:PRK15134 378 RLNVLQ--IIEEGLRVHQ----PTLSAAQREQQVIAVMEEVGLDpetrHRYPAE---FSGGQRQRIAIARALILKPSLII 448
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 927264579 176 LDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:PRK15134 449 LDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEV 504
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
26-255 |
1.50e-12 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 65.61 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 26 LDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQvIYKDKDITNMSVvkrtsflsrvfqdpKLGTAPRMTVAE 105
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGK-VDRNGEVSVIAI--------------SAGLSGQLTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 106 NLLLAEKRGGHHHLVPRKLKGEMKRFKEitakmnnnLDHRLNTATGSLSGGQRQALSFLMATIKKPGILLLDEHTAALDP 185
Cdd:PRK13546 105 NIEFKMLCMGFKRKEIKAMTPKIIEFSE--------LGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 186 KTSQNLMDITDEtIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKIS-----------YDISGEDKQKLTKEELLTFFND 254
Cdd:PRK13546 177 TFAQKCLDKIYE-FKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKdygelddvlpkYEAFLNDFKKKSKAEQKEFRNK 255
|
.
gi 927264579 255 I 255
Cdd:PRK13546 256 L 256
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
26-231 |
1.86e-12 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 66.58 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 26 LDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDI---------TNMSVVKRTSFLsrvFQDpklg 96
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLrdytlaslrNQVALVSQNVHL---FND---- 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 97 taprmTVAENLLLAEKRgghhhlvpRKLKGEMKRFKEITAKMN--NNLDHRLNTATG----SLSGGQRQALSFLMATIKK 170
Cdd:PRK11176 432 -----TIANNIAYARTE--------QYSREQIEEAARMAYAMDfiNKMDNGLDTVIGengvLLSGGQRQRIAIARALLRD 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 927264579 171 PGILLLDEHTAALDPKTSQNLMDITDETIKeqNLTCLMITHHLEdALKYGNRLLVLHQGKI 231
Cdd:PRK11176 499 SPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLS-TIEKADEILVVEDGEI 556
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-216 |
2.68e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 64.80 E-value: 2.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 2 TKTIFQLKDVVKTvnedtpEELNI-------LDHVDLDIHEGDFITILGSNGAGKSTL---FNTIGgNLRPT---SGQVI 68
Cdd:PRK14243 1 TSTLNGTETVLRT------ENLNVyygsflaVKNVWLDIPKNQITAFIGPSGCGKSTIlrcFNRLN-DLIPGfrvEGKVT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 69 YKDKDITNMSV--VKRTSFLSRVFQDPKlgTAPRmTVAENLLLAEKRGGHH----HLVPRKLKgemkrfkeiTAKMNNNL 142
Cdd:PRK14243 74 FHGKNLYAPDVdpVEVRRRIGMVFQKPN--PFPK-SIYDNIAYGARINGYKgdmdELVERSLR---------QAALWDEV 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 927264579 143 DHRLNTATGSLSGGQRQALSFLMATIKKPGILLLDEHTAALDPKTSQNLMDITDEtIKEQnLTCLMITHHLEDA 216
Cdd:PRK14243 142 KDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHE-LKEQ-YTIIIVTHNMQQA 213
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
18-187 |
2.90e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 66.13 E-value: 2.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 18 DTPeelnILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYkDKDITnmsvvkrtsfLSRVFQDPklgt 97
Cdd:PRK11147 15 DAP----LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIY-EQDLI----------VARLQQDP---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 98 aPRMT-------VAENLL-LAEKRGGHHHLVPRKLKGEMKRFKEITAKMNNNLDH--------RLN-----------TAT 150
Cdd:PRK11147 76 -PRNVegtvydfVAEGIEeQAEYLKRYHDISHLVETDPSEKNLNELAKLQEQLDHhnlwqlenRINevlaqlgldpdAAL 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 927264579 151 GSLSGG-QRQAlSFLMATIKKPGILLLDEHTAALDPKT 187
Cdd:PRK11147 155 SSLSGGwLRKA-ALGRALVSNPDVLLLDEPTNHLDIET 191
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-256 |
3.51e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 66.15 E-value: 3.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 20 PEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSFLSRVFQDPKLGTAp 99
Cdd:PLN03232 1246 PGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSG- 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 100 rmTVAENLllaeKRGGHHHLVPRKLKGEMKRFKEITAKMNNNLDHRLNTATGSLSGGQRQALSFLMATIKKPGILLLDEH 179
Cdd:PLN03232 1325 --TVRFNI----DPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEA 1398
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 927264579 180 TAALDPKTSQnlmdITDETIKEQNLTC--LMITHHLEDALKYgNRLLVLHQGKIsydISGEDKQKLTKEELLTFFNDIQ 256
Cdd:PLN03232 1399 TASVDVRTDS----LIQRTIREEFKSCtmLVIAHRLNTIIDC-DKILVLSSGQV---LEYDSPQELLSRDTSAFFRMVH 1469
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-231 |
4.99e-12 |
|
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: 65.09 E-value: 4.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 1 MTKTIFQLKDV-VKTVNEDtpEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTI----GGNLRPTSGQVIYKDKDIT 75
Cdd:COG4172 2 MSMPLLSVEDLsVAFGQGG--GTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSIlrllPDPAAHPSGSILFDGQDLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 76 NMSVVK----RTSFLSRVFQDPklGTA--PRMTV----AENLLLaekrgghhHlvpRKLKGemkrfKEITAKMNNNLDH- 144
Cdd:COG4172 80 GLSERElrriRGNRIAMIFQEP--MTSlnPLHTIgkqiAEVLRL--------H---RGLSG-----AAARARALELLERv 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 145 -------RLNTATGSLSGGQRQALSFLMATIKKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLedAL 217
Cdd:COG4172 142 gipdperRLDAYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDL--GV 219
|
250
....*....|....*.
gi 927264579 218 --KYGNRLLVLHQGKI 231
Cdd:COG4172 220 vrRFADRVAVMRQGEI 235
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
22-229 |
5.51e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.44 E-value: 5.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 22 ELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNL--RPTSGQVIYKDKDI-TNMSVV----KRTSF------LSR 88
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFgREASLIdaigRKGDFkdavelLNA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 89 VfqdpKLGTAPrmtvaenLLLAekrgghhhlvprklkgemkRFKEitakmnnnldhrlntatgsLSGGQRQALSFLMATI 168
Cdd:COG2401 122 V----GLSDAV-------LWLR-------------------RFKE-------------------LSTGQKFRFRLALLLA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 927264579 169 KKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHH--LEDALKyGNRLLVLHQG 229
Cdd:COG2401 153 ERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHydVIDDLQ-PDLLIFVGYG 214
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
22-234 |
6.06e-12 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 64.76 E-value: 6.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 22 ELNILDHVDLDIHEGDFITILGSNGAG--KSTLFNTIGGnlrPTSGQVIYKDKD-ITNMSVVKRTSFLSRVFqdpKLGTA 98
Cdd:NF000106 25 EVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRRPWRF*TwCANRRALRRTIG*HRPV---R*GRR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 99 PRMTVAENLllaekrgghhHLVPRKL----KGEMKRFKEITAKMNnnLDHRLNTATGSLSGGQRQALSFLMATIKKPGIL 174
Cdd:NF000106 99 ESFSGRENL----------YMIGR*LdlsrKDARARADELLERFS--LTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 175 LLDEHTAALDPKTSQNLMDITDETIKEqNLTCLMITHHLEDALKYGNRLLVLHQGKISYD 234
Cdd:NF000106 167 YLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIAD 225
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
25-231 |
6.27e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 63.87 E-value: 6.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDK--DITNMSVVKRTSFLSRVFQDPK---LGTAP 99
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQDPEqqiFYTDI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 100 RMTVA---ENLLLAEkrgghhhlvprklkgemkrfKEITAKMNNNL-----DHRLNTATGSLSGGQRQALSFLMATIKKP 171
Cdd:PRK13638 96 DSDIAfslRNLGVPE--------------------AEITRRVDEALtlvdaQHFRHQPIQCLSHGQKKRVAIAGALVLQA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 172 GILLLDEHTAALDPKTSQNLMDITDETIKEQNlTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:PRK13638 156 RYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGN-HVIISSHDIDLIYEISDAVYVLRQGQI 214
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
18-246 |
6.28e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 65.44 E-value: 6.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 18 DTPEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKD----KDI------TNMSVVKRTSFL- 86
Cdd:PTZ00265 393 DTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDInlkwwrSKIGVVSQDPLLf 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 87 -----------------------------SRVFQDPKLGTAPRMTVAENLLLAEKRGGHHHLVPRKLKGEMKRFKEITAK 137
Cdd:PTZ00265 473 snsiknnikyslyslkdlealsnyynedgNDSQENKNKRNSCRAKCAGDLNDMSNTTDSNELIEMRKNYQTIKDSEVVDV 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 138 MNNNLDH--------RLNTATGS----LSGGQRQALSFLMATIKKPGILLLDEHTAALDPKtSQNLMDITDETIK-EQNL 204
Cdd:PTZ00265 553 SKKVLIHdfvsalpdKYETLVGSnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNK-SEYLVQKTINNLKgNENR 631
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 927264579 205 TCLMITHHLEdALKYGNRLLVLHQ----GKISYDISGEDKQKLTKE 246
Cdd:PTZ00265 632 ITIIIAHRLS-TIRYANTIFVLSNrergSTVDVDIIGEDPTKDNKE 676
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
7-255 |
7.14e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 64.68 E-value: 7.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 7 QLKDVVKTVNEDTPEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRP---TSGQVIYKDKDITNMSVVKRT 83
Cdd:TIGR00955 22 QLVSRLRGCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKEMRAIS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 84 SFlsrVFQDPKLgtAPRMTVAENLLL-AEKRGGHHhlVPRKLKgeMKRFKEITAKMNnnLDHRLNTATG------SLSGG 156
Cdd:TIGR00955 102 AY---VQQDDLF--IPTLTVREHLMFqAHLRMPRR--VTKKEK--RERVDEVLQALG--LRKCANTRIGvpgrvkGLSGG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 157 QRQALSFLMATIKKPGILLLDEHTAALDPKTSQNLMditdETIKE--QNLTCLMITHHLEDALKYG--NRLLVLHQGKIS 232
Cdd:TIGR00955 171 ERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVV----QVLKGlaQKGKTIICTIHQPSSELFElfDKIILMAEGRVA 246
|
250 260
....*....|....*....|...
gi 927264579 233 YdiSGedkqklTKEELLTFFNDI 255
Cdd:TIGR00955 247 Y--LG------SPDQAVPFFSDL 261
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
28-239 |
8.29e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 64.69 E-value: 8.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 28 HVDLDIHEGDFITILGSNGAGKSTLFNTIGGnLRPT-SGQVIYKDKDITNMSVVKRtsflsrvfqdpklgtaprmtVAEN 106
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYG-LRPArGGRIMLNGKEINALSTAQR--------------------LARG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 107 LL-LAEKRGGH----------------HHLVPRKLKG--EMKRFKEITAKMNNNLDHrLNTATGSLSGGQRQALsfLMAT 167
Cdd:PRK15439 340 LVyLPEDRQSSglyldaplawnvcaltHNRRGFWIKParENAVLERYRRALNIKFNH-AEQAARTLSGGNQQKV--LIAK 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 927264579 168 I--KKPGILLLDEHTAALDPKTSQNLMDITdETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKISYDISGED 239
Cdd:PRK15439 417 CleASPQLLIVDEPTRGVDVSARNDIYQLI-RSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAA 489
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
28-230 |
8.84e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 64.49 E-value: 8.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 28 HVDLDIHEGDFITILGSNGAGKST-------LFNTIGGN-------LRPTSGQVI-YKDKDITNMSVVkRTSFLSRVFQD 92
Cdd:PRK10261 34 NLSFSLQRGETLAIVGESGSGKSVtalalmrLLEQAGGLvqcdkmlLRRRSRQVIeLSEQSAAQMRHV-RGADMAMIFQE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 93 PKLGTAPRMTV----AENLLLAEKRGGHHHLVPRKLKGEMKRFKEITAkMNNNLDHRLntatgslSGGQRQALSFLMATI 168
Cdd:PRK10261 113 PMTSLNPVFTVgeqiAESIRLHQGASREEAMVEAKRMLDQVRIPEAQT-ILSRYPHQL-------SGGMRQRVMIAMALS 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 927264579 169 KKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGK 230
Cdd:PRK10261 185 CRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGE 246
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
21-192 |
1.25e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 64.13 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 21 EELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTS--GQVIYKDKDITNmSVVKRTSFlsrVFQDPKLgtA 98
Cdd:PLN03211 79 QERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTK-QILKRTGF---VTQDDIL--Y 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 99 PRMTVAENLLLAEKRgghhhLVPRKLKGEMKRFKEITAKMNNNLDHRLNTATGS-----LSGGQRQALSFLMATIKKPGI 173
Cdd:PLN03211 153 PHLTVRETLVFCSLL-----RLPKSLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSL 227
|
170
....*....|....*....
gi 927264579 174 LLLDEHTAALDPKTSQNLM 192
Cdd:PLN03211 228 LILDEPTSGLDATAAYRLV 246
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
36-248 |
1.38e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 62.64 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 36 GDFITILGSNGAGKSTLFNTIGGnLRPTSGQVIYKDKDITNMSVVK---RTSFLSRvfQDPklgTAPRMTVAENLLLaek 112
Cdd:PRK03695 22 GEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQPLEAWSAAElarHRAYLSQ--QQT---PPFAMPVFQYLTL--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 113 rgghHHLVPRKLKGEMKRFKEITAKMnnNLDHRLNTATGSLSGGQ----RQALSFLMA--TIKKPG-ILLLDEHTAALDp 185
Cdd:PRK03695 93 ----HQPDKTRTEAVASALNEVAEAL--GLDDKLGRSVNQLSGGEwqrvRLAAVVLQVwpDINPAGqLLLLDEPMNSLD- 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 927264579 186 KTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKISydISGEDKQKLTKEEL 248
Cdd:PRK03695 166 VAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLL--ASGRRDEVLTPENL 226
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
21-230 |
1.93e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 63.57 E-value: 1.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 21 EELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIggnLR--PTSgQVIYKDKDI--TNMSVVK---------RTSFLS 87
Cdd:PRK15134 20 TVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSI---LRllPSP-PVVYPSGDIrfHGESLLHaseqtlrgvRGNKIA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 88 RVFQDPKLGTAPRMTVAENL--LLAEKRGghhhlvprkLKGEMKRfkeitAKMNNNLDH--------RLNTATGSLSGGQ 157
Cdd:PRK15134 96 MIFQEPMVSLNPLHTLEKQLyeVLSLHRG---------MRREAAR-----GEILNCLDRvgirqaakRLTDYPHQLSGGE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 927264579 158 RQALSFLMATIKKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGK 230
Cdd:PRK15134 162 RQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
25-231 |
3.66e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 62.81 E-value: 3.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNM---------SVVKRTSFLsrvFQDpkl 95
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLqldswrsrlAVVSQTPFL---FSD--- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 96 gtaprmTVAENLLLAEkrgghhhlvPRKLKGEMkrfkEITAKMNNNLDHRLNTATG----------SLSGGQRQALSFLM 165
Cdd:PRK10789 404 ------TVANNIALGR---------PDATQQEI----EHVARLASVHDDILRLPQGydtevgergvMLSGGQKQRISIAR 464
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 927264579 166 ATIKKPGILLLDEHTAALDPKTSQNLMditdetikeQNLT------CLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:PRK10789 465 ALLLNAEILILDDALSAVDGRTEHQIL---------HNLRqwgegrTVIISAHRLSALTEASEILVMQHGHI 527
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
16-231 |
3.96e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 62.07 E-value: 3.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 16 NEDTPeeLNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNL----RPTSGQVIYKDKDITNMSVVKRTSF----LS 87
Cdd:PRK11022 15 DESAP--FRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQDLQRISEKERRNLvgaeVA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 88 RVFQDPKLGTAPRMTVAENLLLAEK--RGGHHhlvprklKGEMKRFKEITAKMN-NNLDHRLNTATGSLSGGQRQALSFL 164
Cdd:PRK11022 93 MIFQDPMTSLNPCYTVGFQIMEAIKvhQGGNK-------KTRRQRAIDLLNQVGiPDPASRLDVYPHQLSGGMSQRVMIA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 927264579 165 MATIKKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:PRK11022 166 MAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQV 232
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
25-228 |
4.13e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 61.28 E-value: 4.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGqviykdkditnmsVVKRTSFLsrvfqdpKLGTAP-RMTV 103
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG-------------VIKRNGKL-------RIGYVPqKLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 104 AENLLLAEKRGghhhlvpRKLKGEMKRFKEITAKMNNNLDHRLNTATGSLSGGQRQALSFLMATIKKPGILLLDEHTAAL 183
Cdd:PRK09544 79 DTTLPLTVNRF-------LRLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGV 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 927264579 184 DPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQ 228
Cdd:PRK09544 152 DVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
25-212 |
5.05e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 60.35 E-value: 5.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNmsvvKRTSFLSRV-FQDPKLGTAPRMTV 103
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK----DLCTYQKQLcFVGHRSGINPYLTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 104 AENLLLAEkrggHHHLVPRKLKGEMKRFKeitakmnnnLDHRLNTATGSLSGGQRQALSFLMATIKKPGILLLDEHTAAL 183
Cdd:PRK13540 92 RENCLYDI----HFSPGAVGITELCRLFS---------LEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVAL 158
|
170 180
....*....|....*....|....*....
gi 927264579 184 DPKTSQNLMDITDETiKEQNLTCLMITHH 212
Cdd:PRK13540 159 DELSLLTIITKIQEH-RAKGGAVLLTSHQ 186
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
7-230 |
6.35e-11 |
|
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: 58.61 E-value: 6.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 7 QLKDVVKTVNEDTpeelnILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKditnmsvvKRTSFL 86
Cdd:cd03221 2 ELENLSKTYGGKL-----LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST--------VKIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 87 SRvfqdpklgtaprmtvaenlllaekrgghhhlvprklkgemkrfkeitakmnnnldhrlntatgsLSGGQRQALSFLMA 166
Cdd:cd03221 69 EQ----------------------------------------------------------------LSGGEKMRLALAKL 84
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 927264579 167 TIKKPGILLLDEHTAALDPKTSQNLmditDETIKEQNLTCLMITH--HLEDALkyGNRLLVLHQGK 230
Cdd:cd03221 85 LLENPNLLLLDEPTNHLDLESIEAL----EEALKEYPGTVILVSHdrYFLDQV--ATKIIELEDGK 144
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-211 |
7.42e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 61.67 E-value: 7.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 1 MTKTIFQLKDVVKTVNEDTPeelnILDHVDLDIHEGDFITILGSNGAGKSTLfntiggnLRPTSGQviykDKDIT----- 75
Cdd:PRK11819 2 MAQYIYTMNRVSKVVPPKKQ----ILKDISLSFFPGAKIGVLGLNGAGKSTL-------LRIMAGV----DKEFEgearp 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 76 --NMSVvkrtSFLSrvfQDPKLGtaPRMTVAENLL--LAEKrgghhhlvprklKGEMKRFKEITAKMNN----------- 140
Cdd:PRK11819 67 apGIKV----GYLP---QEPQLD--PEKTVRENVEegVAEV------------KAALDRFNEIYAAYAEpdadfdalaae 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 141 --------------NLDHRLNTA------------TGSLSGGQRQ--ALSFLMatIKKPGILLLDEHTAALDPKTSQNLm 192
Cdd:PRK11819 126 qgelqeiidaadawDLDSQLEIAmdalrcppwdakVTKLSGGERRrvALCRLL--LEKPDMLLLDEPTNHLDAESVAWL- 202
|
250 260
....*....|....*....|....
gi 927264579 193 ditdetikEQNL-----TCLMITH 211
Cdd:PRK11819 203 --------EQFLhdypgTVVAVTH 218
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-211 |
8.65e-11 |
|
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: 61.49 E-value: 8.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 5 IFQLKDVVKTVnedtPEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGnlrptsgqviyKDKDITNMSVVKRTS 84
Cdd:TIGR03719 4 IYTMNRVSKVV----PPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-----------VDKDFNGEARPQPGI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 85 FLSRVFQDPKLGtaPRMTVAENLLLAekrgghhhlvPRKLKGEMKRFKEITAKMNN------------------------ 140
Cdd:TIGR03719 69 KVGYLPQEPQLD--PTKTVRENVEEG----------VAEIKDALDRFNEISAKYAEpdadfdklaaeqaelqeiidaada 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 141 -NLDHRLNTA------------TGSLSGGQRQ--ALSFLMatIKKPGILLLDEHTAALDPKTSQNLmditdetikEQNL- 204
Cdd:TIGR03719 137 wDLDSQLEIAmdalrcppwdadVTKLSGGERRrvALCRLL--LSKPDMLLLDEPTNHLDAESVAWL---------ERHLq 205
|
250
....*....|.
gi 927264579 205 ----TCLMITH 211
Cdd:TIGR03719 206 eypgTVVAVTH 216
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
13-233 |
1.45e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 61.28 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 13 KTVNEDTPEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNL----RPTSGQVIYKDKDITNMSVVKRTSFLSR 88
Cdd:TIGR00956 64 KLKKFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTdgfhIGVEGVITYDGITPEEIKKHYRGDVVYN 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 89 VFQDPKLgtaPRMTVAENLLLAEkrgghhhlvprKLKGEMKRFKEITAKMNNN-----------LDHRLNTATGS----- 152
Cdd:TIGR00956 144 AETDVHF---PHLTVGETLDFAA-----------RCKTPQNRPDGVSREEYAKhiadvymatygLSHTRNTKVGNdfvrg 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 153 LSGGQRQALSFLMATIKKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLM-ITHHLEDALKYGNRLLVLHQGKI 231
Cdd:TIGR00956 210 VSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVaIYQCSQDAYELFDKVIVLYEGYQ 289
|
..
gi 927264579 232 SY 233
Cdd:TIGR00956 290 IY 291
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
27-184 |
1.78e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 58.66 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 27 DHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMsvvkRTSFLSRVFQdpkLGTAP----RMT 102
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQ----RDEYHQDLLY---LGHQPgiktELT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 103 VAENLLLAEkrgghhhlvprKLKGEMKRFK--EITAKMnnNLDHRLNTATGSLSGGQ--RQALSFLMATikKPGILLLDE 178
Cdd:PRK13538 91 ALENLRFYQ-----------RLHGPGDDEAlwEALAQV--GLAGFEDVPVRQLSAGQqrRVALARLWLT--RAPLWILDE 155
|
....*.
gi 927264579 179 HTAALD 184
Cdd:PRK13538 156 PFTAID 161
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
25-231 |
3.30e-10 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 59.83 E-value: 3.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIggnLR---PTSGQVIYKDKDITNmsvVKRTSfLSR----VFQDPKLGT 97
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLL---FRfydVTSGRILIDGQDIRD---VTQAS-LRAaigiVPQDTVLFN 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 98 AprmTVAENL-----------LLAEKRGGH-HHLVprklkgemkrfkeitakmnNNLDHRLNTATGS----LSGGQRQAL 161
Cdd:COG5265 446 D---TIAYNIaygrpdaseeeVEAAARAAQiHDFI-------------------ESLPDGYDTRVGErglkLSGGEKQRV 503
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 927264579 162 SFLMATIKKPGILLLDEHTAALDPKTSQNLMDitdeTIKE--QNLTCLMITHHLE---DAlkygNRLLVLHQGKI 231
Cdd:COG5265 504 AIARTLLKNPPILIFDEATSALDSRTERAIQA----ALREvaRGRTTLVIAHRLStivDA----DEILVLEAGRI 570
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
19-226 |
3.65e-10 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 57.16 E-value: 3.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 19 TPEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGnLRP-TSGQVIykdkditnMSVVKRTSFLSrvfQDPKLgt 97
Cdd:cd03223 10 TPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG-LWPwGSGRIG--------MPEGEDLLFLP---QRPYL-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 98 aPRMTVAENLLLAEKRgghhhlvprklkgemkrfkeitakmnnnldhrlntatgSLSGGQRQALSFLMATIKKPGILLLD 177
Cdd:cd03223 76 -PLGTLREQLIYPWDD--------------------------------------VLSGGEQQRLAFARLLLHKPKFVFLD 116
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 927264579 178 EHTAALDPKTSQNLMDItdetIKEQNLTCLMITHHlEDALKYGNRLLVL 226
Cdd:cd03223 117 EATSALDEESEDRLYQL----LKELGITVISVGHR-PSLWKFHDRVLDL 160
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
44-250 |
9.70e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.89 E-value: 9.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 44 SNGAGKSTLFNTiggnlrptSGQVIYKDKDITNMSVVKRTSFLSRVFQDPKLGTaprMTVAENLLLAeKRGGHHHLVPRK 123
Cdd:PTZ00265 1264 GGSGEDSTVFKN--------SGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFN---MSIYENIKFG-KEDATREDVKRA 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 124 LKgeMKRFKEITAKMNNNLDHRLNTATGSLSGGQRQALSFLMATIKKPGILLLDEHTAALDpKTSQNLMDITDETIKEQ- 202
Cdd:PTZ00265 1332 CK--FAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLD-SNSEKLIEKTIVDIKDKa 1408
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 927264579 203 NLTCLMITHHLEdALKYGNRLLVLHQGkisyDISGEDKQ-KLTKEELLT 250
Cdd:PTZ00265 1409 DKTIITIAHRIA-SIKRSDKIVVFNNP----DRTGSFVQaHGTHEELLS 1452
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
26-230 |
1.03e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 57.89 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 26 LDHVDLDIHEGDFITILGSNGAGKSTLFNTIGG----NLRPTSGQVIYKDKDITNMSVVKRTSF----LSRVFQDPKLGT 97
Cdd:PRK15093 23 VDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGvtkdNWRVTADRMRFDDIDLLRLSPRERRKLvghnVSMIFQEPQSCL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 98 APRMTVAENLLLAEKRGGHHHLVPRKLKGEMKRFKEITAKMNNNlDHR--LNTATGSLSGGQRQALSFLMATIKKPGILL 175
Cdd:PRK15093 103 DPSERVGRQLMQNIPGWTYKGRWWQRFGWRKRRAIELLHRVGIK-DHKdaMRSFPYELTEGECQKVMIAIALANQPRLLI 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 927264579 176 LDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGK 230
Cdd:PRK15093 182 ADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQ 236
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
22-231 |
1.65e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.94 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 22 ELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSF---LSRVFQDPKLGTA 98
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALrrdIQFIFQDPYASLD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 99 PRMTVAENLLLAEKrgghhhlVPRKLKGE--MKRFKEITAKMNNNLDHRLNTATgSLSGGQRQALSFLMATIKKPGILLL 176
Cdd:PRK10261 416 PRQTVGDSIMEPLR-------VHGLLPGKaaAARVAWLLERVGLLPEHAWRYPH-EFSGGQRQRICIARALALNPKVIIA 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 927264579 177 DEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:PRK10261 488 DEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQI 542
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
36-213 |
1.83e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 56.81 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 36 GDFITILGSNGAGKSTLFNTIGGNLRPTSGQViykdkDITNMSVVK--RTSFLSRVFQDPKLGTAPRMTVAENLLLAekR 113
Cdd:PRK15056 33 GSIAALVGVNGSGKSTLFKALMGFVRLASGKI-----SILGQPTRQalQKNLVAYVPQSEEVDWSFPVLVEDVVMMG--R 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 114 GGHHHLVPRKLKGEMKRFKEITAKMnNNLDHRlNTATGSLSGGQRQALsFLMATIKKPG-ILLLDEHTAALDPKTSQNLM 192
Cdd:PRK15056 106 YGHMGWLRRAKKRDRQIVTAALARV-DMVEFR-HRQIGELSGGQKKRV-FLARAIAQQGqVILLDEPFTGVDVKTEARII 182
|
170 180
....*....|....*....|.
gi 927264579 193 DITDEtIKEQNLTCLMITHHL 213
Cdd:PRK15056 183 SLLRE-LRDEGKTMLVSTHNL 202
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
26-249 |
4.70e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.17 E-value: 4.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 26 LDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMS----VVKRTSFLSrvfQDPK-----LG 96
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSpqdgLANGIVYIS---EDRKrdglvLG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 97 taprMTVAENLLLA-----EKRGGH-HHLVPRKLKGEMKRFKEI-TAKMNNnldhrlntATGSLSGGQRQALSFLMATIK 169
Cdd:PRK10762 345 ----MSVKENMSLTalryfSRAGGSlKHADEQQAVSDFIRLFNIkTPSMEQ--------AIGLLSGGNQQKVAIARGLMT 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 170 KPGILLLDEHTAALDPKTSQNLMDITDEtIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKISYDISGEDKqklTKEELL 249
Cdd:PRK10762 413 RPKVLILDEPTRGVDVGAKKEIYQLINQ-FKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTREQA---TQEKLM 488
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-230 |
6.31e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.78 E-value: 6.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 2 TKTIFQLKDVVKTVnedtpEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITnmsvvk 81
Cdd:PRK10762 1 MQALLQLKGIDKAF-----PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVT------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 82 rtsflsrvFQDPK-------------LGTAPRMTVAENLLLAekrgghhhlvpRKLKGEMKR--FKEITAKMNN-----N 141
Cdd:PRK10762 70 --------FNGPKssqeagigiihqeLNLIPQLTIAENIFLG-----------REFVNRFGRidWKKMYAEADKllarlN 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 142 LDHRLNTATGSLSGGQRQ------ALSFlmatikKPGILLLDEHTAALDPKTSQNLMDITDEtIKEQNLTCLMITHHLED 215
Cdd:PRK10762 131 LRFSSDKLVGELSIGEQQmveiakVLSF------ESKVIIMDEPTDALTDTETESLFRVIRE-LKSQGRGIVYISHRLKE 203
|
250
....*....|....*
gi 927264579 216 ALKYGNRLLVLHQGK 230
Cdd:PRK10762 204 IFEICDDVTVFRDGQ 218
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
26-251 |
6.35e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 56.05 E-value: 6.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 26 LDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQViykdkDITNMSVVKRTSflsrvfqdpkLGTAPRMTVAE 105
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----DIKGSAALIAIS----------SGLNGQLTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 106 NLllaekrgghhhlvprKLKGEM-----KRFKEITAKMNNNLD--HRLNTATGSLSGGQRQALSFLMATIKKPGILLLDE 178
Cdd:PRK13545 105 NI---------------ELKGLMmgltkEKIKEIIPEIIEFADigKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 179 HTAALDPKTSQNLMDITDEtIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI-----------SYD--------ISGED 239
Cdd:PRK13545 170 ALSVGDQTFTKKCLDKMNE-FKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVkeygdikevvdHYDeflkkynqMSVEE 248
|
250
....*....|..
gi 927264579 240 KQKLTKEELLTF 251
Cdd:PRK13545 249 RKDFREEQISQF 260
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
25-231 |
9.49e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 54.83 E-value: 9.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNL---RPTSGQVIYKDKDITNMSVVK----RTSFLSRVFqdPKLGT 97
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtggGAPRGARVTGDVTLNGEPLAAidapRLARLRAVL--PQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 98 -APRMTVAENLLLAE----KRGGHHHLVPRKLKGEMKRFKEITAkmnnnLDHRLNTatgSLSGGQRQALSFLMA------ 166
Cdd:PRK13547 94 pAFAFSAREIVLLGRyphaRRAGALTHRDGEIAWQALALAGATA-----LVGRDVT---TLSGGELARVQFARVlaqlwp 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 927264579 167 ---TIKKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKI 231
Cdd:PRK13547 166 phdAAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAI 233
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
23-214 |
1.11e-08 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 53.87 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 23 LNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSF----LSRVFQDPKLGTA 98
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLLNA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 99 prmTVAENLLLAEKRgghhhlvprklkgEMKRFKEIT--AKMNNNLD---HRLNTATG----SLSGGQRQALSFLMATIK 169
Cdd:cd03290 94 ---TVEENITFGSPF-------------NKQRYKAVTdaCSLQPDIDllpFGDQTEIGergiNLSGGQRQRICVARALYQ 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 927264579 170 KPGILLLDEHTAALDPKTSQNLM-DITDETIKEQNLTCLMITHHLE 214
Cdd:cd03290 158 NTNIVFLDDPFSALDIHLSDHLMqEGILKFLQDDKRTLVLVTHKLQ 203
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-231 |
1.12e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 54.26 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 1 MTKTIFQLKDVVKTVNEDTpeelnILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNlrP----TSGQVIYKDKDITN 76
Cdd:CHL00131 3 KNKPILEIKNLHASVNENE-----ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH--PaykiLEGDILFKGESILD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 77 MSVVKRTS---FLSrvFQDPKlgTAPRMTVAENLLLA----EKRGGHHHLVPrklkgeMKRFKEITAK-----MNNNLDH 144
Cdd:CHL00131 76 LEPEERAHlgiFLA--FQYPI--EIPGVSNADFLRLAynskRKFQGLPELDP------LEFLEIINEKlklvgMDPSFLS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 145 RlNTATGsLSGGQRQALSFLMATIKKPGILLLDEHTAALDPKTsqnLMDITDE--TIKEQNLTCLMITHHledalkygNR 222
Cdd:CHL00131 146 R-NVNEG-FSGGEKKRNEILQMALLDSELAILDETDSGLDIDA---LKIIAEGinKLMTSENSIILITHY--------QR 212
|
250
....*....|....*...
gi 927264579 223 LL---------VLHQGKI 231
Cdd:CHL00131 213 LLdyikpdyvhVMQNGKI 230
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
22-184 |
3.06e-08 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 52.50 E-value: 3.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 22 ELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSFLSRVFQDpklGTAPRM 101
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAP---GIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 102 TVAENLLLAEKRGGHHHLvprklkgemkrfKEITAKMN-NNLDHRlntATGSLSGGQRQALSFLMATIKKPGILLLDEHT 180
Cdd:cd03231 89 SVLENLRFWHADHSDEQV------------EEALARVGlNGFEDR---PVAQLSAGQQRRVALARLLLSGRPLWILDEPT 153
|
....
gi 927264579 181 AALD 184
Cdd:cd03231 154 TALD 157
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
25-231 |
4.16e-08 |
|
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: 52.60 E-value: 4.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSFLSRVFQDPKLGTAprmTVA 104
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSG---SIR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 105 ENLLlAEKRGGHHHLVPRKlkgEMKRFKEITAKMNNNLDHRLNTATGSLSGGQRQALSFLMATIKKPGILLLDEHTAALD 184
Cdd:cd03288 113 FNLD-PECKCTDDRLWEAL---EIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASID 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 927264579 185 PKTSQNLMDITDETIKEQnlTCLMITHHLEDALKyGNRLLVLHQGKI 231
Cdd:cd03288 189 MATENILQKVVMTAFADR--TVVTIAHRVSTILD-ADLVLVLSRGIL 232
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-225 |
4.37e-08 |
|
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: 52.41 E-value: 4.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 32 DIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGqviykDKDITNMSVVKRTSFLSRVFQdpklgtaprMTVAEnlLLAE 111
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEG-----DIEIELDTVSYKPQYIKADYE---------GTVRD--LLSS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 112 KRGGHhhlvprklkGEMKRFK-EITA--KMNNNLDHRLNTatgsLSGGQRQALSfLMATIKKPG-ILLLDEHTAALDpkT 187
Cdd:cd03237 85 ITKDF---------YTHPYFKtEIAKplQIEQILDREVPE----LSGGELQRVA-IAACLSKDAdIYLLDEPSAYLD--V 148
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 927264579 188 SQNLM--DITDETIKEQNLTCLMITHHLEDALKYGNRLLV 225
Cdd:cd03237 149 EQRLMasKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
6-216 |
6.88e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.71 E-value: 6.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 6 FQLKDVVKTVNeDTPeelnILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGN-------------LRPTSGQVIYKDK 72
Cdd:PRK10938 261 IVLNNGVVSYN-DRP----ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDhpqgysndltlfgRRRGSGETIWDIK 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 73 D-ITNMSvvkrtsflSRVFQDPKLGTAPRmtvaeNLLLAekrG-----GHHHLVP---RKLKGEMKRFKEITAKMNNNLD 143
Cdd:PRK10938 336 KhIGYVS--------SSLHLDYRVSTSVR-----NVILS---GffdsiGIYQAVSdrqQKLAQQWLDILGIDKRTADAPF 399
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 927264579 144 HrlntatgSLSGGQRQALSFLMATIKKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTCLMITHHLEDA 216
Cdd:PRK10938 400 H-------SLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
33-184 |
7.05e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.89 E-value: 7.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 33 IHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQViykDKDItnmsvvkrtsflsRVFQDPK-LGTAPRMTVAENLLLAE 111
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV---DPEL-------------KISYKPQyIKPDYDGTVEDLLRSIT 425
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 927264579 112 KRGGHHHLVPrklkgemkrfkEITAKMNNN--LDHRLNTatgsLSGGQRQALSFLMATIKKPGILLLDEHTAALD 184
Cdd:PRK13409 426 DDLGSSYYKS-----------EIIKPLQLErlLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
25-229 |
7.70e-08 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 52.17 E-value: 7.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDkditnmsvvkRTSFLSRVfqdpklgtAPRM--T 102
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG----------RISFSSQF--------SWIMpgT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 103 VAENLLLAEKRGGHHHLVPRK---LKGEMKRFKEitakmnnnldhRLNTATG----SLSGGQRQALSFLMATIKKPGILL 175
Cdd:cd03291 114 IKENIIFGVSYDEYRYKSVVKacqLEEDITKFPE-----------KDNTVLGeggiTLSGGQRARISLARAVYKDADLYL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 927264579 176 LDEHTAALDPKTSQNLMDITDETIKeQNLTCLMITHHLEDaLKYGNRLLVLHQG 229
Cdd:cd03291 183 LDSPFGYLDVFTEKEIFESCVCKLM-ANKTRILVTSKMEH-LKKADKILILHEG 234
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
26-230 |
8.54e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.42 E-value: 8.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 26 LDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDItNMSVVKRT--SFLSRVFQDpkLGTAPRMTV 103
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI-DFKSSKEAleNGISMVHQE--LNLVLQRSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 104 AENLLLAEkrgghhhlVPRKL----KGEMKR-FKEITAKMNNNLDHRLNTATGSLSggQRQALSFLMATIKKPGILLLDE 178
Cdd:PRK10982 91 MDNMWLGR--------YPTKGmfvdQDKMYRdTKAIFDELDIDIDPRAKVATLSVS--QMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 927264579 179 HTAALDPKTSQNLMDITDEtIKEQNLTCLMITHHLEDALKYGNRLLVLHQGK 230
Cdd:PRK10982 161 PTSSLTEKEVNHLFTIIRK-LKERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
5-229 |
9.43e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.80 E-value: 9.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 5 IFQLKDVVKTVNEDTpEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGnlRPTSGqVIYKDKDITNMSvvKRTS 84
Cdd:TIGR00956 759 IFHWRNLTYEVKIKK-EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTG-VITGGDRLVNGR--PLDS 832
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 85 FLSRVF-----QDPKLGTAprmTVAENLLL-AEKRGGHHhlVPRKlkgEMKRFKEITAK---MNNNLDHRLNTATGSLSG 155
Cdd:TIGR00956 833 SFQRSIgyvqqQDLHLPTS---TVRESLRFsAYLRQPKS--VSKS---EKMEYVEEVIKlleMESYADAVVGVPGEGLNV 904
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 927264579 156 GQRQALSFLMATIKKPGILL-LDEHTAALDPKTSQNLMDITDETIKE-QNLTClmiTHHLEDALKYG--NRLLVLHQG 229
Cdd:TIGR00956 905 EQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHgQAILC---TIHQPSAILFEefDRLLLLQKG 979
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
18-248 |
1.78e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 51.66 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 18 DTPEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQviykdkditnmSVVKRTSflsrVFQDPKLGT 97
Cdd:PLN03130 625 DSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDA-----------SVVIRGT----VAYVPQVSW 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 98 APRMTVAENLLLaekrgGHHHLVPRklkgeMKRFKEITAkmnnnLDHRLNTATG-----------SLSGGQRQALSFLMA 166
Cdd:PLN03130 690 IFNATVRDNILF-----GSPFDPER-----YERAIDVTA-----LQHDLDLLPGgdlteigergvNISGGQKQRVSMARA 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 167 TIKKPGILLLDEHTAALDPKTSQNLMD--ITDETikeQNLTCLMITHHLEdALKYGNRLLVLHQGKIsydisgedKQKLT 244
Cdd:PLN03130 755 VYSNSDVYIFDDPLSALDAHVGRQVFDkcIKDEL---RGKTRVLVTNQLH-FLSQVDRIILVHEGMI--------KEEGT 822
|
....
gi 927264579 245 KEEL 248
Cdd:PLN03130 823 YEEL 826
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
25-226 |
2.24e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 50.23 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNmsvVKRTSFLSRVFQDPklGTAPRMTVA 104
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR---GDRSRFMAYLGHLP--GLKADLSTL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 105 ENLLLAEKRGGHHhlvPRKLKGEMKRFKEITakmnnnlDHRlNTATGSLSGGQRQALSFLMATIKKPGILLLDEHTAALD 184
Cdd:PRK13543 101 ENLHFLCGLHGRR---AKQMPGSALAIVGLA-------GYE-DTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 927264579 185 PKTSQNLMDITDETIKEQNLTcLMITHHLEDALKYGNRLLVL 226
Cdd:PRK13543 170 LEGITLVNRMISAHLRGGGAA-LVTTHGAYAAPPVRTRMLTL 210
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
25-229 |
3.82e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 50.68 E-value: 3.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDkditnmsvvkRTSFlsrvfqDPKLGTAPRMTVA 104
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG----------RISF------SPQTSWIMPGTIK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 105 ENLLLAEKRGGHHHLVPRKlkgeMKRFKEITAKMNNNLDHRLNTATGSLSGGQRQALSFLMATIKKPGILLLDEHTAALD 184
Cdd:TIGR01271 505 DNIIFGLSYDEYRYTSVIK----ACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 927264579 185 PKTSQnlmDITDETIKE--QNLTCLMITHHLEDaLKYGNRLLVLHQG 229
Cdd:TIGR01271 581 VVTEK---EIFESCLCKlmSNKTRILVTSKLEH-LKKADKILLLHEG 623
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
29-232 |
6.43e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.86 E-value: 6.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 29 VDLDIHegdfITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKditnmsvvKRTSFLSRVFQDPklgtaprMTVAENLL 108
Cdd:PLN03073 532 IDLDSR----IAMVGPNGIGKSTILKLISGELQPSSGTVFRSAK--------VRMAVFSQHHVDG-------LDLSSNPL 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 109 LAEKRGghHHLVP-RKLKGEMKRFKeitakMNNNLDHRlntATGSLSGGQRQALSFLMATIKKPGILLLDEHTAALDpkt 187
Cdd:PLN03073 593 LYMMRC--FPGVPeQKLRAHLGSFG-----VTGNLALQ---PMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD--- 659
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 927264579 188 sqnlMDITDETIkeQNLT-----CLMITHhlEDALKYG--NRLLVLHQGKIS 232
Cdd:PLN03073 660 ----LDAVEALI--QGLVlfqggVLMVSH--DEHLISGsvDELWVVSEGKVT 703
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
22-233 |
1.25e-06 |
|
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: 47.64 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 22 ELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPT---SGQVIYKDKDITNMSVVKRTSFLSRVFQDPKLgta 98
Cdd:cd03233 19 KIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHF--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 99 PRMTVAENLllaekrgghhhlvprklkgemkrfkEITAKMNNNLDHRlntatgSLSGGQRQALSFLMATIKKPGILLLDE 178
Cdd:cd03233 96 PTLTVRETL-------------------------DFALRCKGNEFVR------GISGGERKRVSIAEALVSRASVLCWDN 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 927264579 179 HTAALDPKTSQNLMDITDETIKEQNLTCLMITHHL-EDALKYGNRLLVLHQGKISY 233
Cdd:cd03233 145 STRGLDSSTALEILKCIRTMADVLKTTTFVSLYQAsDEIYDLFDKVLVLYEGRQIY 200
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
26-249 |
1.76e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 48.67 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 26 LDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDK---DITNMSVVKRTSfLSRVFQDPKL-GTAPRM 101
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKFEGNVFINGkpvDIRNPAQAIRAG-IAMVPEDRKRhGIVPIL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 102 TVAENLLLA--EKRGGHHHLVPRK----LKGEMKRFKEITAKMnnnldhrlNTATGSLSGGQRQALSFLMATIKKPGILL 175
Cdd:TIGR02633 355 GVGKNITLSvlKSFCFKMRIDAAAelqiIGSAIQRLKVKTASP--------FLPIGRLSGGNQQKAVLAKMLLTNPRVLI 426
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 927264579 176 LDEHTAALDPKTSQNLMDITDEtIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKISYDISGEDkqkLTKEELL 249
Cdd:TIGR02633 427 LDEPTRGVDVGAKYEIYKLINQ-LAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGDFVNHA---LTQEQVL 496
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
25-246 |
2.50e-06 |
|
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: 47.54 E-value: 2.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIggnLRptsgqVIYKDKDITNMSVVKRTSFLSRVFQdpKLGTAPRM--- 101
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAF---LR-----LLNTEGDIQIDGVSWNSVPLQKWRK--AFGVIPQKvfi 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 102 ---TVAENLllaEKRGGHHHLVPRKLKGEMKrFKEITAKMNNNLDHRLNTATGSLSGGQRQALSFLMATIKKPGILLLDE 178
Cdd:cd03289 89 fsgTFRKNL---DPYGKWSDEEIWKVAEEVG-LKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 179 HTAALDPKTSQnlmdITDETIKEQNLTCLMI-THHLEDALKYGNRLLVLHQGKI-SYDisgeDKQKLTKE 246
Cdd:cd03289 165 PSAHLDPITYQ----VIRKTLKQAFADCTVIlSEHRIEAMLECQRFLVIEENKVrQYD----SIQKLLNE 226
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
25-193 |
3.05e-06 |
|
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: 47.62 E-value: 3.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDkditnmsVVKrtsfLSRVFQDPKlGTAPRMTVA 104
Cdd:TIGR03719 337 LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGE-------TVK----LAYVDQSRD-ALDPNKTVW 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 105 EnlllaEKRGGHHHLVPRKLkgEMK------RF--------KEItakmnnnldhrlntatGSLSGGQRQALsFLMATIKK 170
Cdd:TIGR03719 405 E-----EISGGLDIIKLGKR--EIPsrayvgRFnfkgsdqqKKV----------------GQLSGGERNRV-HLAKTLKS 460
|
170 180
....*....|....*....|....
gi 927264579 171 PG-ILLLDEHTAALDPKTSQNLMD 193
Cdd:TIGR03719 461 GGnVLLLDEPTNDLDVETLRALEE 484
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
19-224 |
3.30e-06 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 47.82 E-value: 3.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 19 TPEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGnLRPTSGQVIYKDKDiTNMSVVKRTSFLSR---------- 88
Cdd:TIGR00954 461 TPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGE-LWPVYGGRLTKPAK-GKLFYVPQRPYMTLgtlrdqiiyp 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 89 ----VFQDPKLGTAPRMTVAENLLLaekrgghHHLVPRKLKGE-MKRFKEItakmnnnldhrlntatgsLSGGQRQALSF 163
Cdd:TIGR00954 539 dsseDMKRRGLSDKDLEQILDNVQL-------THILEREGGWSaVQDWMDV------------------LSGGEKQRIAM 593
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 927264579 164 LMATIKKPGILLLDEHTAALDPKTSQNLMditdETIKEQNLTCLMITHHlEDALKYGNRLL 224
Cdd:TIGR00954 594 ARLFYHKPQFAILDECTSAVSVDVEGYMY----RLCREFGITLFSVSHR-KSLWKYHEYLL 649
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2-249 |
3.52e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 47.47 E-value: 3.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 2 TKTIFQLKDVvktvnedTPEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMS--- 78
Cdd:PRK09700 262 HETVFEVRNV-------TSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpld 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 79 -VVKRTSFLSRVFQDPklGTAPRMTVAENLLLAE--KRGGHHHLVPRKLKGEMKRFKEITAKMNNNLDHRLNTATGSLSG 155
Cdd:PRK09700 335 aVKKGMAYITESRRDN--GFFPNFSIAQNMAISRslKDGGYKGAMGLFHEVDEQRTAENQRELLALKCHSVNQNITELSG 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 156 GQRQALSFLMATIKKPGILLLDEHTAALDPKTSQNLMDITdETIKEQNLTCLMITHHLEDALKYGNRLLVLHQGKISYDI 235
Cdd:PRK09700 413 GNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVM-RQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQIL 491
|
250
....*....|....
gi 927264579 236 SGEDkqKLTKEELL 249
Cdd:PRK09700 492 TNRD--DMSEEEIM 503
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-184 |
4.88e-06 |
|
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: 47.09 E-value: 4.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 32 DIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQViykDKDItnmsvvkrtsflsRVFQDPK-LGTAPRMTVAENLlla 110
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV---DEDL-------------KISYKPQyISPDYDGTVEEFL--- 422
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 927264579 111 ekrgghhhlvpRKLKGEM---KRFK-EITAKMnnNLDHRLNTATGSLSGGQRQALSFLMATIKKPGILLLDEHTAALD 184
Cdd:COG1245 423 -----------RSANTDDfgsSYYKtEIIKPL--GLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
21-93 |
8.98e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 45.55 E-value: 8.98e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 927264579 21 EELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGG--NLRPTSGQVIYKDKDITNMSVVKRTS---FLSrvFQDP 93
Cdd:PRK09580 12 EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKGKDLLELSPEDRAGegiFMA--FQYP 87
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
41-218 |
1.09e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 44.86 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 41 ILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSvvkrTSFLSRVFQDpkLGTAPRMTVAENLLLAEKRGGHHHLV 120
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA----KPYCTYIGHN--LGLKLEMTVFENLKFWSEIYNSAETL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 121 PrklkGEMKRFKeitakmnnnLDHRLNTATGSLSGGQRQ--ALSFLMATIKKpgILLLDEHTAALDPKTSQNLMDITdeT 198
Cdd:PRK13541 105 Y----AAIHYFK---------LHDLLDEKCYSLSSGMQKivAIARLIACQSD--LWLLDEVETNLSKENRDLLNNLI--V 167
|
170 180
....*....|....*....|
gi 927264579 199 IKEQNLTCLMITHHLEDALK 218
Cdd:PRK13541 168 MKANSGGIVLLSSHLESSIK 187
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
36-215 |
1.15e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 44.29 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 36 GDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRtsflsrvfqdpklgtaprmtvaenlllaekrgg 115
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQ--------------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 116 hhhlvprklkgemkrfkeitakmnnNLDHRLNTATGSLSGGQRQALSFLMATIKKPGILLLDEHTAALDPKTSQNLMDIT 195
Cdd:smart00382 49 -------------------------LLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLE 103
|
170 180
....*....|....*....|....*
gi 927264579 196 D-----ETIKEQNLTCLMITHHLED 215
Cdd:smart00382 104 ElrlllLLKSEKNLTVILTTNDEKD 128
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
25-250 |
1.35e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 45.69 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLR-PTSGQVIYKDKDITNMSVVKRTSF-LSRVFQDPKL-GTAPRM 101
Cdd:PRK13549 277 RVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQQAIAQgIAMVPEDRKRdGIVPVM 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 102 TVAENLLLAEKRGGHHHLVPRKLKgEMKRFKEITAKMnnnldhRLNTAT-----GSLSGGQRQALSFLMATIKKPGILLL 176
Cdd:PRK13549 357 GVGKNITLAALDRFTGGSRIDDAA-ELKTILESIQRL------KVKTASpelaiARLSGGNQQKAVLAKCLLLNPKILIL 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 927264579 177 DEHTAALDPKTSQNLMDITDETIKeQNLTCLMITHHLEDALKYGNRLLVLHQGKISYDISGEDkqkLTKEELLT 250
Cdd:PRK13549 430 DEPTRGIDVGAKYEIYKLINQLVQ-QGVAIIVISSELPEVLGLSDRVLVMHEGKLKGDLINHN---LTQEQVME 499
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
25-193 |
2.04e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.16 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQvIYKDKDItnmsvvkrtsflsrvfqdpKLGTAPRMTVa 104
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGE-IGLAKGI-------------------KLGYFAQHQL- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 105 eNLLLAEKRGGHH--HLVPRKLKGEMKRFkeiTAKMNNNLDhRLNTATGSLSGGQRQALSFLMATIKKPGILLLDEHTAA 182
Cdd:PRK10636 386 -EFLRADESPLQHlaRLAPQELEQKLRDY---LGGFGFQGD-KVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNH 460
|
170
....*....|.
gi 927264579 183 LDPKTSQNLMD 193
Cdd:PRK10636 461 LDLDMRQALTE 471
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
25-246 |
2.06e-05 |
|
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: 45.67 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGgNLRPTSGQVIYKDKDITNMSVVK-RTSF---------LSRVFQDpK 94
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQIDGVSWNSVTLQTwRKAFgvipqkvfiFSGTFRK-N 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 95 LGTAPRMTVAENLLLAEKRGghhhlvprkLKGEMKRFKeitakmnNNLDHRLNTATGSLSGGQRQALSFLMATIKKPGIL 174
Cdd:TIGR01271 1312 LDPYEQWSDEEIWKVAEEVG---------LKSVIEQFP-------DKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKIL 1375
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 927264579 175 LLDEHTAALDPKTSQnlmdITDETIKEQNLTCLMI-THHLEDALKYGNRLLVLHQGKI-SYDisgeDKQKLTKE 246
Cdd:TIGR01271 1376 LLDEPSAHLDPVTLQ----IIRKTLKQSFSNCTVIlSEHRVEALLECQQFLVIEGSSVkQYD----SIQKLLNE 1441
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
21-67 |
3.74e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.50 E-value: 3.74e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 927264579 21 EELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQV 67
Cdd:PRK15064 330 DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
28-219 |
3.83e-05 |
|
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: 43.36 E-value: 3.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 28 HVDLDIHEGDFIT-ILGSNGAGKSTLFNTIG----GNLRPTSGQVIYKDKDITNMSVVkrtsflsrvfqdpklgtaprmt 102
Cdd:cd03240 13 HERSEIEFFSPLTlIVGQNGAGKTTIIEALKyaltGELPPNSKGGAHDPKLIREGEVR---------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 103 vAENLLLAEKRGGHHHLVPRKL----------KGEMKRFKeitakmnnnLDHRlntatGSLSGGQRQALSFL------MA 166
Cdd:cd03240 71 -AQVKLAFENANGKKYTITRSLailenvifchQGESNWPL---------LDMR-----GRCSGGEKVLASLIirlalaET 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 927264579 167 TIKKPGILLLDEHTAALDP-KTSQNLMDITDETIKEQNLTCLMITHH--LEDALKY 219
Cdd:cd03240 136 FGSNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHDeeLVDAADH 191
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-231 |
4.02e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 44.58 E-value: 4.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 18 DTPEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSgqviykdkditNMSVVKRTSflsrVFQDPKLGT 97
Cdd:PLN03232 625 DSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAE-----------TSSVVIRGS----VAYVPQVSW 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 98 APRMTVAENLLLAEKRGGHHHLvprklkgemkRFKEITAkmnnnLDHRLNTATG-----------SLSGGQRQALSFLMA 166
Cdd:PLN03232 690 IFNATVRENILFGSDFESERYW----------RAIDVTA-----LQHDLDLLPGrdlteigergvNISGGQKQRVSMARA 754
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 927264579 167 TIKKPGILLLDEHTAALDPKTSQNLMditDETIKE--QNLTCLMITHHLEdALKYGNRLLVLHQGKI 231
Cdd:PLN03232 755 VYSNSDIYIFDDPLSALDAHVAHQVF---DSCMKDelKGKTRVLVTNQLH-FLPLMDRIILVSEGMI 817
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
32-211 |
6.16e-05 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 43.03 E-value: 6.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 32 DIHEGDFITILGSNGAGKSTLFNTIGGNLrptSGQVIYKDK---DITNMSVVKRTSFLSRVFQdpklgtaprmtvaenll 108
Cdd:cd03279 24 GLDNNGLFLICGPTGAGKSTILDAITYAL---YGKTPRYGRqenLRSVFAPGEDTAEVSFTFQ----------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 109 laekRGGHHHLVPRKLKGEMKRFKEITAKMNNNLDHRLNTATGSLSGGQ--------RQALSFLMATIKKPGI--LLLDE 178
Cdd:cd03279 84 ----LGGKKYRVERSRGLDYDQFTRIVLLPQGEFDRFLARPVSTLSGGEtflaslslALALSEVLQNRGGARLeaLFIDE 159
|
170 180 190
....*....|....*....|....*....|...
gi 927264579 179 HTAALDPKTSQNLMDITDEtIKEQNLTCLMITH 211
Cdd:cd03279 160 GFGTLDPEALEAVATALEL-IRTENRMVGVISH 191
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-211 |
6.46e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 43.79 E-value: 6.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 3 KTIFQLKDVVKTVnedtpEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSG--------QVIYKDKdi 74
Cdd:PRK11147 317 KIVFEMENVNYQI-----DGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGrihcgtklEVAYFDQ-- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 75 tnmsvvkrtsflSRVFQDPKlgtaprMTVAENllLAEKR-----GGhhhlVPRKLKGEMKRFkeitakmnnnLDH--RLN 147
Cdd:PRK11147 390 ------------HRAELDPE------KTVMDN--LAEGKqevmvNG----RPRHVLGYLQDF----------LFHpkRAM 435
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 927264579 148 TATGSLSGGQRQALsfLMATI--KKPGILLLDEHTAALDPKTsqnlMDITDETIKEQNLTCLMITH 211
Cdd:PRK11147 436 TPVKALSGGERNRL--LLARLflKPSNLLILDEPTNDLDVET----LELLEELLDSYQGTVLLVSH 495
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
145-224 |
2.37e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 40.77 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 145 RLNTATGSLSGGQRQAL---SFLMATIKkPGILLLDEHTAALDPKTSQNLMDITDETIKEQNlTCLMITHHlEDALKYGN 221
Cdd:cd03238 80 TLGQKLSTLSGGELQRVklaSELFSEPP-GTLFILDEPSTGLHQQDINQLLEVIKGLIDLGN-TVILIEHN-LDVLSSAD 156
|
...
gi 927264579 222 RLL 224
Cdd:cd03238 157 WII 159
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
25-185 |
3.60e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 41.69 E-value: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 25 ILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSFLSRVFQDPKLGTAprmTVA 104
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDG---TVR 1401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 105 ENL--LL----AEkrgghhhlVPRKLkgEMKRFKEITAKMNNNLDHRLNTATGSLSGGQRQALSFLMATIKK-PGILLLD 177
Cdd:PTZ00243 1402 QNVdpFLeassAE--------VWAAL--ELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKgSGFILMD 1471
|
....*...
gi 927264579 178 EHTAALDP 185
Cdd:PTZ00243 1472 EATANIDP 1479
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
143-197 |
4.05e-04 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 38.37 E-value: 4.05e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 927264579 143 DHRLNTATGSLSGGQRQ---------ALSFLM----ATIKKPGILLLDEHTAALDPKTSQNLMDITDE 197
Cdd:pfam13558 23 EVETYRRSGGLSGGEKQllaylplaaALAAQYgsaeGRPPAPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
41-67 |
4.11e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 41.26 E-value: 4.11e-04
10 20
....*....|....*....|....*..
gi 927264579 41 ILGSNGAGKSTLFNTIGGNLRPTSGQV 67
Cdd:PRK11819 355 IIGPNGAGKSTLFKMITGQEQPDSGTI 381
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
30-230 |
5.99e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.77 E-value: 5.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 30 DLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVKRTSFLSRVFQD-------PKLGTAPRmT 102
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDEWQRnntdmlsPGEDDTGR-T 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 103 VAENLLLAEKRG----------GHHHLVPRklkgemkRFKEitakmnnnldhrlntatgsLSGGQ-RQALsFLMATIKKP 171
Cdd:PRK10938 102 TAEIIQDEVKDParceqlaqqfGITALLDR-------RFKY-------------------LSTGEtRKTL-LCQALMSEP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 927264579 172 GILLLDEHTAALDPKTSQNLMDITdETIKEQNLTCLMITHHLEDALKYGNRLLVL------HQGK 230
Cdd:PRK10938 155 DLLILDEPFDGLDVASRQQLAELL-ASLHQSGITLVLVLNRFDEIPDFVQFAGVLadctlaETGE 218
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
152-214 |
6.78e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.66 E-value: 6.78e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 927264579 152 SLSGGQRQALSFLMAT------IKKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNL--TCLMITHHLE 214
Cdd:PRK01156 801 SLSGGEKTAVAFALRVavaqflNNDKSLLIMDEPTAFLDEDRRTNLKDIIEYSLKDSSDipQVIMISHHRE 871
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
3-214 |
1.46e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 39.30 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 3 KTIFQLKDVVKTVNEDTPEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNtIGGNLRPTSGQVIYKDKDITNMSVVKR 82
Cdd:pfam13304 96 KRLLLREDSEEREPKFPPEAEELRLGLDVEERIELSLSELSDLISGLLLLSI-ISPLSFLLLLDEGLLLEDWAVLDLAAD 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 83 TSFLSRVFQDPKLGTAPRMTVAENLLLAEKRGGHHHLVPRKLKGEMKRFKEItakmnnnlDHRLNTATGSLSGGQRQALS 162
Cdd:pfam13304 175 LALFPDLKELLQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLILLEN--------GGGGELPAFELSDGTKRLLA 246
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 927264579 163 FLMA---TIKKPGILLLDEHTAALDPKTSQNLMDITDETiKEQNLTCLMITHHLE 214
Cdd:pfam13304 247 LLAAllsALPKGGLLLIDEPESGLHPKLLRRLLELLKEL-SRNGAQLILTTHSPL 300
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
153-214 |
2.65e-03 |
|
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: 37.34 E-value: 2.65e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 927264579 153 LSGGQRQ--ALSFLM--ATIKKPGILLLDEHTAALDPKTSQNLMDITDETIKEQNLTcLMITHHLE 214
Cdd:cd03227 78 LSGGEKElsALALILalASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQV-IVITHLPE 142
|
|
| ABC_MutS-like |
cd03283 |
ATP-binding cassette domain of MutS-like homolog; The MutS protein initiates DNA mismatch ... |
30-60 |
2.79e-03 |
|
ATP-binding cassette domain of MutS-like homolog; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
Pssm-ID: 213250 [Multi-domain] Cd Length: 199 Bit Score: 37.66 E-value: 2.79e-03
10 20 30
....*....|....*....|....*....|.
gi 927264579 30 DLDIHEGDFITILGSNGAGKSTLFNTIGGNL 60
Cdd:cd03283 19 DIDMEKKNGILITGSNMSGKSTFLRTIGVNV 49
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
43-67 |
3.18e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 38.33 E-value: 3.18e-03
10 20
....*....|....*....|....*
gi 927264579 43 GSNGAGKSTLFNTIGGNLRPTSGQV 67
Cdd:PRK15064 34 GANGCGKSTFMKILGGDLEPSAGNV 58
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
153-191 |
5.50e-03 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213240 [Multi-domain] Cd Length: 251 Bit Score: 37.28 E-value: 5.50e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 927264579 153 LSGGQRQ--ALSFLMATIK-KPG-ILLLDEHTAALDPKTSQNL 191
Cdd:cd03273 167 LSGGQRSlvALSLILALLLfKPApMYILDEVDAALDLSHTQNI 209
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
9-249 |
6.63e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 37.40 E-value: 6.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 9 KDVVKTVNEDTPEELNILDHVDLDIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQVIYKDKDITNMSVVK--RTSFL 86
Cdd:PRK10982 247 GEVILEVRNLTSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEaiNHGFA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 87 SRVFQDPKLGTAPRMTVAENLLLA---EKRGGHHHLVPRKLKGEMKRFkeITAKMNNNLDHRlnTATGSLSGGQRQALSF 163
Cdd:PRK10982 327 LVTEERRSTGIYAYLDIGFNSLISnirNYKNKVGLLDNSRMKSDTQWV--IDSMRVKTPGHR--TQIGSLSGGNQQKVII 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927264579 164 LMATIKKPGILLLDEHTAALDPKTSQNLMDITDETIKEqNLTCLMITHHLEDALKYGNRLLVLHQGKISYDIsgeDKQKL 243
Cdd:PRK10982 403 GRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLVAGIV---DTKTT 478
|
....*.
gi 927264579 244 TKEELL 249
Cdd:PRK10982 479 TQNEIL 484
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
32-67 |
7.04e-03 |
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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: 36.40 E-value: 7.04e-03
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gi 927264579 32 DIHEGDFITILGSNGAGKSTLFNTIGGNLRPTSGQV 67
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDND 56
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