|
Name |
Accession |
Description |
Interval |
E-value |
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-226 |
7.70e-72 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 217.99 E-value: 7.70e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 3 ELVIEAKQLTREFIRREKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQLS 82
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 83 ELRNRTMGICTQSQSLLASLNALDNAILPAtLYSKASSETAFTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARALV 162
Cdd:COG1136 82 RLRRRHIGFVFQFFNLLPELTALENVALPL-LLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 307615102 163 NHPQVFIADEPTGDLDAQSTELVMRLLAGLP-EAGTAVVFATHDPQALETARTVYEINAGVLSRQ 226
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNrELGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-223 |
3.42e-71 |
|
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: 216.20 E-value: 3.42e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 6 IEAKQLTREFIRREKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQLSELR 85
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 86 NRTMGICTQSQSLLASLNALDNAILPATLYSKASSETAfTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNHP 165
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERR-ERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 307615102 166 QVFIADEPTGDLDAQSTELVMRLLAGL-PEAGTAVVFATHDPQALETARTVYEINAGVL 223
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-223 |
1.43e-55 |
|
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: 176.86 E-value: 1.43e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 1 MSELVIEAKQLTREFIRREKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQ 80
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 81 LSELRNRTMGICTQSQSLLASLNALDNAILPATLyskASSETAFTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARA 160
Cdd:COG4181 84 RARLRARHVGFVFQSFQLLPTLTALENVMLPLEL---AGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 307615102 161 LVNHPQVFIADEPTGDLDAQSTELVMRLLAGLP-EAGTAVVFATHDPQALETARTVYEINAGVL 223
Cdd:COG4181 161 FATEPAILFADEPTGNLDAATGEQIIDLLFELNrERGTTLVLVTHDPALAARCDRVLRLRAGRL 224
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
24-225 |
4.48e-55 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 175.24 E-value: 4.48e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 24 AVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQLSELRnRTMGICTQSQSLLASLN 103
Cdd:COG2884 17 ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLR-RRIGVVFQDFRLLPDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 104 ALDNAILPaTLYSKASSETAFTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTE 183
Cdd:COG2884 96 VYENVALP-LRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSW 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 307615102 184 LVMRLLAGLPEAGTAVVFATHDPQALET--ARTVyEINAGVLSR 225
Cdd:COG2884 175 EIMELLEEINRRGTTVLIATHDLELVDRmpKRVL-ELEDGRLVR 217
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-204 |
1.19e-45 |
|
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: 151.58 E-value: 1.19e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 5 VIEAKQLTREFIRREKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQLSEL 84
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 85 RnRTMGICTQSQSLLASLNALDNAILPATLYSKASSETAfTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNH 164
Cdd:cd03258 81 R-RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIE-ERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANN 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 307615102 165 PQVFIADEPTGDLDAQSTELVMRLLAGL-PEAGTAVVFATH 204
Cdd:cd03258 159 PKVLLCDEATSALDPETTQSILALLRDInRELGLTIVLITH 199
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
6-213 |
1.36e-45 |
|
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: 151.02 E-value: 1.36e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 6 IEAKQLTREFirrekPFN--AVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQLSE 83
Cdd:cd03292 1 IEFINVTKTY-----PNGtaALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 84 LRnRTMGICTQSQSLLASLNALDNAILPATLYSKASSETAfTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARALVN 163
Cdd:cd03292 76 LR-RKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIR-KRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVN 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 307615102 164 HPQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATHDPQALETAR 213
Cdd:cd03292 154 SPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTR 203
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
5-213 |
1.95e-45 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 150.48 E-value: 1.95e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 5 VIEAKQLTREFIRrekPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQLSEL 84
Cdd:TIGR02673 1 MIEFHNVSKAYPG---GVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 85 RnRTMGICTQSQSLLASLNALDNAILPATLySKASSETAFTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNH 164
Cdd:TIGR02673 78 R-RRIGVVFQDFRLLPDRTVYENVALPLEV-RGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 307615102 165 PQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATHDPQALETAR 213
Cdd:TIGR02673 156 PPLLLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVA 204
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-221 |
2.01e-44 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 157.19 E-value: 2.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 1 MSELvIEAKQLTREFIRREKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQ 80
Cdd:PRK10535 1 MTAL-LELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 81 LSELRNRTMGICTQSQSLLASLNALDNAILPAtLYSKASSETAFTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARA 160
Cdd:PRK10535 80 LAQLRREHFGFIFQRYHLLSHLTAAQNVEVPA-VYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 307615102 161 LVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATHDPQALETARTVYEINAG 221
Cdd:PRK10535 159 LMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDG 219
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
27-226 |
4.11e-41 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 139.95 E-value: 4.11e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 27 NVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQLSELRNRTMGICTQSQSLLASLNALD 106
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQFHHLLPDFTALE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 107 NAILPATLYSKASSEtAFTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELVM 186
Cdd:PRK11629 107 NVAMPLLIGKKKPAE-INSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIF 185
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 307615102 187 RLLAGLPEA-GTAVVFATHDPQAletartvyeinAGVLSRQ 226
Cdd:PRK11629 186 QLLGELNRLqGTAFLVVTHDLQL-----------AKRMSRQ 215
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-205 |
4.46e-40 |
|
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: 136.87 E-value: 4.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 5 VIEAKQLTREFIRREKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQLSEL 84
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 85 RNRtMGICtqSQSLLASLNAL----DNAILPATLYSKASSETAFTRA-LELFEALEI-KHLTEAYPNELSGGEMRRVAIA 158
Cdd:cd03257 81 RKE-IQMV--FQDPMSSLNPRmtigEQIAEPLRIHGKLSKKEARKEAvLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 307615102 159 RALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPEA-GTAVVFATHD 205
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHD 205
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-205 |
1.17e-39 |
|
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: 135.68 E-value: 1.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 6 IEAKQLTREFIRREKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRqlselr 85
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 86 nrtMGICTQSQSLLASLNALDNAILPATLYSKASSETAfTRALELFEALEIKHLTEAYPNELSGGeMR-RVAIARALVNH 164
Cdd:cd03293 75 ---RGYVFQQDALLPWLTVLDNVALGLELQGVPKAEAR-ERAEELLELVGLSGFENAYPHQLSGG-MRqRVALARALAVD 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 307615102 165 PQVFIADEPTGDLDAQSTELVMRLLAGL-PEAGTAVVFATHD 205
Cdd:cd03293 150 PDVLLLDEPFSALDALTREQLQEELLDIwRETGKTVLLVTHD 191
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-205 |
1.25e-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: 136.76 E-value: 1.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 1 MSELVIEAKQLTREFIRREKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRq 80
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 81 lselrnrtMGICTQSQSLLASLNALDNAILPATLySKASSETAFTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARA 160
Cdd:COG1116 82 --------RGVVFQEPALLPWLTVLDNVALGLEL-RGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 307615102 161 LVNHPQVFIADEPTGDLDAQSTELVMRLLAGL-PEAGTAVVFATHD 205
Cdd:COG1116 153 LANDPEVLLMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHD 198
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-205 |
2.72e-39 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 137.90 E-value: 2.72e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 6 IEAKQLTREFIRREKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQLSELR 85
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 86 nRTMGICTQSQSLLASLNALDNAILPATL--YSKASSEtafTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARALVN 163
Cdd:COG1135 82 -RKIGMIFQHFNLLSSRTVAENVALPLEIagVPKAEIR---KRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALAN 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 307615102 164 HPQVFIADEPTGDLDAQSTELVMRLLAGL-PEAGTAVVFATHD 205
Cdd:COG1135 158 NPKVLLCDEATSALDPETTRSILDLLKDInRELGLTIVLITHE 200
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-213 |
7.68e-39 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 140.04 E-value: 7.68e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 1 MSELVIEAKQLTREF-IRREKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDR 79
Cdd:COG1123 256 AAEPLLEVRNLSKRYpVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 80 QLSELRnRTMGICTQ--SQSLLASLNALDNAILPATLYSKASSETAFTRALELFEA--LEIKHLtEAYPNELSGGEMRRV 155
Cdd:COG1123 336 SLRELR-RRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERvgLPPDLA-DRYPHELSGGQRQRV 413
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 307615102 156 AIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGL-PEAGTAVVFATHDpqaLETAR 213
Cdd:COG1123 414 AIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLqRELGLTYLFISHD---LAVVR 469
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-221 |
4.90e-38 |
|
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: 131.69 E-value: 4.90e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 6 IEAKQLTreFIRREKPfNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAElgdRQLSELR 85
Cdd:COG1122 1 IELENLS--FSYPGGT-PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITK---KNLRELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 86 nRTMGICTQsqsllaslNAlDNAILPATLY---------SKASSETAFTRALELFEALEIKHLTEAYPNELSGGEMRRVA 156
Cdd:COG1122 75 -RKVGLVFQ--------NP-DDQLFAPTVEedvafgpenLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 307615102 157 IARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATHDPQ-ALETARTVYEINAG 221
Cdd:COG1122 145 IAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDlVAELADRVIVLDDG 210
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-215 |
1.22e-37 |
|
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: 131.26 E-value: 1.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 1 MSELVIEAKQLTREFIRREkpfnAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQ 80
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRV----VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 81 LSELRNRtMGICTQSQSLLASLNALDNAILPATLYSKASSETAFTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARA 160
Cdd:COG1127 77 LYELRRR-IGMLFQGGALFDSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 307615102 161 LVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPEA-GTAVVFATHDpqaLETARTV 215
Cdd:COG1127 156 LALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHD---LDSAFAI 208
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-204 |
3.84e-37 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 132.62 E-value: 3.84e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 5 VIEAKQLTREFIRREKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQLSEL 84
Cdd:PRK11153 1 MIELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 85 RnRTMGICTQSQSLLASLNALDNAILPATL--YSKASSEtafTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARALV 162
Cdd:PRK11153 81 R-RQIGMIFQHFNLLSSRTVFDNVALPLELagTPKAEIK---ARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 307615102 163 NHPQVFIADEPTGDLDAQSTELVMRLLAGL-PEAGTAVVFATH 204
Cdd:PRK11153 157 SNPKVLLCDEATSALDPATTRSILELLKDInRELGLTIVLITH 199
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
26-215 |
4.58e-37 |
|
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: 129.54 E-value: 4.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 26 ENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQLSELRNRtMGICTQSQSLLASLNAL 105
Cdd:cd03261 17 KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRR-MGMLFQSGALFDSLTVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 106 DNAILPATLYSKASSETAFTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELV 185
Cdd:cd03261 96 ENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVI 175
|
170 180 190
....*....|....*....|....*....|.
gi 307615102 186 MRLLAGLPEA-GTAVVFATHDpqaLETARTV 215
Cdd:cd03261 176 DDLIRSLKKElGLTSIMVTHD---LDTAFAI 203
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-205 |
7.75e-36 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 126.33 E-value: 7.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 6 IEAKQLTREFirreKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAelgdRQLSELR 85
Cdd:COG1131 1 IEVRGLTKRY----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA----RDPAEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 86 NRtMGICTQSQSLLASLNALDNAILPATLYsKASSETAFTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNHP 165
Cdd:COG1131 73 RR-IGYVPQEPALYPDLTVRENLRFFARLY-GLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDP 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 307615102 166 QVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATHD 205
Cdd:COG1131 151 ELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHY 190
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-205 |
9.56e-36 |
|
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: 128.25 E-value: 9.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 5 VIEAKQLTREFIRREKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKP---TSGEVRVAGQNLAELGDRQL 81
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 82 SELRNRTMGICTQSQslLASLNAL----DNAILPATLYSKASSETAFTRALELFEALEI----KHLtEAYPNELSGGEMR 153
Cdd:COG0444 81 RKIRGREIQMIFQDP--MTSLNPVmtvgDQIAEPLRIHGGLSKAEARERAIELLERVGLpdpeRRL-DRYPHELSGGMRQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 307615102 154 RVAIARALVNHPQVFIADEPTGDLD----AQstelVMRLLAGL-PEAGTAVVFATHD 205
Cdd:COG0444 158 RVMIARALALEPKLLIADEPTTALDvtiqAQ----ILNLLKDLqRELGLAILFITHD 210
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
26-218 |
1.22e-35 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 125.04 E-value: 1.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 26 ENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQLSELRNRTMGICTQSQSLLASLNAL 105
Cdd:TIGR03608 15 DDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRREKLGYLFQNFALIENETVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 106 DNAILPaTLYSKASSETAFTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELV 185
Cdd:TIGR03608 95 ENLDLG-LKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLDPKNRDEV 173
|
170 180 190
....*....|....*....|....*....|...
gi 307615102 186 MRLLAGLPEAGTAVVFATHDPQALETARTVYEI 218
Cdd:TIGR03608 174 LDLLLELNDEGKTIIIVTHDPEVAKQADRVIEL 206
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-207 |
3.68e-35 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 124.51 E-value: 3.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 2 SELVIEAKQLTREFIRREKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQL 81
Cdd:PRK10584 3 AENIVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 82 SELRNRTMGICTQSQSLLASLNALDNAILPATLYSKASSETAfTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARAL 161
Cdd:PRK10584 83 AKLRAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSR-NGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAF 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 307615102 162 VNHPQVFIADEPTGDLDAQSTELVMRLLAGLP-EAGTAVVFATHDPQ 207
Cdd:PRK10584 162 NGRPDVLFADEPTGNLDRQTGDKIADLLFSLNrEHGTTLILVTHDLQ 208
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-223 |
9.53e-35 |
|
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: 129.25 E-value: 9.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 5 VIEAKQLTREFIRREKPfnAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPT---SGEVRVAGQNLAELGDRQL 81
Cdd:COG1123 4 LLEVRDLSVRYPGGDVP--AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 82 SELrnrtmgICTQSQSLLASLNAL--DNAILPATLYSKASSETAFTRALELFEALEIKHLTEAYPNELSGGEMRRVAIAR 159
Cdd:COG1123 82 GRR------IGMVFQDPMTQLNPVtvGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 307615102 160 ALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLP-EAGTAVVFATHDP-QALETARTVYEINAGVL 223
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQrERGTTVLLITHDLgVVAEIADRVVVMDDGRI 221
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
5-213 |
2.04e-34 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 122.86 E-value: 2.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 5 VIEAKQLTREFIRREKpfnAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQLSEL 84
Cdd:COG3638 2 MLELRNLSKRYPGGTP---ALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 85 RnRTMGICTQSQSLLASLNALDNAI---LPAT--------LYSKASSEtaftRALELFEALEIKHLTEAYPNELSGGEMR 153
Cdd:COG3638 79 R-RRIGMIFQQFNLVPRLSVLTNVLagrLGRTstwrsllgLFPPEDRE----RALEALERVGLADKAYQRADQLSGGQQQ 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 307615102 154 RVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGL-PEAGTAVVFATHDpqaLETAR 213
Cdd:COG3638 154 RVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIaREDGITVVVNLHQ---VDLAR 211
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-221 |
9.99e-34 |
|
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: 120.26 E-value: 9.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 7 EAKQLTreFIRREKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQLSelrn 86
Cdd:cd03225 1 ELKNLS--FSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELR---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 87 RTMGICTQsqsllaslNAlDNAILPATLYSkassETAF-------------TRALELFEALEIKHLTEAYPNELSGGEMR 153
Cdd:cd03225 75 RKVGLVFQ--------NP-DDQFFGPTVEE----EVAFglenlglpeeeieERVEEALELVGLEGLRDRSPFTLSGGQKQ 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 307615102 154 RVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATHDPQ-ALETARTVYEINAG 221
Cdd:cd03225 142 RVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDlLLELADRVIVLEDG 210
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-205 |
1.92e-33 |
|
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: 119.56 E-value: 1.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 6 IEAKQLTREFirreKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLaELGDRQLSELR 85
Cdd:cd03262 1 IEIKNLHKSF----GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL-TDDKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 86 NRtMGICTQSQSLLASLNALDNAILPATLYSKASSETAFTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNHP 165
Cdd:cd03262 76 QK-VGMVFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 307615102 166 QVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATHD 205
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHE 194
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
6-205 |
4.50e-33 |
|
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: 119.33 E-value: 4.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 6 IEAKQLTRefiRREKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELgdrQLSELR 85
Cdd:cd03295 1 IEFENVTK---RYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQ---DPVELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 86 nRTMGICTQSQSLLASLNALDN-AILPATLysKASSETAFTRALELFE--ALEIKHLTEAYPNELSGGEMRRVAIARALV 162
Cdd:cd03295 75 -RKIGYVIQQIGLFPHMTVEENiALVPKLL--KWPKEKIRERADELLAlvGLDPAEFADRYPHELSGGQQQRVGVARALA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 307615102 163 NHPQVFIADEPTGDLDAQSTELVMRLLAGLPEA-GTAVVFATHD 205
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHD 195
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-221 |
1.81e-32 |
|
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: 116.85 E-value: 1.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 6 IEAKQLTREFirreKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQlselr 85
Cdd:cd03259 1 LELKGLSKTY----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 86 nRTMGICTQSQSLLASLNALDNAILPATLySKASSETAFTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNHP 165
Cdd:cd03259 72 -RNIGMVFQDYALFPHLTVAENIAFGLKL-RGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 307615102 166 QVFIADEPTGDLDAQSTELVMRLLAGL-PEAGTAVVFATHDPQ-ALETARTVYEINAG 221
Cdd:cd03259 150 SLLLLDEPLSALDAKLREELREELKELqRELGITTIYVTHDQEeALALADRIAVMNEG 207
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-221 |
5.50e-32 |
|
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: 115.99 E-value: 5.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 1 MSELvIEAKQLTREFI---RREKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQ----NL 73
Cdd:COG4778 1 MTTL-LEVENLSKTFTlhlQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 74 AELGDRQLSELRNRTMGICTQSQSLLASLNALDNAILPAtLYSKASSETAFTRALELFEALEIK-HLTEAYPNELSGGEM 152
Cdd:COG4778 80 AQASPREILALRRRTIGYVSQFLRVIPRVSALDVVAEPL-LERGVDREEARARARELLARLNLPeRLWDLPPATFSGGEQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 153 RRVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATHDPQALET-ARTVYEINAG 221
Cdd:COG4778 159 QRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAvADRVVDVTPF 228
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-210 |
1.18e-30 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 113.03 E-value: 1.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 5 VIEAKQLTREFirreKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAelgdRQLSEL 84
Cdd:COG4555 1 MIEVENLSKKY----GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVR----KEPREA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 85 RNRtMGICTQSQSLLASLNALDNAILPATLYSKASSETAFtRALELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNH 164
Cdd:COG4555 73 RRQ-IGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKK-RIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHD 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 307615102 165 PQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATHDPQALE 210
Cdd:COG4555 151 PKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVE 196
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-205 |
1.26e-30 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 112.78 E-value: 1.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 5 VIEAKQLTrefirreKPFNAVE---NVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAeLGDRQL 81
Cdd:COG1126 1 MIEIENLH-------KSFGDLEvlkGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 82 SELRnRTMGICTQSQSLLASLNALDNAILPATLYSKASSETAFTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARAL 161
Cdd:COG1126 73 NKLR-RKVGMVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARAL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 307615102 162 VNHPQVFIADEPTGDLDAqstEL------VMRLLAglpEAGTAVVFATHD 205
Cdd:COG1126 152 AMEPKVMLFDEPTSALDP---ELvgevldVMRDLA---KEGMTMVVVTHE 195
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
6-206 |
2.11e-30 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 113.12 E-value: 2.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 6 IEAKQLTREFIRREKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQLSELR 85
Cdd:cd03294 21 LAKGKSKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 86 NRTMGICTQSQSLLASLNALDNAILPATLySKASSETAFTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNHP 165
Cdd:cd03294 101 RKKISMVFQSFALLPHRTVLENVAFGLEV-QGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDP 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 307615102 166 QVFIADEPTGDLD----AQSTELVMRLLAglpEAGTAVVFATHDP 206
Cdd:cd03294 180 DILLMDEAFSALDplirREMQDELLRLQA---ELQKTIVFITHDL 221
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-223 |
2.29e-30 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 111.45 E-value: 2.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 6 IEAKQLTREFIRRekpfNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELgdrQLSELR 85
Cdd:COG4619 1 LELEGLSFRVGGK----PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAM---PPPEWR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 86 NRTMGICTQSQSLLASLnaLDNAILPATLYSKASSETaftRALELFEALeikHLTEAY----PNELSGGEMRRVAIARAL 161
Cdd:COG4619 74 RQVAYVPQEPALWGGTV--RDNLPFPFQLRERKFDRE---RALELLERL---GLPPDIldkpVERLSGGERQRLALIRAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 307615102 162 VNHPQVFIADEPTGDLDAQSTELVMRLLAGLP-EAGTAVVFATHDP-QALETARTVYEINAGVL 223
Cdd:COG4619 146 LLQPDVLLLDEPTSALDPENTRRVEELLREYLaEEGRAVLWVSHDPeQIERVADRVLTLEAGRL 209
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-223 |
4.61e-30 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 111.72 E-value: 4.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 1 MSELVIEAKQLTreFIRREKPfnAVENVNLEIAPHDLVAIVGRSGNGKttllnlltgllKPTSGEVRVAGQNLAELGDR- 79
Cdd:COG1121 2 MMMPAIELENLT--VSYGGRP--VLEDVSLTIPPGEFVAIVGPNGAGKstllkailgllPPTSGTVRLFGKPPRRARRRi 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 80 ----QLSELrNRT----------MGiCTQSQSLLASLNALDNAilpatlyskassetaftRALELFEALEIKHLTEAYPN 145
Cdd:COG1121 78 gyvpQRAEV-DWDfpitvrdvvlMG-RYGRRGLFRRPSRADRE-----------------AVDEALERVGLEDLADRPIG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 307615102 146 ELSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATHDPQALET-ARTVYEINAGVL 223
Cdd:COG1121 139 ELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREyFDRVLLLNRGLV 217
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
6-221 |
6.77e-30 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 111.04 E-value: 6.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 6 IEAKQLTREFIRrekpFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELgdrqlsELR 85
Cdd:TIGR00968 1 IEIANISKRFGS----FQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRV------HAR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 86 NRTMGICTQSQSLLASLNALDNAILPATLYSKASSETAfTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNHP 165
Cdd:TIGR00968 71 DRKIGFVFQHYALFKHLTVRDNIAFGLEIRKHPKAKIK-ARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 307615102 166 QVFIADEPTGDLDAQSTELVMRLLAGL-PEAGTAVVFATHD-PQALETARTVYEINAG 221
Cdd:TIGR00968 150 QVLLLDEPFGALDAKVRKELRSWLRKLhDEVHVTTVFVTHDqEEAMEVADRIVVMSNG 207
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
24-205 |
2.72e-29 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 109.19 E-value: 2.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 24 AVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQLSELRnRTMGICTQSQSLLASLN 103
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLR-RQIGMIFQDHHLLMDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 104 ALDNAILPATLySKASSETAFTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTE 183
Cdd:PRK10908 96 VYDNVAIPLII-AGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSE 174
|
170 180
....*....|....*....|..
gi 307615102 184 LVMRLLAGLPEAGTAVVFATHD 205
Cdd:PRK10908 175 GILRLFEEFNRVGVTVLMATHD 196
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
22-221 |
3.43e-29 |
|
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: 109.19 E-value: 3.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 22 FNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQLSELRNRtMGICTQSQSLLAS 101
Cdd:cd03256 14 KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQ-IGMIFQQFNLIER 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 102 LNALDNAILPA-----------TLYSKASSEtaftRALELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNHPQVFIA 170
Cdd:cd03256 93 LSVLENVLSGRlgrrstwrslfGLFPKEEKQ----RALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 307615102 171 DEPTGDLDAQSTELVMRLLAGL-PEAGTAVVFATHDPQ-ALETARTVYEINAG 221
Cdd:cd03256 169 DEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDlAREYADRIVGLKDG 221
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
23-223 |
1.28e-28 |
|
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: 106.85 E-value: 1.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 23 NAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDR-----QLSELrNRTMGIctqsqS 97
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRigyvpQRRSI-DRDFPI-----S 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 98 LLAS-LNALDNAILPATLYSKASSEtaftRALELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNHPQVFIADEPTGD 176
Cdd:cd03235 87 VRDVvLMGLYGHKGLFRRLSKADKA----KVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 307615102 177 LDAQSTELVMRLLAGLPEAGTAVVFATHDPQALET-ARTVYEINAGVL 223
Cdd:cd03235 163 VDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEyFDRVLLLNRTVV 210
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-210 |
5.02e-28 |
|
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: 106.43 E-value: 5.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 6 IEAKQLTREFIRREKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQnlaELGDRQLSELR 85
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGR---PVTRRRRKAFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 86 nRTMGICTQSQslLASLNA---LDNAIL-PATLYSKASSETAFTRALELFEaleikhLTEA----YPNELSGGEMRRVAI 157
Cdd:COG1124 79 -RRVQMVFQDP--YASLHPrhtVDRILAePLRIHGLPDREERIAELLEQVG------LPPSfldrYPHQLSGGQRQRVAI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 307615102 158 ARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGL-PEAGTAVVFATHDPQALE 210
Cdd:COG1124 150 ARALILEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVA 203
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
22-215 |
8.32e-28 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 105.48 E-value: 8.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 22 FNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNL---AELGDRQLSELRnRTMGICTQSQSL 98
Cdd:COG4161 15 HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIRLLR-QKVGMVFQQYNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 99 LASLNALDNAILPATLYSKASSETAFTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNHPQVFIADEPTGDLD 178
Cdd:COG4161 94 WPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALD 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 307615102 179 AQSTELVMRLLAGLPEAGTAVVFATHDpqaLETARTV 215
Cdd:COG4161 174 PEITAQVVEIIRELSQTGITQVIVTHE---VEFARKV 207
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-223 |
1.33e-27 |
|
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: 104.26 E-value: 1.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 6 IEAKQLTREFirreKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELgdrqlsELR 85
Cdd:cd03301 1 VELENVTKRF----GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDL------PPK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 86 NRTMGICTQSQSLLASLNALDNAILPATLySKASSETAFTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNHP 165
Cdd:cd03301 71 DRDIAMVFQNYALYPHMTVYDNIAFGLKL-RKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 307615102 166 QVFIADEPTGDLDAQ-----STELVmRLLAGLpeaGTAVVFATHDP-QALETARTVYEINAGVL 223
Cdd:cd03301 150 KVFLMDEPLSNLDAKlrvqmRAELK-RLQQRL---GTTTIYVTHDQvEAMTMADRIAVMNDGQI 209
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-209 |
1.85e-27 |
|
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: 105.13 E-value: 1.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 5 VIEAKQLTreFIRREKPfnAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQLSel 84
Cdd:COG1120 1 MLEAENLS--VGYGGRP--VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELA-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 85 rnRTMGICTQSQSLLASLNALDNAIL---PATLYSKASSETAFTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARAL 161
Cdd:COG1120 75 --RRIAYVPQEPPAPFGLTVRELVALgryPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARAL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 307615102 162 VNHPQVFIADEPTGDLDAQSTELVMRLLAGL-PEAGTAVVFATHDP-QAL 209
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDLAHQLEVLELLRRLaRERGRTVVMVLHDLnLAA 202
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
6-221 |
2.10e-27 |
|
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: 104.34 E-value: 2.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 6 IEAKQLTREFIRrekpFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGdrqlseLR 85
Cdd:cd03296 3 IEVRNVSKRFGD----FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP------VQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 86 NRTMGICTQSQSLLASLNALDNA-----ILPATlySKASSETAFTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARA 160
Cdd:cd03296 73 ERNVGFVFQHYALFRHMTVFDNVafglrVKPRS--ERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 307615102 161 LVNHPQVFIADEPTGDLDAQSTELVMRLLAGL-PEAGTAVVFATHD-PQALETARTVYEINAG 221
Cdd:cd03296 151 LAVEPKVLLLDEPFGALDAKVRKELRRWLRRLhDELHVTTVFVTHDqEEALEVADRVVVMNKG 213
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-215 |
2.33e-27 |
|
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: 103.33 E-value: 2.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 5 VIEAKQLTREFIRREkpfnAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRqlsel 84
Cdd:COG4133 2 MLEAENLSCRRGERL----LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARED----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 85 RNRTMGICTQSQSLLASLNALDNAILPATLYSKASSETAFTRALElfeALEIKHLTEAYPNELSGGEMRRVAIARALVNH 164
Cdd:COG4133 73 YRRRLAYLGHADGLKPELTVRENLRFWAALYGLRADREAIDEALE---AVGLAGLADLPVRQLSAGQKRRVALARLLLSP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 307615102 165 PQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATHDPQALETARTV 215
Cdd:COG4133 150 APLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELAAARVL 200
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
22-221 |
2.59e-27 |
|
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: 104.24 E-value: 2.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 22 FNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQlselrnRTMGICTQSQSLLAS 101
Cdd:cd03300 13 FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK------RPVNTVFQNYALFPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 102 LNALDNAILPATL--YSKASSETAFTRALELFEALEIKHlteAYPNELSGGEMRRVAIARALVNHPQVFIADEPTGDLDA 179
Cdd:cd03300 87 LTVFENIAFGLRLkkLPKAEIKERVAEALDLVQLEGYAN---RKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 307615102 180 Q-STELVMRLLAGLPEAGTAVVFATHDPQ-ALETARTVYEINAG 221
Cdd:cd03300 164 KlRKDMQLELKRLQKELGITFVFVTHDQEeALTMSDRIAVMNKG 207
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-205 |
2.75e-27 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 105.97 E-value: 2.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 1 MSELVIEAKQLTREF-------IRREKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNL 73
Cdd:COG4608 3 MAEPLLEVRDLKKHFpvrgglfGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 74 AELGDRQLSELRnRTMGICTQSQslLASLN-------ALDNAILPATLYSKASSETaftRALELFEA--LEIKHLtEAYP 144
Cdd:COG4608 83 TGLSGRELRPLR-RRMQMVFQDP--YASLNprmtvgdIIAEPLRIHGLASKAERRE---RVAELLELvgLRPEHA-DRYP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 307615102 145 NELSGGEMRRVAIARALVNHPQVFIADEPTGDLD----AQstelVMRLLAGLP-EAGTAVVFATHD 205
Cdd:COG4608 156 HEFSGGQRQRIGIARALALNPKLIVCDEPVSALDvsiqAQ----VLNLLEDLQdELGLTYLFISHD 217
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-221 |
2.78e-27 |
|
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: 102.08 E-value: 2.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 6 IEAKQLTreFIRREKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELgdrQLSELR 85
Cdd:cd03228 1 IEFKNVS--FSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDL---DLESLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 86 NRtMGICTQsqsllaslnalDNAILPATLYSkassetaftralelfealeikhlteaypNELSGGEMRRVAIARALVNHP 165
Cdd:cd03228 76 KN-IAYVPQ-----------DPFLFSGTIRE----------------------------NILSGGQRQRIAIARALLRDP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 307615102 166 QVFIADEPTGDLDAQSTELVMRLLAGLPEaGTAVVFATHDPQALETARTVYEINAG 221
Cdd:cd03228 116 PILILDEATSALDPETEALILEALRALAK-GKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
21-226 |
9.71e-27 |
|
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: 103.69 E-value: 9.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 21 PF--NAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQLSELRnRTMGICTQ---S 95
Cdd:TIGR04521 15 PFekKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLR-KKVGLVFQfpeH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 96 QsLLASLNALDNAILPATLysKASSETAFTRAlelFEALEIKHLTEAY----PNELSGGEMRRVAIARALVNHPQVFIAD 171
Cdd:TIGR04521 94 Q-LFEETVYKDIAFGPKNL--GLSEEEAEERV---KEALELVGLDEEYlersPFELSGGQMRRVAIAGVLAMEPEVLILD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 307615102 172 EPTGDLDAQSTELVMRLLAGL-PEAGTAVVFATHD-PQALETARTVYEINAGVLSRQ 226
Cdd:TIGR04521 168 EPTAGLDPKGRKEILDLFKRLhKEKGLTVILVTHSmEDVAEYADRVIVMHKGKIVLD 224
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-205 |
1.26e-26 |
|
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: 106.69 E-value: 1.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 1 MSELVIEAKQLTREFIRREKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLL----TGLLKPTSGEVRVAGQNLAEL 76
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSIlrllPDPAAHPSGSILFDGQDLLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 77 GDRQLSELRNRTMGICTQSQslLASLNAL----DNAILPATLYSKASSETAFTRALELFEALEIKHLTE---AYPNELSG 149
Cdd:COG4172 82 SERELRRIRGNRIAMIFQEP--MTSLNPLhtigKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERrldAYPHQLSG 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 307615102 150 GEMRRVAIARALVNHPQVFIADEPTGDLD----AQstelVMRLLAGLP-EAGTAVVFATHD 205
Cdd:COG4172 160 GQRQRVMIAMALANEPDLLIADEPTTALDvtvqAQ----ILDLLKDLQrELGMALLLITHD 216
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-206 |
1.94e-26 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 104.41 E-value: 1.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 1 MSELVIEAKQLTREFirreKPFNAVENVNLEIAPHDLVAIVGRSGNGKttllnlltglLKPTSGEVRVAGQNLAELgdrq 80
Cdd:COG3842 1 MAMPALELENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKttllrmiagfETPDSGRILLDGRDVTGL---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 81 LSELRNrtMGICTQSQSLLASLNALDN-AilpatlYS----KASSETAFTRALELFEALEIKHLTEAYPNELSGGEMRRV 155
Cdd:COG3842 73 PPEKRN--VGMVFQDYALFPHLTVAENvA------FGlrmrGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRV 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 307615102 156 AIARALVNHPQVFIADEPTGDLDAQSTE----LVMRLLAglpEAGTAVVFATHDP 206
Cdd:COG3842 145 ALARALAPEPRVLLLDEPLSALDAKLREemreELRRLQR---ELGITFIYVTHDQ 196
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
24-215 |
2.46e-26 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 101.63 E-value: 2.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 24 AVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNL---AELGDRQLSELRnRTMGICTQSQSLLA 100
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAIRELR-RNVGMVFQQYNLWP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 101 SLNALDNAILPATLYSKASSETAFTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQ 180
Cdd:PRK11124 96 HLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE 175
|
170 180 190
....*....|....*....|....*....|....*
gi 307615102 181 STELVMRLLAGLPEAGTAVVFATHDpqaLETARTV 215
Cdd:PRK11124 176 ITAQIVSIIRELAETGITQVIVTHE---VEVARKT 207
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-223 |
3.79e-26 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 103.62 E-value: 3.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 1 MSelvIEAKQLTREFIRREkpfnAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELgdrq 80
Cdd:PRK10851 1 MS---IEIANIKKSFGRTQ----VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 81 lsELRNRTMGICTQSQSLLASLNALDN-----AILPAtlYSKASSETAFTRALELFEALEIKHLTEAYPNELSGGEMRRV 155
Cdd:PRK10851 70 --HARDRKVGFVFQHYALFRHMTVFDNiafglTVLPR--RERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 156 AIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGL-PEAGTAVVFATHDPQ-ALETARTVYEINAGVL 223
Cdd:PRK10851 146 ALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLhEELKFTSVFVTHDQEeAMEVADRVVVMSQGNI 215
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
24-221 |
7.15e-26 |
|
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: 98.80 E-value: 7.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 24 AVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELgDRQLSELRNRTmGICTQSQSLLASLN 103
Cdd:cd03229 15 VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDL-EDELPPLRRRI-GMVFQDFALFPHLT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 104 ALDNAILPatlyskassetaftralelfealeikhlteaypneLSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTE 183
Cdd:cd03229 93 VLENIALG-----------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRR 137
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 307615102 184 LVMRLLAGL-PEAGTAVVFATHDP-QALETARTVYEINAG 221
Cdd:cd03229 138 EVRALLKSLqAQLGITVVLVTHDLdEAARLADRVVVLRDG 177
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-223 |
8.49e-26 |
|
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: 99.95 E-value: 8.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 6 IEAKQLTREFirreKPFNAVENVNLEIAPHDLVAIVGRSGNGK-----TTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQ 80
Cdd:cd03260 1 IELRDLNVYY----GDKHALKDISLDIPKGEITALIGPSGCGKstllrLLNRLNDLIPGAPDEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 81 LsELRnRTMGICTQSQSLLaSLNALDNAILPATLYSKASSETAFTRALElfeALEIKHLTE-----AYPNELSGGEMRRV 155
Cdd:cd03260 77 L-ELR-RRVGMVFQKPNPF-PGSIYDNVAYGLRLHGIKLKEELDERVEE---ALRKAALWDevkdrLHALGLSGGQQQRL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 307615102 156 AIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPEAgTAVVFATHDP-QALETARTVYEINAGVL 223
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMqQAARVADRTAFLLNGRL 218
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-223 |
1.11e-25 |
|
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: 98.24 E-value: 1.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 6 IEAKQLTREFirreKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDrqlsELR 85
Cdd:cd03230 1 IEVRNLSKRY----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPE----EVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 86 NRtMGICTQSQSLLASLNALDNAilpatlyskassetaftralelfealeikhlteaypnELSGGEMRRVAIARALVNHP 165
Cdd:cd03230 73 RR-IGYLPEEPSLYENLTVRENL-------------------------------------KLSGGMKQRLALAQALLHDP 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 307615102 166 QVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATHDPQALET-ARTVYEINAGVL 223
Cdd:cd03230 115 ELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
23-223 |
2.02e-25 |
|
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: 103.76 E-value: 2.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 23 NAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGdrqLSELRNRtMGICTQSQSLLA-S 101
Cdd:COG2274 489 PVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQID---PASLRRQ-IGVVLQDVFLFSgT 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 102 LnaLDNaIlpaTLYSKASSETAFTRALELFEALE-IKHLTEAYP-------NELSGGEMRRVAIARALVNHPQVFIADEP 173
Cdd:COG2274 565 I--REN-I---TLGDPDATDEEIIEAARLAGLHDfIEALPMGYDtvvgeggSNLSGGQRQRLAIARALLRNPRILILDEA 638
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 307615102 174 TGDLDAQSTELVMRLLAGLpEAGTAVVFATHDPQALETARTVYEINAGVL 223
Cdd:COG2274 639 TSALDAETEAIILENLRRL-LKGRTVIIIAHRLSTIRLADRIIVLDKGRI 687
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-205 |
2.54e-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: 2.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 6 IEAKQLTREFirreKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAelgdRQLSELR 85
Cdd:cd03265 1 IEVENLVKKY----GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV----REPREVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 86 nRTMGICTQSQSLLASLNALDNAILPATLYSKASSETAfTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNHP 165
Cdd:cd03265 73 -RRIGIVFQDLSVDDELTGWENLYIHARLYGVPGAERR-ERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRP 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 307615102 166 QVFIADEPTGDLDAQSTELVMRLLAGLPEA-GTAVVFATHD 205
Cdd:cd03265 151 EVLFLDEPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHY 191
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-206 |
3.48e-25 |
|
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: 97.12 E-value: 3.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 7 EAKQLTreFIRREKPfnAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQLSELRn 86
Cdd:cd03214 1 EVENLS--VGYGGRT--VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKI- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 87 rtmgictqsqsllaslnaldnAILPATLyskassetaftralelfEALEIKHLTEAYPNELSGGEMRRVAIARALVNHPQ 166
Cdd:cd03214 76 ---------------------AYVPQAL-----------------ELLGLAHLADRPFNELSGGERQRVLLARALAQEPP 117
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 307615102 167 VFIADEPTGDLDAQSTELVMRLLAGL-PEAGTAVVFATHDP 206
Cdd:cd03214 118 ILLLDEPTSHLDIAHQIELLELLRRLaRERGKTVVMVLHDL 158
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-226 |
3.59e-25 |
|
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: 102.53 E-value: 3.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 2 SELVIEAKQLTrefIRREKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELgdrQL 81
Cdd:COG4988 333 GPPSIELEDVS---FSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDL---DP 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 82 SELRNRtMGICTQSQSLLA-SLnaLDNaILpatLYSKASSETAFTRALELFEALEikhLTEAYPNE-----------LSG 149
Cdd:COG4988 407 ASWRRQ-IAWVPQNPYLFAgTI--REN-LR---LGRPDASDEELEAALEAAGLDE---FVAALPDGldtplgeggrgLSG 476
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 307615102 150 GEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPeAGTAVVFATHDPQALETARTVYEINAGVLSRQ 226
Cdd:COG4988 477 GQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLALLAQADRILVLDDGRIVEQ 552
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
14-215 |
4.44e-25 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 98.63 E-value: 4.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 14 EFIRREKPFNAVE---NVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAElGDRQLSELRnRTMG 90
Cdd:PRK09493 3 EFKNVSKHFGPTQvlhNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVND-PKVDERLIR-QEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 91 ICTQSQSLLASLNALDNAILPATLYSKASSETAFTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNHPQVFIA 170
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 307615102 171 DEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATHDpqaLETARTV 215
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHE---IGFAEKV 202
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
24-205 |
5.96e-25 |
|
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: 96.72 E-value: 5.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 24 AVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAeLGDRQLSELRnRTMGICTQS--QSLLAS 101
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLD-YSRKGLLERR-QRVGLVFQDpdDQLFAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 102 LNALDNAILPATLysKASSETAFTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQS 181
Cdd:TIGR01166 85 DVDQDVAFGPLNL--GLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAG 162
|
170 180
....*....|....*....|....
gi 307615102 182 TELVMRLLAGLPEAGTAVVFATHD 205
Cdd:TIGR01166 163 REQMLAILRRLRAEGMTVVISTHD 186
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
25-214 |
1.15e-24 |
|
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: 97.41 E-value: 1.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 25 VENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRqlselrNRTMGICTQSQSLLASLNA 104
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE------KRDISYVPQNYALFPHMTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 105 LDNAI--LPATLYSKASSETaftRALELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQST 182
Cdd:cd03299 89 YKNIAygLKKRKVDKKEIER---KVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
|
170 180 190
....*....|....*....|....*....|...
gi 307615102 183 ELVMRLLAGL-PEAGTAVVFATHDpqaLETART 214
Cdd:cd03299 166 EKLREELKKIrKEFGVTVLHVTHD---FEEAWA 195
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-205 |
1.79e-24 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 97.24 E-value: 1.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 1 MSELVIEAKQLTREFIRREKPfnAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELG-DR 79
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGQPQP--ALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGaDR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 80 qlselrnrtmGICTQSQSLLASLNALDNAILPATL--YSKASSETaftRALELFEALEIKHLTEAYPNELSGGEMRRVAI 157
Cdd:COG4525 79 ----------GVVFQKDALLPWLNVLDNVAFGLRLrgVPKAERRA---RAEELLALVGLADFARRRIWQLSGGMRQRVGI 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 307615102 158 ARALVNHPQVFIADEPTGDLDA----QSTELVMRLLAglpEAGTAVVFATHD 205
Cdd:COG4525 146 ARALAADPRFLLMDEPFGALDAltreQMQELLLDVWQ---RTGKGVFLITHS 194
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
25-174 |
2.12e-24 |
|
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: 94.25 E-value: 2.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 25 VENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLaelgDRQLSELRNRTMGICTQSQSLLASLNA 104
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDL----TDDERKSLRKEIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 307615102 105 LDNAILPATLYSKaSSETAFTRALELFEALEIKHLTE----AYPNELSGGEMRRVAIARALVNHPQVFIADEPT 174
Cdd:pfam00005 77 RENLRLGLLLKGL-SKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-221 |
2.42e-24 |
|
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: 94.23 E-value: 2.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 7 EAKQLTREFIRREkpfnAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQLSelrn 86
Cdd:cd00267 1 EIENLSFRYGGRT----ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELR---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 87 RTMGICTQsqsllaslnaldnailpatlyskassetaftralelfealeikhlteaypneLSGGEMRRVAIARALVNHPQ 166
Cdd:cd00267 73 RRIGYVPQ----------------------------------------------------LSGGQRQRVALARALLLNPD 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 307615102 167 VFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATHDPQALETAR-TVYEINAG 221
Cdd:cd00267 101 LLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAAdRVIVLKDG 156
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
6-226 |
3.14e-24 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 96.36 E-value: 3.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 6 IEAKQLTREFirreKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRV------AGQNLAElGDR 79
Cdd:PRK11264 4 IEVKNLVKKF----HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidTARSLSQ-QKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 80 QLSELRNRtMGICTQSQSLLASLNALDNAILPATLYSKASSETAFTRALELFEALEIKHLTEAYPNELSGGEMRRVAIAR 159
Cdd:PRK11264 79 LIRQLRQH-VGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 307615102 160 ALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATHDPQ-ALETARTVYEINAGVLSRQ 226
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSfARDVADRAIFMDQGRIVEQ 225
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
6-210 |
7.11e-24 |
|
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: 94.74 E-value: 7.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 6 IEAKQLTREFIRREKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAelgdRQLSELR 85
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVV----KEPAEAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 86 NRtMGICTQSQSLLASLNALDNAILPATLYSKASSEtAFTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNHP 165
Cdd:cd03266 78 RR-LGFVSDSTGLYDRLTARENLEYFAGLYGLKGDE-LTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 307615102 166 QVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATHDPQALE 210
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVE 200
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-204 |
1.05e-23 |
|
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: 95.15 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 3 ELVIEAKQLTreFIRREKPfnAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSG-EVRVAGQnlaELGDRQL 81
Cdd:COG1119 1 DPLLELRNVT--VRRGGKT--ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGE---RRGGEDV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 82 SELRNRtMGICTQS--QSLLASLNALDnAILPA-----TLYSKASSETAfTRALELFEALEIKHLTEAYPNELSGGEMRR 154
Cdd:COG1119 74 WELRKR-IGLVSPAlqLRFPRDETVLD-VVLSGffdsiGLYREPTDEQR-ERARELLELLGLAHLADRPFGTLSQGEQRR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 307615102 155 VAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPEAG-TAVVFATH 204
Cdd:COG1119 151 VLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTH 201
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
25-205 |
1.08e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 95.67 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 25 VENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNL-AELGDRQLSELRNRTMGICTQSQSLLasln 103
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItPETGNKNLKKLRKKVSLVFQFPEAQL---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 104 aLDNAILPATLYSK----ASSETAFTRALELFEALEIKH-LTEAYPNELSGGEMRRVAIARALVNHPQVFIADEPTGDLD 178
Cdd:PRK13641 99 -FENTVLKDVEFGPknfgFSEDEAKEKALKWLKKVGLSEdLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180
....*....|....*....|....*..
gi 307615102 179 AQSTELVMRLLAGLPEAGTAVVFATHD 205
Cdd:PRK13641 178 PEGRKEMMQLFKDYQKAGHTVILVTHN 204
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-206 |
1.08e-22 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 93.98 E-value: 1.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 1 MSELVIEakQLTREFirreKPFNAVENVNLEIAPHDLVAIVGRSGNGKttllnlltgllKPTSGEVRVAGQNLAELgdrq 80
Cdd:COG3839 1 MASLELE--NVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKstllrmiagleDPTSGEILIGGRDVTDL---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 81 lsELRNRTMGICTQSQSLLASLNALDNAILPATL--YSKASSETAFTRALELfeaLEIKHLTEAYPNELSGGEMRRVAIA 158
Cdd:COG3839 71 --PPKDRNIAMVFQSYALYPHMTVYENIAFPLKLrkVPKAEIDRRVREAAEL---LGLEDLLDRKPKQLSGGQRQRVALG 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 307615102 159 RALVNHPQVFIADEPTGDLDAQS-----TELvMRLLAGLpeaGTAVVFATHDP 206
Cdd:COG3839 146 RALVREPKVFLLDEPLSNLDAKLrvemrAEI-KRLHRRL---GTTTIYVTHDQ 194
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-207 |
1.65e-22 |
|
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: 91.03 E-value: 1.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 6 IEAKQLTREFIRREKPfnAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAelgdRQLSELR 85
Cdd:cd03263 1 LQIRNLTKTYKKGTKP--AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR----TDRKAAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 86 NRtMGICTQSQSLLASLNALDNAILPATLYSKaSSETAFTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNHP 165
Cdd:cd03263 75 QS-LGYCPQFDALFDELTVREHLRFYARLKGL-PKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 307615102 166 QVFIADEPTGDLDAQSTELVMRLLAGLPEaGTAVVFATHDPQ 207
Cdd:cd03263 153 SVLLLDEPTSGLDPASRRAIWDLILEVRK-GRSIILTTHSMD 193
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-210 |
2.52e-22 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 94.48 E-value: 2.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 6 IEAKQLTREFirreKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLL--TGLLKPTSGEV----------------- 66
Cdd:TIGR03269 1 IEVKNLTKKF----DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIiyhvalcekcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 67 ------RVAGQNLAE-------LGDRQLSELRNRTMGICTQSQSLLASLNALDNAI--LPATLYSkasSETAFTRALELF 131
Cdd:TIGR03269 77 kvgepcPVCGGTLEPeevdfwnLSDKLRRRIRKRIAIMLQRTFALYGDDTVLDNVLeaLEEIGYE---GKEAVGRAVDLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 132 EALEIKHLTEAYPNELSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELVMR-LLAGLPEAGTAVVFATHDPQALE 210
Cdd:TIGR03269 154 EMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNaLEEAVKASGISMVLTSHWPEVIE 233
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-205 |
2.72e-22 |
|
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: 90.96 E-value: 2.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 6 IEAKQLTREFirreKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQLSElr 85
Cdd:cd03219 1 LEVRGLTKRF----GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIAR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 86 nrtMGIC-T-QSQSLLASLNALDNAILPATLYSKASSETAFT---------RALELFEALEIKHLTEAYPNELSGGEMRR 154
Cdd:cd03219 75 ---LGIGrTfQIPRLFPELTVLENVMVAAQARTGSGLLLARArreereareRAEELLERVGLADLADRPAGELSYGQQRR 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 307615102 155 VAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATHD 205
Cdd:cd03219 152 LEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHD 202
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-205 |
2.76e-22 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 92.72 E-value: 2.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 1 MSELVIEAKQLTREF-IRR-----EKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLA 74
Cdd:PRK11308 1 SQQPLLQAIDLKKHYpVKRglfkpERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 75 ElGDRQLSELRNRTMGICTQSQslLASLNALDN--AIL--PATLYSKASSETAFTRALELFE--ALEIKHlTEAYPNELS 148
Cdd:PRK11308 81 K-ADPEAQKLLRQKIQIVFQNP--YGSLNPRKKvgQILeePLLINTSLSAAERREKALAMMAkvGLRPEH-YDRYPHMFS 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 307615102 149 GGEMRRVAIARALVNHPQVFIADEPTGDLD----AQSTELVMRLLAglpEAGTAVVFATHD 205
Cdd:PRK11308 157 GGQRQRIAIARALMLDPDVVVADEPVSALDvsvqAQVLNLMMDLQQ---ELGLSYVFISHD 214
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
25-205 |
2.81e-22 |
|
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: 90.99 E-value: 2.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 25 VENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELG-DRQlselrnrtmgICTQSQSLLASLN 103
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGpDRM----------VVFQNYSLLPWLT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 104 ALDNAILPATLYSKASSETAFTRALElfEALEIKHLTEA---YPNELSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQ 180
Cdd:TIGR01184 71 VRENIALAVDRVLPDLSKSERRAIVE--EHIALVGLTEAadkRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
|
170 180
....*....|....*....|....*.
gi 307615102 181 S-TELVMRLLAGLPEAGTAVVFATHD 205
Cdd:TIGR01184 149 TrGNLQEELMQIWEEHRVTVLMVTHD 174
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
6-226 |
3.43e-22 |
|
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: 94.06 E-value: 3.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 6 IEAKQLTreFIRREKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQLSelr 85
Cdd:COG4987 334 LELEDVS--FRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLR--- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 86 nRTMGICTQ-----SQSLLASLN-ALDNAilpatlyskasSETAFTRALElfeALEIKHLTEAYPN-----------ELS 148
Cdd:COG4987 409 -RRIAVVPQrphlfDTTLRENLRlARPDA-----------TDEELWAALE---RVGLGDWLAALPDgldtwlgeggrRLS 473
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 307615102 149 GGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLpEAGTAVVFATHDPQALETARTVYEINAGVLSRQ 226
Cdd:COG4987 474 GGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEA-LAGRTVLLITHRLAGLERMDRILVLEDGRIVEQ 550
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
7-215 |
4.18e-22 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 90.80 E-value: 4.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 7 EAKQLTREFIRREKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGD-------- 78
Cdd:PRK10619 3 ENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDkdgqlkva 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 79 --RQLSELRNRtMGICTQSQSLLASLNALDNAILPATLYSKASSETAFTRALELFEALEIKHLTEA-YPNELSGGEMRRV 155
Cdd:PRK10619 83 dkNQLRLLRTR-LTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGkYPVHLSGGQQQRV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 156 AIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATHDpqaLETARTV 215
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHE---MGFARHV 218
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-221 |
1.30e-21 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 90.98 E-value: 1.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 1 MSelvIEAKQLTREFirreKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLaelgDRQ 80
Cdd:COG1118 1 MS---IEVRNISKRF----GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL----FTN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 81 LSeLRNRTMGICTQSQSLLASLNALDN-AI-LPATLYSKASSETaftRALELFEALEIKHLTEAYPNELSGGEMRRVAIA 158
Cdd:COG1118 70 LP-PRERRVGFVFQHYALFPHMTVAENiAFgLRVRPPSKAEIRA---RVEELLELVQLEGLADRYPSQLSGGQRQRVALA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 307615102 159 RALVNHPQVFIADEPTGDLDAQSTELVMRLLAGL-PEAGTAVVFATHDPQ-ALETARTVYEINAG 221
Cdd:COG1118 146 RALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLhDELGGTTVFVTHDQEeALELADRVVVMNQG 210
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
2-205 |
4.35e-21 |
|
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: 88.17 E-value: 4.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 2 SELVIEAKQLTREF--IRrekpfnAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDR 79
Cdd:COG0411 1 SDPLLEVRGLTKRFggLV------AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 80 QlselRNRtMGIC-T-QSQSLLASLNALDNAILPATLYSKASSETAFT--------------RALELFEALEIKHLTEAY 143
Cdd:COG0411 75 R----IAR-LGIArTfQNPRLFPELTVLENVLVAAHARLGRGLLAALLrlprarreereareRAEELLERVGLADRADEP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 307615102 144 PNELSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLP-EAGTAVVFATHD 205
Cdd:COG0411 150 AGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRdERGITILLIEHD 212
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
15-202 |
4.47e-21 |
|
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: 87.67 E-value: 4.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 15 FIRREKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELgdrQLSELRnRTMGICTQ 94
Cdd:cd03251 8 FRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDY---TLASLR-RQIGLVSQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 95 sQSLLASLNALDNailpaTLYSK-ASSETAFTRALELFEALE-IKHLTEAYPNE-------LSGGEMRRVAIARALVNHP 165
Cdd:cd03251 84 -DVFLFNDTVAEN-----IAYGRpGATREEVEEAARAANAHEfIMELPEGYDTVigergvkLSGGQRQRIAIARALLKDP 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 307615102 166 QVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFA 202
Cdd:cd03251 158 PILILDEATSALDTESERLVQAALERLMKNRTTFVIA 194
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
24-205 |
1.10e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 87.44 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 24 AVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLaELGDRQLSELRnRTMGICTQS--QSLLAS 101
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEVR-KTVGIVFQNpdDQLFAP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 102 LNALDNAILPATLysKASSETAFTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQS 181
Cdd:PRK13639 95 TVEEDVAFGPLNL--GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMG 172
|
170 180
....*....|....*....|....
gi 307615102 182 TELVMRLLAGLPEAGTAVVFATHD 205
Cdd:PRK13639 173 ASQIMKLLYDLNKEGITIIISTHD 196
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
24-202 |
1.58e-20 |
|
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: 86.39 E-value: 1.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 24 AVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELgdrQLSELRnRTMGICTQSqSLLASLN 103
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALA---DPAWLR-RQVGVVLQE-NVLFNRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 104 ALDNAILPATlyskASSETAFTRALELFEALE-IKHLTEAYPN-------ELSGGEMRRVAIARALVNHPQVFIADEPTG 175
Cdd:cd03252 92 IRDNIALADP----GMSMERVIEAAKLAGAHDfISELPEGYDTivgeqgaGLSGGQRQRIAIARALIHNPRILIFDEATS 167
|
170 180
....*....|....*....|....*..
gi 307615102 176 DLDAQSTELVMRLLAGLPEAGTAVVFA 202
Cdd:cd03252 168 ALDYESEHAIMRNMHDICAGRTVIIIA 194
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-205 |
2.04e-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: 88.97 E-value: 2.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 3 ELVIEAKQLTREFI-------RREKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLkPTSGEVRVAGQNLAE 75
Cdd:COG4172 273 PPLLEARDLKVWFPikrglfrRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 76 LGDRQLSELRnRTMGICTQSQslLASLN----ALDnaILPATLYSKASSETAFTRALELFEALEIKHLTEA----YPNEL 147
Cdd:COG4172 352 LSRRALRPLR-RRMQVVFQDP--FGSLSprmtVGQ--IIAEGLRVHGPGLSAAERRARVAEALEEVGLDPAarhrYPHEF 426
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 307615102 148 SGGEMRRVAIARALVNHPQVFIADEPTGDLD----AQstelVMRLLAGLP-EAGTAVVFATHD 205
Cdd:COG4172 427 SGGQRQRIAIARALILEPKLLVLDEPTSALDvsvqAQ----ILDLLRDLQrEHGLAYLFISHD 485
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
23-221 |
2.24e-20 |
|
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: 85.33 E-value: 2.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 23 NAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELgdrQLSELRnRTMGICTQSQSL---- 98
Cdd:cd03245 18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQL---DPADLR-RNIGYVPQDVTLfygt 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 99 ------LASLNALDNAILPAtlySKASSETAFTRALELFEALEIKHLTEAypneLSGGEMRRVAIARALVNHPQVFIADE 172
Cdd:cd03245 94 lrdnitLGAPLADDERILRA---AELAGVTDFVNKHPNGLDLQIGERGRG----LSGGQRQAVALARALLNDPPILLLDE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 307615102 173 PTGDLDAQSTELVMRLLAGLPEAGTAVVfATHDPQALETARTVYEINAG 221
Cdd:cd03245 167 PTSAMDMNSEERLKERLRQLLGDKTLII-ITHRPSLLDLVDRIIVMDSG 214
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
23-215 |
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: 88.50 E-value: 2.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 23 NAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELgdrqLSELRNRTMGICTQSQSLLASl 102
Cdd:TIGR02857 336 PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADA----DADSWRDQIAWVPQHPFLFAG- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 103 NALDNaILpatLYSKASSETAFTRALELFEALE-IKHLTEAY-------PNELSGGEMRRVAIARALVNHPQVFIADEPT 174
Cdd:TIGR02857 411 TIAEN-IR---LARPDASDAEIREALERAGLDEfVAALPQGLdtpigegGAGLSGGQAQRLALARAFLRDAPLLLLDEPT 486
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 307615102 175 GDLDAQSTELVMRLLAGLPEaGTAVVFATHDPQALETARTV 215
Cdd:TIGR02857 487 AHLDAETEAEVLEALRALAQ-GRTVLLVTHRLALAALADRI 526
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
5-221 |
4.34e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 86.01 E-value: 4.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 5 VIEAKQLTREFIRREKpfnAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAElgdRQLSEL 84
Cdd:PRK13652 3 LIETRDLCYSYSGSKE---ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITK---ENIREV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 85 RnRTMGICTQS--QSLLASLNALDNAILPATLysKASSETAFTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARALV 162
Cdd:PRK13652 77 R-KFVGLVFQNpdDQIFSPTVEQDIAFGPINL--GLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 307615102 163 NHPQVFIADEPTGDLDAQSTELVMRLLAGLPEA-GTAVVFATHDPQAL-ETARTVYEINAG 221
Cdd:PRK13652 154 MEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVpEMADYIYVMDKG 214
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
24-216 |
4.79e-20 |
|
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: 84.79 E-value: 4.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 24 AVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAelgdRQLSELRNRtMGI--CTQSQSLLAS 101
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDIT----GLPPHERAR-AGIgyVPEGRRIFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 102 LNALDNAILPATLYSKASSETAFTRALELFEALEIKHLTEAYpnELSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQS 181
Cdd:cd03224 90 LTVEENLLLGAYARRRAKRKARLERVYELFPRLKERRKQLAG--TLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKI 167
|
170 180 190
....*....|....*....|....*....|....*.
gi 307615102 182 TELVMRLLAGLPEAGTAVVFATHD-PQALETARTVY 216
Cdd:cd03224 168 VEEIFEAIRELRDEGVTILLVEQNaRFALEIADRAY 203
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
15-216 |
7.61e-20 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 85.20 E-value: 7.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 15 FIRREKPFnaVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQLSELRNRtMGICTQ 94
Cdd:PRK11831 15 FTRGNRCI--FDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKR-MSMLFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 95 SQSLLASLNALDNAILPATLYSKASSETAFTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNHPQVFIADEPT 174
Cdd:PRK11831 92 SGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPF 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 307615102 175 GDLDAQSTELVMRLLAGLPEA-GTAVVFATHD-PQALETARTVY 216
Cdd:PRK11831 172 VGQDPITMGVLVKLISELNSAlGVTCVVVSHDvPEVLSIADHAY 215
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-204 |
7.80e-20 |
|
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: 83.87 E-value: 7.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 6 IEAKQLTREFirreKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGqnlaelgdRQLSELR 85
Cdd:cd03269 1 LEVENVTKRF----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG--------KPLDIAA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 86 NRTMGICTQSQSLLASLNALDNAILPATLYSKASSEtAFTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNHP 165
Cdd:cd03269 69 RNRIGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEE-ARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDP 147
|
170 180 190
....*....|....*....|....*....|....*....
gi 307615102 166 QVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATH 204
Cdd:cd03269 148 ELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTH 186
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
9-205 |
9.63e-20 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 86.63 E-value: 9.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 9 KQLTREFIRREKPFN-AVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQLSELRNR 87
Cdd:PRK10070 27 QGLSKEQILEKTGLSlGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 88 TMGICTQSQSLLASLNALDNAILPATLYSKASSETAfTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNHPQV 167
Cdd:PRK10070 107 KIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERR-EKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDI 185
|
170 180 190
....*....|....*....|....*....|....*....
gi 307615102 168 FIADEPTGDLDAQ-STELVMRLLAGLPEAGTAVVFATHD 205
Cdd:PRK10070 186 LLMDEAFSALDPLiRTEMQDELVKLQAKHQRTIVFISHD 224
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
27-221 |
1.05e-19 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 86.24 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 27 NVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELgdrqlsELRNRTMGICTQSQSLLASLNALD 106
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDV------PPAERGVGMVFQSYALYPHLSVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 107 NAILPATLySKASSETAFTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNHPQVFIADEPTGDLDA------- 179
Cdd:PRK11000 95 NMSFGLKL-AGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAalrvqmr 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 307615102 180 -QSTELVMRLlaglpeaGTAVVFATHDP-QALETARTVYEINAG 221
Cdd:PRK11000 174 iEISRLHKRL-------GRTMIYVTHDQvEAMTLADKIVVLDAG 210
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
28-213 |
1.17e-19 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 85.93 E-value: 1.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 28 VNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQLSELRNRTMGICTQSQSLLASLNALDN 107
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 108 AILPATLYSKASSETAFTRALELfeaLEIKHLTEAYPNELSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELVMR 187
Cdd:TIGR02142 96 LRYGMKRARPSERRISFERVIEL---LGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
|
170 180
....*....|....*....|....*..
gi 307615102 188 LLAGL-PEAGTAVVFATHDPQalETAR 213
Cdd:TIGR02142 173 YLERLhAEFGIPILYVSHSLQ--EVLR 197
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-205 |
1.80e-19 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 85.16 E-value: 1.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 1 MSELVIEAKQLTREFIRREKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKP---TSGEVRVAGQNLAELG 77
Cdd:PRK09473 8 QADALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 78 DRQLSELRNRTMGICTQSQslLASLNAL----DNAILPATLYSKASSETAFTRALELFEALEIKhltEA------YPNEL 147
Cdd:PRK09473 88 EKELNKLRAEQISMIFQDP--MTSLNPYmrvgEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMP---EArkrmkmYPHEF 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 307615102 148 SGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLP-EAGTAVVFATHD 205
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKrEFNTAIIMITHD 221
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
21-226 |
1.94e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 84.03 E-value: 1.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 21 PFN--AVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNL-AELGDRQLSELRnRTMGICTQ--- 94
Cdd:PRK13649 17 PFEgrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItSTSKNKDIKQIR-KKVGLVFQfpe 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 95 SQsLLASLNALDNAILPATLysKASSETAFTRALELFEALEI-KHLTEAYPNELSGGEMRRVAIARALVNHPQVFIADEP 173
Cdd:PRK13649 96 SQ-LFEETVLKDVAFGPQNF--GVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 307615102 174 TGDLDAQSTELVMRLLAGLPEAGTAVVFATH--DPQAlETARTVYEINAG--VLSRQ 226
Cdd:PRK13649 173 TAGLDPKGRKELMTLFKKLHQSGMTIVLVTHlmDDVA-NYADFVYVLEKGklVLSGK 228
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
29-211 |
3.48e-19 |
|
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: 82.34 E-value: 3.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 29 NLEIA---PHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAElgDRQLSEL--RNRTMGICTQSQSLLASLN 103
Cdd:cd03297 14 TLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFD--SRKKINLppQQRKIGLVFQQYALFPHLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 104 ALDNaiLPATLYSKASSETAFtRALELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTE 183
Cdd:cd03297 92 VREN--LAFGLKRKRNREDRI-SVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180
....*....|....*....|....*....
gi 307615102 184 LVMRLLAGLPEA-GTAVVFATHDPQALET 211
Cdd:cd03297 169 QLLPELKQIKKNlNIPVIFVTHDLSEAEY 197
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
7-206 |
4.04e-19 |
|
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: 81.92 E-value: 4.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 7 EAKQLTREFirrEKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAElGDRQlselrn 86
Cdd:cd03226 1 RIENISFSY---KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA-KERR------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 87 RTMGICTQ-SQSLLASLNALDNAILPATLYSKASSETAftralELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNHP 165
Cdd:cd03226 71 KSIGYVMQdVDYQLFTDSVREELLLGLKELDAGNEQAE-----TVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGK 145
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 307615102 166 QVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATHDP 206
Cdd:cd03226 146 DLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDY 186
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
4-208 |
5.11e-19 |
|
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: 81.44 E-value: 5.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 4 LVIEAKQLTreFIRREKPFNAVE----NVNLEIAPHDLVAIVGRSGNGKTT--LLNLLTGLLKPTSGEVRVAGQNlaelg 77
Cdd:cd03213 2 VTLSFRNLT--VTVKSSPSKSGKqllkNVSGKAKPGELTAIMGPSGAGKSTllNALAGRRTGLGVSGEVLINGRP----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 78 dRQLSELRNRtMGICTQSQSLLASLnaldnailpaTLYskassETaftraleLFEALEIKhlteaypnELSGGEMRRVAI 157
Cdd:cd03213 75 -LDKRSFRKI-IGYVPQDDILHPTL----------TVR-----ET-------LMFAAKLR--------GLSGGERKRVSI 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 307615102 158 ARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATHDPQA 208
Cdd:cd03213 123 ALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSS 173
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
6-216 |
6.99e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 83.21 E-value: 6.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 6 IEAKQLTREFIRREK-PFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEV----------RVAGQNLA 74
Cdd:PRK13651 3 IKVKNIVKIFNKKLPtELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 75 ELGD-----------RQLSELRNRtMGICTQsqslLASLNALDNAILPATLYSKAS----SETAFTRALELfeaLEIKHL 139
Cdd:PRK13651 83 VLEKlviqktrfkkiKKIKEIRRR-VGVVFQ----FAEYQLFEQTIEKDIIFGPVSmgvsKEEAKKRAAKY---IELVGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 140 TEAY----PNELSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATHD-PQALE-TAR 213
Cdd:PRK13651 155 DESYlqrsPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDlDNVLEwTKR 234
|
...
gi 307615102 214 TVY 216
Cdd:PRK13651 235 TIF 237
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
15-205 |
9.06e-19 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 83.22 E-value: 9.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 15 FIRREKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQLSELRNRTMGICtq 94
Cdd:PRK15079 27 FWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMIF-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 95 sQSLLASLNALDN-----AILPATLYSKASSETAFTRALELFEALEI-KHLTEAYPNELSGGEMRRVAIARALVNHPQVF 168
Cdd:PRK15079 105 -QDPLASLNPRMTigeiiAEPLRTYHPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLI 183
|
170 180 190
....*....|....*....|....*....|....*...
gi 307615102 169 IADEPTGDLDAQSTELVMRLLAGLP-EAGTAVVFATHD 205
Cdd:PRK15079 184 ICDEPVSALDVSIQAQVVNLLQQLQrEMGLSLIFIAHD 221
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
6-213 |
1.33e-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: 80.10 E-value: 1.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 6 IEAKQLTREfiRREKPfnAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDrqlseLR 85
Cdd:TIGR01189 1 LAARNLACS--RGERM--LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRD-----EP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 86 NRTMGICTQSQSLLASLNALDNAILPATLYSKASsetaftraLELFEALE---IKHLTEAYPNELSGGEMRRVAIARALV 162
Cdd:TIGR01189 72 HENILYLGHLPGLKPELSALENLHFWAAIHGGAQ--------RTIEDALAavgLTGFEDLPAAQLSAGQQRRLALARLWL 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 307615102 163 NHPQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATHDPQALETAR 213
Cdd:TIGR01189 144 SRRPLWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTHQDLGLVEAR 194
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
21-204 |
1.59e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 81.99 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 21 PFN--AVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNL-AELGDRQLSELRNRtMGICTQ--- 94
Cdd:PRK13634 17 PFErrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItAGKKNKKLKPLRKK-VGIVFQfpe 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 95 SQsLLASLNALDNAILPATLysKASSETAFTRALELfeaLEIKHLTEAY----PNELSGGEMRRVAIARALVNHPQVFIA 170
Cdd:PRK13634 96 HQ-LFEETVEKDICFGPMNF--GVSEEDAKQKAREM---IELVGLPEELlarsPFELSGGQMRRVAIAGVLAMEPEVLVL 169
|
170 180 190
....*....|....*....|....*....|....*
gi 307615102 171 DEPTGDLDAQSTELVMRLLAGL-PEAGTAVVFATH 204
Cdd:PRK13634 170 DEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTH 204
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
25-223 |
1.67e-18 |
|
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: 79.57 E-value: 1.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 25 VENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGdrqLSELRnRTMGICTQSQSLLA-SLN 103
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWD---PNELG-DHVGYLPQDDELFSgSIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 104 AldnailpatlyskassetaftralelfealeikhlteaypNELSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTE 183
Cdd:cd03246 94 E----------------------------------------NILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGER 133
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 307615102 184 LVMRLLAGLPEAGTAVVFATHDPQALETARTVYEINAGVL 223
Cdd:cd03246 134 ALNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
24-212 |
2.72e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 79.20 E-value: 2.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 24 AVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGqnlaelGDR-----QLSELRNR---------TM 89
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG------GARvayvpQRSEVPDSlpltvrdlvAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 90 GICtQSQSLLASLNALDNAILpatlyskassetafTRALElfeALEIKHLTEAYPNELSGGEMRRVAIARALVNHPQVFI 169
Cdd:NF040873 81 GRW-ARRGLWRRLTRDDRAAV--------------DDALE---RVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 307615102 170 ADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATHDPQALETA 212
Cdd:NF040873 143 LDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRA 185
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-205 |
3.37e-18 |
|
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: 80.55 E-value: 3.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 6 IEAKQLTREFIRREKPfnAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAElgDRQLSELR 85
Cdd:TIGR04520 1 IEVENVSFSYPESEKP--ALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLD--EENLWEIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 86 NRtMGICTQsqsllaslNAlDNAILPATlyskASSETAF-------------TRALELFEALEIKHLTEAYPNELSGGEM 152
Cdd:TIGR04520 77 KK-VGMVFQ--------NP-DNQFVGAT----VEDDVAFglenlgvpreemrKRVDEALKLVGMEDFRDREPHLLSGGQK 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 307615102 153 RRVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGL-PEAGTAVVFATHD 205
Cdd:TIGR04520 143 QRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLnKEEGITVISITHD 196
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
21-204 |
3.52e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 80.93 E-value: 3.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 21 PF--NAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQLSELRNRTMGICTQ--SQ 96
Cdd:PRK13643 16 PFasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQfpES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 97 SLLASLNALDNAILPATLysKASSETAFTRALELFEALEI-KHLTEAYPNELSGGEMRRVAIARALVNHPQVFIADEPTG 175
Cdd:PRK13643 96 QLFEETVLKDVAFGPQNF--GIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTA 173
|
170 180
....*....|....*....|....*....
gi 307615102 176 DLDAQSTELVMRLLAGLPEAGTAVVFATH 204
Cdd:PRK13643 174 GLDPKARIEMMQLFESIHQSGQTVVLVTH 202
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
25-205 |
4.59e-18 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 80.12 E-value: 4.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 25 VENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQLSELRnRTMGICTQSqsllaSLNA 104
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFR-RDIQMVFQD-----SISA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 105 LD-----NAILPATL-----YSKASSETaftRALELFEALEIK-HLTEAYPNELSGGEMRRVAIARALVNHPQVFIADEP 173
Cdd:PRK10419 102 VNprktvREIIREPLrhllsLDKAERLA---RASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEA 178
|
170 180 190
....*....|....*....|....*....|...
gi 307615102 174 TGDLDAQSTELVMRLLAGL-PEAGTAVVFATHD 205
Cdd:PRK10419 179 VSNLDLVLQAGVIRLLKKLqQQFGTACLFITHD 211
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
6-223 |
4.86e-18 |
|
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: 79.68 E-value: 4.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 6 IEAKQLTREFIRREKP----------FN-------AVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRV 68
Cdd:cd03267 1 IEVSNLSKSYRVYSKEpgligslkslFKrkyreveALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 69 AGqnlaELGDRQLSELRNRTMGICTQSQSLLASLNALDNAILPATLYSKASSETAFTRAlELFEALEIKHLTEAYPNELS 148
Cdd:cd03267 81 AG----LVPWKRRKKFLRRIGVVFGQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLD-ELSELLDLEELLDTPVRQLS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 307615102 149 GGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGL-PEAGTAVVFATHDPQALET-ARTVYEINAGVL 223
Cdd:cd03267 156 LGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHYMKDIEAlARRVLVIDKGRL 232
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-178 |
5.22e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 80.48 E-value: 5.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 1 MSelvIEAKQLTreFIRREK-PFN--AVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELG 77
Cdd:PRK13637 1 MS---IKIENLT--HIYMEGtPFEkkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 78 dRQLSELRNRtMGICTQ--SQSLLASLNALDNAILPATL-YSKASSETAFTRALELFeALEIKHLTEAYPNELSGGEMRR 154
Cdd:PRK13637 76 -VKLSDIRKK-VGLVFQypEYQLFEETIEKDIAFGPINLgLSEEEIENRVKRAMNIV-GLDYEDYKDKSPFELSGGQKRR 152
|
170 180
....*....|....*....|....
gi 307615102 155 VAIARALVNHPQVFIADEPTGDLD 178
Cdd:PRK13637 153 VAIAGVVAMEPKILILDEPTAGLD 176
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-178 |
6.24e-18 |
|
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: 81.77 E-value: 6.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 5 VIEAKQLTREFIRREKPF-NAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRV-AGQNLAELGDRQLS 82
Cdd:TIGR03269 279 IIKVRNVSKRYISVDRGVvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrVGDEWVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 83 ElRNRT---MGICTQSQSLLASLNALDN---AI---LPATLyskASSETAFTRALELFEALEIKHLTEAYPNELSGGEMR 153
Cdd:TIGR03269 359 G-RGRAkryIGILHQEYDLYPHRTVLDNlteAIgleLPDEL---ARMKAVITLKMVGFDEEKAEEILDKYPDELSEGERH 434
|
170 180
....*....|....*....|....*
gi 307615102 154 RVAIARALVNHPQVFIADEPTGDLD 178
Cdd:TIGR03269 435 RVALAQVLIKEPRIVILDEPTGTMD 459
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
25-223 |
1.40e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 78.40 E-value: 1.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 25 VENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELgdrQLSELRNRTMGICTQSQSLLASLNA 104
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLL---PLHARARRGIGYLPQEASIFRRLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 105 LDNAILPATLYSKASSETAFTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTEL 184
Cdd:PRK10895 96 YDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVID 175
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 307615102 185 VMRLLAGLPEAGTAVVFATHD-PQALETARTVYEINAGVL 223
Cdd:PRK10895 176 IKRIIEHLRDSGLGVLITDHNvRETLAVCERAYIVSQGHL 215
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
9-209 |
1.45e-17 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 79.56 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 9 KQLTREFIRREKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKP----TSGEVRVAGQNLAELGDRQLSEL 84
Cdd:COG4170 7 RNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSPRERRKI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 85 RNRTMGICTQ--------SQSLLASLN-ALDNAILPATLYSKASseTAFTRALELFEALEIK---HLTEAYPNELSGGEM 152
Cdd:COG4170 87 IGREIAMIFQepsscldpSAKIGDQLIeAIPSWTFKGKWWQRFK--WRKKRAIELLHRVGIKdhkDIMNSYPHELTEGEC 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 307615102 153 RRVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPE-AGTAVVFATHDPQAL 209
Cdd:COG4170 165 QKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESI 222
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
6-206 |
1.77e-17 |
|
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: 77.53 E-value: 1.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 6 IEAKQLTREfiRREKPFnaVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQlselr 85
Cdd:cd03231 1 LEADELTCE--RDGRAL--FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSI----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 86 NRTMGICTQSQSLLASLNALDNAILPATLYSKASSETAFTRA-LELFEALEIkhlteaypNELSGGEMRRVAIARALVNH 164
Cdd:cd03231 72 ARGLLYLGHAPGIKTTLSVLENLRFWHADHSDEQVEEALARVgLNGFEDRPV--------AQLSAGQQRRVALARLLLSG 143
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 307615102 165 PQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATHDP 206
Cdd:cd03231 144 RPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQD 185
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
25-205 |
1.95e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 77.83 E-value: 1.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 25 VENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGdrqlSELRNRTMGICTQSQSLLASlNA 104
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLK----PEIYRQQVSYCAQTPTLFGD-TV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 105 LDNAILPATLYSKASSETAFTRALELFEALEikHLTEAYPNELSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTEL 184
Cdd:PRK10247 98 YDNLIFPWQIRNQQPDPAIFLDDLERFALPD--TILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHN 175
|
170 180
....*....|....*....|..
gi 307615102 185 VMRLLAGL-PEAGTAVVFATHD 205
Cdd:PRK10247 176 VNEIIHRYvREQNIAVLWVTHD 197
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
22-218 |
4.00e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 77.90 E-value: 4.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 22 FNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNL-AELGDRQLSELRNRtMGICTQ-SQSLL 99
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITItHKTKDKYIRPVRKR-IGMVFQfPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 100 ASlNALDNAILPATLYSKASSETAFTRALELFEALEI-KHLTEAYPNELSGGEMRRVAIARALVNHPQVFIADEPTGDLD 178
Cdd:PRK13646 99 FE-DTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFsRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 307615102 179 AQSTELVMRLLAGLP-EAGTAVVFATHDPQalETARTVYEI 218
Cdd:PRK13646 178 PQSKRQVMRLLKSLQtDENKTIILVSHDMN--EVARYADEV 216
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-222 |
4.14e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 77.85 E-value: 4.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 3 ELVIEAKQLtreFIRREKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQnlaELGDRQLS 82
Cdd:PRK13647 2 DNIIEVEDL---HFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGR---EVNAENEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 83 ELRNRtMGICTQS--QSLLASLNALDNAILPATLysKASSETAFTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARA 160
Cdd:PRK13647 76 WVRSK-VGLVFQDpdDQVFSSTVWDDVAFGPVNM--GLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 307615102 161 LVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATHDPQ-ALETARTVYEINAGV 222
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDlAAEWADQVIVLKEGR 215
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-205 |
6.21e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 78.98 E-value: 6.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 1 MSELVIEAKQLTREFIRREKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLkPT------SGEVRVAGQNLA 74
Cdd:PRK15134 1 MTQPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLL-PSppvvypSGDIRFHGESLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 75 ELGDRQLSELRNRTMGICTQSQslLASLNALDNaiLPATLYSKAS------SETAFTRALELFEALEIKHLTE---AYPN 145
Cdd:PRK15134 80 HASEQTLRGVRGNKIAMIFQEP--MVSLNPLHT--LEKQLYEVLSlhrgmrREAARGEILNCLDRVGIRQAAKrltDYPH 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 307615102 146 ELSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLP-EAGTAVVFATHD 205
Cdd:PRK15134 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQqELNMGLLFITHN 216
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-210 |
6.57e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 78.74 E-value: 6.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 2 SELVIEAKQLTREFIRREKPFN-------AVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLA 74
Cdd:PRK10261 310 GEPILQVRNLVTRFPLRSGLLNrvtrevhAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRID 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 75 ELGDRQLSELRNRTMGICTQSQSLLASLNALDNAIL-PATLYSKASSETAFTRALELFE--ALEIKHLTEaYPNELSGGE 151
Cdd:PRK10261 390 TLSPGKLQALRRDIQFIFQDPYASLDPRQTVGDSIMePLRVHGLLPGKAAAARVAWLLErvGLLPEHAWR-YPHEFSGGQ 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 152 MRRVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLP-EAGTAVVFATHDPQALE 210
Cdd:PRK10261 469 RQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQrDFGIAYLFISHDMAVVE 528
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
24-205 |
7.22e-17 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 76.66 E-value: 7.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 24 AVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQlselrnrtmGICTQSQSLLASLN 103
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER---------GVVFQNEGLLPWRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 104 ALDNAILPATLySKASSETAFTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNHPQVFIADEPTGDLDA---- 179
Cdd:PRK11248 87 VQDNVAFGLQL-AGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAftre 165
|
170 180
....*....|....*....|....*.
gi 307615102 180 QSTELVMRLLAglpEAGTAVVFATHD 205
Cdd:PRK11248 166 QMQTLLLKLWQ---ETGKQVLLITHD 188
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-207 |
9.35e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 76.49 E-value: 9.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 5 VIEAKQLTREFIRREkpfnAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLK-----PTSGEVRVAGQNLAELgdr 79
Cdd:PRK14247 3 KIEIRDLKVSFGQVE----VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKM--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 80 QLSELRNRTMGIcTQSQSLLASLNALDNAILPATL----YSKASSETAFTRALE---LFEalEIKHLTEAYPNELSGGEM 152
Cdd:PRK14247 76 DVIELRRRVQMV-FQIPNPIPNLSIFENVALGLKLnrlvKSKKELQERVRWALEkaqLWD--EVKDRLDAPAGKLSGGQQ 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 307615102 153 RRVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTaVVFATHDPQ 207
Cdd:PRK14247 153 QRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMT-IVLVTHFPQ 206
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
24-205 |
1.18e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 76.81 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 24 AVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLaELGDRQLSELRnRTMGICTQSQsllasln 103
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGLMKLR-ESVGMVFQDP------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 104 alDNAILPATLYSKAS---------SETAFTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNHPQVFIADEPT 174
Cdd:PRK13636 92 --DNQLFSASVYQDVSfgavnlklpEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPT 169
|
170 180 190
....*....|....*....|....*....|..
gi 307615102 175 GDLDAQSTELVMRLLAGL-PEAGTAVVFATHD 205
Cdd:PRK13636 170 AGLDPMGVSEIMKLLVEMqKELGLTIIIATHD 201
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
27-213 |
1.47e-16 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 77.06 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 27 NVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNL--AELGDRQLSELRNrtMGICTQSQSLLASLNA 104
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdSARGIFLPPHRRR--IGYVFQEARLFPHLSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 105 LDNaiLpatLY-----SKASSETAFTRALELfeaLEIKHLTEAYPNELSGGEMRRVAIARALVNHPQVFIADEPTGDLDA 179
Cdd:COG4148 95 RGN--L---LYgrkraPRAERRISFDEVVEL---LGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166
|
170 180 190
....*....|....*....|....*....|....*
gi 307615102 180 QSTELVMRLLAGLP-EAGTAVVFATHDPQalETAR 213
Cdd:COG4148 167 ARKAEILPYLERLRdELDIPILYVSHSLD--EVAR 199
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
27-202 |
1.90e-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: 75.34 E-value: 1.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 27 NVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELgdrQLSELRnRTMGICTQSQSLLaslnalD 106
Cdd:cd03253 19 DVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREV---TLDSLR-RAIGVVPQDTVLF------N 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 107 NAILPATLYSK--ASSEtaftralELFEAL-------EIKHLTEAYPNE-------LSGGEMRRVAIARALVNHPQVFIA 170
Cdd:cd03253 89 DTIGYNIRYGRpdATDE-------EVIEAAkaaqihdKIMRFPDGYDTIvgerglkLSGGEKQRVAIARAILKNPPILLL 161
|
170 180 190
....*....|....*....|....*....|..
gi 307615102 171 DEPTGDLDAQSTELVMRLLAGLPEAGTAVVFA 202
Cdd:cd03253 162 DEATSALDTHTEREIQAALRDVSKGRTTIVIA 193
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-221 |
2.22e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 76.80 E-value: 2.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 5 VIEAKQLTREFIRRekpfNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQlsel 84
Cdd:PRK11607 19 LLEIRNLTKSFDGQ----HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 85 rnRTMGICTQSQSLLASLNALDNAILPATLYSKASSETAfTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNH 164
Cdd:PRK11607 91 --RPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIA-SRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 307615102 165 PQVFIADEPTGDLDAQSTE-LVMRLLAGLPEAGTAVVFATHD-PQALETARTVYEINAG 221
Cdd:PRK11607 168 PKLLLLDEPMGALDKKLRDrMQLEVVDILERVGVTCVMVTHDqEEAMTMAGRIAIMNRG 226
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
6-204 |
2.36e-16 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 74.74 E-value: 2.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 6 IEAKQLTREFIRRekpfNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAElgdrqlSELR 85
Cdd:TIGR03740 1 LETKNLSKRFGKQ----TAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTR------KDLH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 86 NrtMGICTQSQSLLASLNALDNAILPATLYSkasseTAFTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNHP 165
Cdd:TIGR03740 71 K--IGSLIESPPLYENLTARENLKVHTTLLG-----LPDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHP 143
|
170 180 190
....*....|....*....|....*....|....*....
gi 307615102 166 QVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATH 204
Cdd:TIGR03740 144 KLLILDEPTNGLDPIGIQELRELIRSFPEQGITVILSSH 182
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
19-210 |
2.42e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 77.17 E-value: 2.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 19 EKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQLSElrnrTMGICTQSQSL 98
Cdd:PRK11160 350 DQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQ----AISVVSQRVHL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 99 L-ASLNalDNAILPAtlySKASSEtaftralELFEALEI----KHLTEAYP---------NELSGGEMRRVAIARALVNH 164
Cdd:PRK11160 426 FsATLR--DNLLLAA---PNASDE-------ALIEVLQQvgleKLLEDDKGlnawlgeggRQLSGGEQRRLGIARALLHD 493
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 307615102 165 PQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTaVVFATHDPQALE 210
Cdd:PRK11160 494 APLLLLDEPTEGLDAETERQILELLAEHAQNKT-VLMITHRLTGLE 538
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6-221 |
2.80e-16 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 73.50 E-value: 2.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 6 IEAKQLTREFIRREKPfnAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDrQLSELr 85
Cdd:cd03247 1 LSINNVSFSYPEQEQQ--VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK-ALSSL- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 86 nrtMGICTQSQSLLAslnaldnailpATLYSKASSetaftralelfealeikhlteaypnELSGGEMRRVAIARALVNHP 165
Cdd:cd03247 77 ---ISVLNQRPYLFD-----------TTLRNNLGR-------------------------RFSGGERQRLALARILLQDA 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 307615102 166 QVFIADEPTGDLDAQSTELVMRLLAGLPEAGTaVVFATHDPQALETARTVYEINAG 221
Cdd:cd03247 118 PIVLLDEPTVGLDPITERQLLSLIFEVLKDKT-LIWITHHLTGIEHMDKILFLENG 172
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-205 |
2.83e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 77.20 E-value: 2.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 2 SELVIEAKQLTREFIRREKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRvAGQNLAELGDRQL 81
Cdd:PRK10261 9 ARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQ-CDKMLLRRRSRQV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 82 SELRnrtmgicTQSQSLLASLNALDNAIL---PAT-----------------LYSKASSETAFTRALELFEALEI---KH 138
Cdd:PRK10261 88 IELS-------EQSAAQMRHVRGADMAMIfqePMTslnpvftvgeqiaesirLHQGASREEAMVEAKRMLDQVRIpeaQT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 307615102 139 LTEAYPNELSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGL-PEAGTAVVFATHD 205
Cdd:PRK10261 161 ILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLqKEMSMGVIFITHD 228
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
5-209 |
3.12e-16 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 75.99 E-value: 3.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 5 VIEAKQLTREFIRREKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKP----TSGEVRVAGQNLAELGDRQ 80
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLRLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 81 LSEL--RNRTMgICTQSQSLLASLNALDNAI---LPATLYsKASSETAF----TRALELFEALEIK---HLTEAYPNELS 148
Cdd:PRK15093 83 RRKLvgHNVSM-IFQEPQSCLDPSERVGRQLmqnIPGWTY-KGRWWQRFgwrkRRAIELLHRVGIKdhkDAMRSFPYELT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 307615102 149 GGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPE-AGTAVVFATHDPQAL 209
Cdd:PRK15093 161 EGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnNNTTILLISHDLQML 222
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
25-179 |
4.27e-16 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 75.91 E-value: 4.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 25 VENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAElgdrqlSELRNRTMGICTQSQSLLASLNA 104
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH------RSIQQRDICMVFQSYALFPHMSL 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 307615102 105 LDNAILPATLYSKASSEtaftRALELFEALEIKHLT---EAYPNELSGGEMRRVAIARALVNHPQVFIADEPTGDLDA 179
Cdd:PRK11432 96 GENVGYGLKMLGVPKEE----RKQRVKEALELVDLAgfeDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDA 169
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-205 |
4.37e-16 |
|
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: 73.77 E-value: 4.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 6 IEAKQLTREFIRREkpfnAVENVNLEIaPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAelgdRQLSELR 85
Cdd:cd03264 1 LQLENLTKRYGKKR----ALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVL----KQPQKLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 86 nRTMGICTQSQSLLASLNALDNAILPATLYSKASSEtaFTRALElfEALEIKHLTEAY---PNELSGGEMRRVAIARALV 162
Cdd:cd03264 72 -RRIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKE--VKARVD--EVLELVNLGDRAkkkIGSLSGGMRRRVGIAQALV 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 307615102 163 NHPQVFIADEPTGDLDAQSTELVMRLLAGLPEaGTAVVFATHD 205
Cdd:cd03264 147 GDPSILIVDEPTAGLDPEERIRFRNLLSELGE-DRIVILSTHI 188
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
24-204 |
8.50e-16 |
|
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: 73.41 E-value: 8.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 24 AVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELgdrQLSELRNRtMGICTQSqSLLASLN 103
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDI---SRKSLRSM-IGVVLQD-TFLFSGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 104 ALDNaILPATLYSKASSETAFTRALELfeALEIKHLTEAY---PNE----LSGGEMRRVAIARALVNHPQVFIADEPTGD 176
Cdd:cd03254 93 IMEN-IRLGRPNATDEEVIEAAKEAGA--HDFIMKLPNGYdtvLGEnggnLSQGERQLLAIARAMLRDPKILILDEATSN 169
|
170 180
....*....|....*....|....*...
gi 307615102 177 LDAQSTELVMRLLAGLPEAGTAVVFATH 204
Cdd:cd03254 170 IDTETEKLIQEALEKLMKGRTSIIIAHR 197
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
23-189 |
8.98e-16 |
|
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: 73.30 E-value: 8.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 23 NAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGdrqLSELRNRtMGICTQsqsllasl 102
Cdd:cd03244 18 PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIG---LHDLRSR-ISIIPQ-------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 103 nalDNAILPATL------YSKASSEtaftralELFEALEIKHLTEAYPNE--------------LSGGEMRRVAIARALV 162
Cdd:cd03244 86 ---DPVLFSGTIrsnldpFGEYSDE-------ELWQALERVGLKEFVESLpggldtvveeggenLSVGQRQLLCLARALL 155
|
170 180
....*....|....*....|....*..
gi 307615102 163 NHPQVFIADEPTGDLDAQSTELVMRLL 189
Cdd:cd03244 156 RKSKILVLDEATASVDPETDALIQKTI 182
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
27-205 |
1.01e-15 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 73.56 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 27 NVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVrvagqnLAelGDRQLSELRN--RTMgicTQSQSLLASLNA 104
Cdd:PRK11247 30 QLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL------LA--GTAPLAEAREdtRLM---FQDARLLPWKKV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 105 LDNAILPATLYSKAssetaftRALELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQsTEL 184
Cdd:PRK11247 99 IDNVGLGLKGQWRD-------AALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDAL-TRI 170
|
170 180
....*....|....*....|...
gi 307615102 185 VMR-LLAGL-PEAGTAVVFATHD 205
Cdd:PRK11247 171 EMQdLIESLwQQHGFTVLLVTHD 193
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
26-215 |
1.02e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 72.60 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 26 ENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGqnlaelGDRQLSELRNRTMGICTQSqSLLASLNAL 105
Cdd:PRK13539 19 SGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG------GDIDDPDVAEACHYLGHRN-AMKPALTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 106 DNAILPATLYskASSETAFTRALELFEALEIKHLTEAYpneLSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELV 185
Cdd:PRK13539 92 ENLEFWAAFL--GGEELDIAAALEAVGLAPLAHLPFGY---LSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALF 166
|
170 180 190
....*....|....*....|....*....|
gi 307615102 186 MRLLAGLPEAGTAVVFATHDPQALETARTV 215
Cdd:PRK13539 167 AELIRAHLAQGGIVIAATHIPLGLPGAREL 196
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
27-202 |
1.19e-15 |
|
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: 72.96 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 27 NVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELgdrQLSELRNRtMGICTQSQSLLaslnalD 106
Cdd:cd03249 21 GLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDL---NLRWLRSQ-IGLVSQEPVLF------D 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 107 NAILPATLYSK--ASSETAfTRALELFEALE-IKHLTEAYPNE-------LSGGEMRRVAIARALVNHPQVFIADEPTGD 176
Cdd:cd03249 91 GTIAENIRYGKpdATDEEV-EEAAKKANIHDfIMSLPDGYDTLvgergsqLSGGQKQRIAIARALLRNPKILLLDEATSA 169
|
170 180
....*....|....*....|....*.
gi 307615102 177 LDAQSTELVMRLLAGLPEAGTAVVFA 202
Cdd:cd03249 170 LDAESEKLVQEALDRAMKGRTTIVIA 195
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
5-205 |
1.52e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 73.27 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 5 VIEAKQLTreFIRREKPfnAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQLSEL 84
Cdd:PRK13548 2 MLEARNLS--VRLGGRT--LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 85 RnrtmGICTQSQSLLASLNALDnaILPATLYSKASSETAFTRALElfEALE---IKHLTE-AYPnELSGGEMRRVAIARA 160
Cdd:PRK13548 78 R----AVLPQHSSLSFPFTVEE--VVAMGRAPHGLSRAEDDALVA--AALAqvdLAHLAGrDYP-QLSGGEQQRVQLARV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 307615102 161 LV------NHPQVFIADEPTGDLDAQSTELVMRLLAGL-PEAGTAVVFATHD 205
Cdd:PRK13548 149 LAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHD 200
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
30-224 |
1.96e-15 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 72.19 E-value: 1.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 30 LEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNlaelgdrqlSELRNRTMGICTQSQSLL---------A 100
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGAS---------PGKGWRHIGYVPQRHEFAwdfpisvahT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 101 SLNALDNAILPATlYSKASSETAFTRALElfeALEIKHLTEAYPNELSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQ 180
Cdd:TIGR03771 72 VMSGRTGHIGWLR-RPCVADFAAVRDALR---RVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMP 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 307615102 181 STELVMRLLAGLPEAGTAVVFATHD-PQALETARTVYEINAGVLS 224
Cdd:TIGR03771 148 TQELLTELFIELAGAGTAILMTTHDlAQAMATCDRVVLLNGRVIA 192
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-204 |
2.33e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 72.74 E-value: 2.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 3 ELVIEAKQLTREFIRREkpfnAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLT---GLLKPTSGEVRVAGQNLAELGD- 78
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQ----ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSgliTGDKSAGSHIELLGRTVQREGRl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 79 -RQLSELRNRTmGICTQSQSLLASLNALDNAILPAtLYSKASSETAFT--------RALELFEALEIKHLTEAYPNELSG 149
Cdd:PRK09984 78 aRDIRKSRANT-GYIFQQFNLVNRLSVLENVLIGA-LGSTPFWRTCFSwftreqkqRALQALTRVGMVHFAHQRVSTLSG 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 307615102 150 GEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPEA-GTAVVFATH 204
Cdd:PRK09984 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLH 211
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
2-204 |
3.13e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 72.81 E-value: 3.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 2 SELVIEAKQLTREFIRREKPFN--AVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDr 79
Cdd:PRK13633 1 MNEMIKCKNVSYKYESNEESTEklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEN- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 80 qLSELRNRTmGICTQS--QSLLASLNALDNAILPATLysKASSETAFTRALELFEALEIKHLTEAYPNELSGGEMRRVAI 157
Cdd:PRK13633 80 -LWDIRNKA-GMVFQNpdNQIVATIVEEDVAFGPENL--GIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAI 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 307615102 158 ARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGL-PEAGTAVVFATH 204
Cdd:PRK13633 156 AGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELnKKYGITIILITH 203
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
24-200 |
3.30e-15 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 73.66 E-value: 3.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 24 AVENVNLEIAPHDLVAIVGRSGNGkttllnlltgllK------------PTSGEVRVAGQNLAELgdrQLSELRNRtMGI 91
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSG------------KstlvnlllrfydPTSGRILIDGVDIRDL---TLESLRRQ-IGV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 92 CTQsQSLLASLNALDNaIlpatLYSKAS-SETAFTRALELFEALE-IKHLTEAYP-------NELSGGEMRRVAIARALV 162
Cdd:COG1132 419 VPQ-DTFLFSGTIREN-I----RYGRPDaTDEEVEEAAKAAQAHEfIEALPDGYDtvvgergVNLSGGQRQRIAIARALL 492
|
170 180 190
....*....|....*....|....*....|....*...
gi 307615102 163 NHPQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVV 200
Cdd:COG1132 493 KDPPILILDEATSALDTETEALIQEALERLMKGRTTIV 530
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-221 |
4.20e-15 |
|
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: 71.42 E-value: 4.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 6 IEAKQLTREFIRREkpfnAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQlselR 85
Cdd:cd03218 1 LRAENLSKRYGKRK----VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK----R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 86 NRtMGIC--TQSQSLLASLNALDN--AILPATLYSKASSETaftRALELFEALEIKHLTEAYPNELSGGEMRRVAIARAL 161
Cdd:cd03218 73 AR-LGIGylPQEASIFRKLTVEENilAVLEIRGLSKKEREE---KLEELLEEFHITHLRKSKASSLSGGERRRVEIARAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 307615102 162 VNHPQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATHD-PQALETARTVYEINAG 221
Cdd:cd03218 149 ATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNvRETLSITDRAYIIYEG 209
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
6-202 |
4.95e-15 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 73.51 E-value: 4.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 6 IEAKQLTREFIRREKPfnAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAelgDRQLSELR 85
Cdd:PRK11176 342 IEFRNVTFTYPGKEVP--ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLR---DYTLASLR 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 86 NRtmgICTQSQSLLASLNALDNAILPAT--LYSKASSETA--FTRALELFEALEIKHLTEAYPN--ELSGGEMRRVAIAR 159
Cdd:PRK11176 417 NQ---VALVSQNVHLFNDTIANNIAYARteQYSREQIEEAarMAYAMDFINKMDNGLDTVIGENgvLLSGGQRQRIAIAR 493
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 307615102 160 ALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFA 202
Cdd:PRK11176 494 ALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIA 536
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
6-223 |
9.09e-15 |
|
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: 72.44 E-value: 9.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 6 IEAKQLTREFIRREKPfnAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELgdrQLSELR 85
Cdd:TIGR02203 331 VEFRNVTFRYPGRDRP--ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADY---TLASLR 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 86 nRTMGICTQSQSLLASLNALDNAILPATLYSKASSETAFTRA--LELFEALEIKHLTEAYPN--ELSGGEMRRVAIARAL 161
Cdd:TIGR02203 406 -RQVALVSQDVVLFNDTIANNIAYGRTEQADRAEIERALAAAyaQDFVDKLPLGLDTPIGENgvLLSGGQRQRLAIARAL 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 307615102 162 VNHPQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFAtHDPQALETARTVYEINAGVL 223
Cdd:TIGR02203 485 LKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIA-HRLSTIEKADRIVVMDDGRI 545
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
12-206 |
1.03e-14 |
|
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: 70.38 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 12 TREFIRREKPFNAVENVNLEIAPHDLVAIVGRSGNGKTT---LLNLLTGLLKPTSGEVRVAGQNLaelgDRQLSElrnRT 88
Cdd:cd03234 10 GLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTlldAISGRVEGGGTTSGQILFNGQPR----KPDQFQ---KC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 89 MGICTQSQSLLASLNALDNAILPATL---YSKASSETAFTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNHP 165
Cdd:cd03234 83 VAYVRQDDILLPGLTVRETLTYTAILrlpRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 307615102 166 QVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATHDP 206
Cdd:cd03234 163 KVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQP 203
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-205 |
1.23e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 71.98 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 3 ELVIEAKQLTrefIRREKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQLs 82
Cdd:COG3845 255 EVVLEVENLS---VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRER- 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 83 elrnRTMGICT-----QSQSLLASLNALDNAILpaTLYSKA--------SSETAFTRALELFEALEIKhlteaYPNE--- 146
Cdd:COG3845 331 ----RRLGVAYipedrLGRGLVPDMSVAENLIL--GRYRRPpfsrggflDRKAIRAFAEELIEEFDVR-----TPGPdtp 399
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 307615102 147 ---LSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATHD 205
Cdd:COG3845 400 arsLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISED 461
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
24-207 |
1.53e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 72.05 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 24 AVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLkPTSGEVRVAGQNLAELGDRQLSELRNRtMGICTQ--SQSLLAS 101
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQLLPVRHR-IQVVFQdpNSSLNPR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 102 LNALDnaILPATLYSKASSETAFTRALELFEALEIKHLTEA----YPNELSGGEMRRVAIARALVNHPQVFIADEPTGDL 177
Cdd:PRK15134 379 LNVLQ--IIEEGLRVHQPTLSAAQREQQVIAVMEEVGLDPEtrhrYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSL 456
|
170 180 190
....*....|....*....|....*....|.
gi 307615102 178 DAQSTELVMRLLAGLPEA-GTAVVFATHDPQ 207
Cdd:PRK15134 457 DKTVQAQILALLKSLQQKhQLAYLFISHDLH 487
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-226 |
1.53e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 70.79 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 2 SELVIEAKQLTREFIRREKPfnAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQnlaELGDRQL 81
Cdd:PRK13632 4 KSVMIKVENVSFSYPNSENN--ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGI---TISKENL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 82 SELRNRtMGICTQSQsllaslnalDNAILPATlyskASSETAF-------------TRALELFEALEIKHLTEAYPNELS 148
Cdd:PRK13632 79 KEIRKK-IGIIFQNP---------DNQFIGAT----VEDDIAFglenkkvppkkmkDIIDDLAKKVGMEDYLDKEPQNLS 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 307615102 149 GGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFA-THDPQALETARTVYEINAGVLSRQ 226
Cdd:PRK13632 145 GGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISiTHDMDEAILADKVIVFSEGKLIAQ 223
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
24-206 |
1.60e-14 |
|
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: 72.01 E-value: 1.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 24 AVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQLSelrnRTMGICTQSQSLLASlN 103
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVR----RRVSVCAQDAHLFDT-T 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 104 ALDNAILPATLYSKASSETAFTRA--LELFEALEIKHLTEAYPN--ELSGGEMRRVAIARALVNHPQVFIADEPTGDLDA 179
Cdd:TIGR02868 425 VRENLRLARPDATDEELWAALERVglADWLRALPDGLDTVLGEGgaRLSGGERQRLALARALLADAPILLLDEPTEHLDA 504
|
170 180
....*....|....*....|....*...
gi 307615102 180 Q-STELVMRLLAGLPeaGTAVVFATHDP 206
Cdd:TIGR02868 505 EtADELLEDLLAALS--GRTVVLITHHL 530
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
24-221 |
1.63e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 70.79 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 24 AVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGdrQLSELRnRTMGICTQ---SQSLLA 100
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFS--KLQGIR-KLVGIVFQnpeTQFVGR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 101 SLN-----ALDNAILPATLYSKassetAFTRALELFEALEIKHLTeayPNELSGGEMRRVAIARALVNHPQVFIADEPTG 175
Cdd:PRK13644 94 TVEedlafGPENLCLPPIEIRK-----RVDRALAEIGLEKYRHRS---PKTLSGGQGQCVALAGILTMEPECLIFDEVTS 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 307615102 176 DLDAQSTELVMRLLAGLPEAGTAVVFATHDPQALETARTVYEINAG 221
Cdd:PRK13644 166 MLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRG 211
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
5-205 |
1.72e-14 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 71.52 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 5 VIEAKQLTREFIRREkpfnAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQlsel 84
Cdd:PRK09452 14 LVELRGISKSFDGKE----VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 85 rnRTMGICTQSQSLLASLNALDNAILPATLYSKASSETAfTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNH 164
Cdd:PRK09452 86 --RHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEIT-PRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNK 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 307615102 165 PQVFIADEPTGDLDAQ-STELVMRLLAGLPEAGTAVVFATHD 205
Cdd:PRK09452 163 PKVLLLDESLSALDYKlRKQMQNELKALQRKLGITFVFVTHD 204
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-204 |
1.87e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 70.60 E-value: 1.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 1 MSELVIEAKQLTREFIRRekpfNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQ 80
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDK----LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 81 lselRNRtMGICTQSQSLLASLNALDNaILPATLYSKASSETAFTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARA 160
Cdd:PRK13537 79 ----RQR-VGVVPQFDNLDPDFTVREN-LLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 307615102 161 LVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATH 204
Cdd:PRK13537 153 LVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTH 196
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
9-204 |
2.03e-14 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 71.97 E-value: 2.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 9 KQLTREFIRREKPfnAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLaelgDRQLSELRnRT 88
Cdd:TIGR01257 932 KNLVKIFEPSGRP--AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI----ETNLDAVR-QS 1004
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 89 MGICTQSQSLLASLNALDNAILPATLYSKASSETaftrALELFEALE---IKHLTEAYPNELSGGEMRRVAIARALVNHP 165
Cdd:TIGR01257 1005 LGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEA----QLEMEAMLEdtgLHHKRNEEAQDLSGGMQRKLSVAIAFVGDA 1080
|
170 180 190
....*....|....*....|....*....|....*....
gi 307615102 166 QVFIADEPTGDLDAQSTELVMRLLAGLpEAGTAVVFATH 204
Cdd:TIGR01257 1081 KVVVLDEPTSGVDPYSRRSIWDLLLKY-RSGRTIIMSTH 1118
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
23-223 |
2.47e-14 |
|
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: 69.42 E-value: 2.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 23 NAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQLselrNRTMGICTQSQSLLAsl 102
Cdd:cd03248 28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYL----HSKVSLVGQEPVLFA-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 103 NALDNAI---LPATLYSKASSETAFTRALELFEALEIKHLTEA--YPNELSGGEMRRVAIARALVNHPQVFIADEPTGDL 177
Cdd:cd03248 102 RSLQDNIaygLQSCSFECVKEAAQKAHAHSFISELASGYDTEVgeKGSQLSGGQKQRVAIARALIRNPQVLILDEATSAL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 307615102 178 DAQSTELVMRLLAGLPEAGTAVVFAtHDPQALETARTVYEINAGVL 223
Cdd:cd03248 182 DAESEQQVQQALYDWPERRTVLVIA-HRLSTVERADQILVLDGGRI 226
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-205 |
2.64e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 70.14 E-value: 2.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 5 VIEAKQLTREFirreKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAElGDRQ---- 80
Cdd:COG4152 1 MLELKGLTKRF----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP-EDRRrigy 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 81 LSELRnrtmgictqsqSLLASLNALDNAILPATL--YSKAsseTAFTRALELFEALEIKHlteaYPN----ELSGGEMRR 154
Cdd:COG4152 76 LPEER-----------GLYPKMKVGEQLVYLARLkgLSKA---EAKRRADEWLERLGLGD----RANkkveELSKGNQQK 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 307615102 155 VAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATHD 205
Cdd:COG4152 138 VQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQ 188
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
5-204 |
2.72e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 68.68 E-value: 2.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 5 VIEAKQLTreFIRREKP-FnavENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQLSE 83
Cdd:PRK13538 1 MLEARNLA--CERDERIlF---SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 84 L-----RNrtmGICTQsqsllasLNALDNAILPATLYSKASSETAFtRALEL-----FEALEIKHLteaypnelSGGEMR 153
Cdd:PRK13538 76 LlylghQP---GIKTE-------LTALENLRFYQRLHGPGDDEALW-EALAQvglagFEDVPVRQL--------SAGQQR 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 307615102 154 RVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATH 204
Cdd:PRK13538 137 RVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTH 187
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
5-221 |
3.20e-14 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 69.23 E-value: 3.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 5 VIEAKQLTREFIRRekpfNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELgdrQLSEL 84
Cdd:TIGR04406 1 TLVAENLIKSYKKR----KVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHL---PMHER 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 85 RNRTMGICTQSQSLLASLNALDNAILPATLYSKASSETAFTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNH 164
Cdd:TIGR04406 74 ARLGIGYLPQEASIFRKLTVEENIMAVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATN 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 307615102 165 PQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATHDPQ-ALETARTVYEINAG 221
Cdd:TIGR04406 154 PKFILLDEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVReTLDICDRAYIISDG 211
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
27-204 |
4.01e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 70.64 E-value: 4.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 27 NVNLEIAPHDLVAIVGRSGNGKttllnlltgllkpTS------------GEVRVAGQNLAELgdrQLSELRnRTMGICTQ 94
Cdd:PRK11174 368 PLNFTLPAGQRIALVGPSGAGK-------------TSllnallgflpyqGSLKINGIELREL---DPESWR-KHLSWVGQ 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 95 SQSLLA-SLnaLDNaILPAtlySKASSETAFTRALELFEALE-IKHLTEAYPNE-------LSGGEMRRVAIARALVNHP 165
Cdd:PRK11174 431 NPQLPHgTL--RDN-VLLG---NPDASDEQLQQALENAWVSEfLPLLPQGLDTPigdqaagLSVGQAQRLALARALLQPC 504
|
170 180 190
....*....|....*....|....*....|....*....
gi 307615102 166 QVFIADEPTGDLDAQSTELVMRLLAGLpEAGTAVVFATH 204
Cdd:PRK11174 505 QLLLLDEPTASLDAHSEQLVMQALNAA-SRRQTTLMVTH 542
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
26-205 |
4.38e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 70.48 E-value: 4.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 26 ENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAgqnlaelgdrqlselRNRTMGICTQSQSLLASLNAL 105
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP---------------KGLRIGYLPQEPPLDDDLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 106 DNAI-----LPATL--YSKASSETAFT-----RALELFEALEIKH----------------LTEAYPN----ELSGGEMR 153
Cdd:COG0488 80 DTVLdgdaeLRALEaeLEELEAKLAEPdedleRLAELQEEFEALGgweaearaeeilsglgFPEEDLDrpvsELSGGWRR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 307615102 154 RVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPeagTAVVFATHD 205
Cdd:COG0488 160 RVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYP---GTVLVVSHD 208
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-204 |
4.85e-14 |
|
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: 67.07 E-value: 4.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 6 IEAKQLTREFirreKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQlselr 85
Cdd:cd03216 1 LELRGITKRF----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 86 nrtmgictqsqsllaslnALDNAIlpATLYskassetaftralelfealeikhlteaypnELSGGEMRRVAIARALVNHP 165
Cdd:cd03216 72 ------------------ARRAGI--AMVY------------------------------QLSVGERQMVEIARALARNA 101
|
170 180 190
....*....|....*....|....*....|....*....
gi 307615102 166 QVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATH 204
Cdd:cd03216 102 RLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISH 140
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
24-205 |
5.05e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 68.86 E-value: 5.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 24 AVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQLSElrnrtMGICTQSQS--LLAS 101
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIAR-----MGVVRTFQHvrLFRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 102 LNALDNAIL-----------------PAtlYSKASSEtAFTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNH 164
Cdd:PRK11300 95 MTVIENLLVaqhqqlktglfsgllktPA--FRRAESE-ALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQ 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 307615102 165 PQVFIADEPTGDLDAQSTELVMRLLAGL-PEAGTAVVFATHD 205
Cdd:PRK11300 172 PEILMLDEPAAGLNPKETKELDELIAELrNEHNVTVLLIEHD 213
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
24-221 |
6.13e-14 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 67.46 E-value: 6.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 24 AVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQnlaELGDRQLSELRNRTMGICT---QSQSLLA 100
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGK---PVTRRSPRDAIRAGIAYVPedrKREGLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 101 SLNALDNAILPATLyskassetaftralelfealeikhlteaypnelSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQ 180
Cdd:cd03215 92 DLSVAENIALSSLL---------------------------------SGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 307615102 181 STELVMRLLAGLPEAGTAVVFATHD-PQALETARTVYEINAG 221
Cdd:cd03215 139 AKAEIYRLIRELADAGKAVLLISSElDELLGLCDRILVMYEG 180
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-223 |
9.41e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 68.33 E-value: 9.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 25 VENVNLEIAPHDLVAIVGRSGNGKTTLLNL-----LTGLLKPTSGEVRVAGQNLAElGDRQLSELRnRTMGICTQSQSLL 99
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrllELNEEARVEGEVRLFGRNIYS-PDVDPIEVR-REVGMVFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 100 ASLNALDNAILPATLYSKASSETAFTRALE-------LFEalEIKHLTEAYPNELSGGEMRRVAIARALVNHPQVFIADE 172
Cdd:PRK14267 98 PHLTIYDNVAIGVKLNGLVKSKKELDERVEwalkkaaLWD--EVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 307615102 173 PTGDLDAQSTELVMRLLAGLPEAGTaVVFATHDP-QALETARTVYEINAGVL 223
Cdd:PRK14267 176 PTANIDPVGTAKIEELLFELKKEYT-IVLVTHSPaQAARVSDYVAFLYLGKL 226
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-205 |
1.12e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 68.12 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 1 MSELVIEAKQLTREFIRREKPfnAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAElgdRQ 80
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDAATY--ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSE---ET 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 81 LSELRnRTMGICTQSQsllaslnalDNAILPATLyskaSSETAFtrALE------------LFEALEIKHLTE---AYPN 145
Cdd:PRK13635 76 VWDVR-RQVGMVFQNP---------DNQFVGATV----QDDVAF--GLEnigvpreemverVDQALRQVGMEDflnREPH 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 307615102 146 ELSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFA-THD 205
Cdd:PRK13635 140 RLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSiTHD 200
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
9-205 |
1.36e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 67.80 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 9 KQLTREFIRREKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKP----TSGEVRVAGQNLAelgdrqLSEL 84
Cdd:PRK10418 3 QQIELRNIALQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVA------PCAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 85 RNRTmgICTQSQSLLASLNAL----DNAILPATLYSKASSETAFTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARA 160
Cdd:PRK10418 77 RGRK--IATIMQNPRSAFNPLhtmhTHARETCLALGKPADDATLTAALEAVGLENAARVLKLYPFEMSGGMLQRMMIALA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 307615102 161 LVNHPQVFIADEPTGDLDAQSTELVMRLLAGL-PEAGTAVVFATHD 205
Cdd:PRK10418 155 LLCEAPFIIADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHD 200
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
24-216 |
1.76e-13 |
|
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: 66.93 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 24 AVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAelgdRQLSELRNRtMGI--CTQSQSLLAS 101
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDIT----GLPPHRIAR-LGIgyVPEGRRIFPS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 102 LNALDNAILPA-TLYSKASSETAFTRALELFEALEIKHLTEAypNELSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQ 180
Cdd:COG0410 93 LTVEENLLLGAyARRDRAEVRADLERVYELFPRLKERRRQRA--GTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPL 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 307615102 181 STELVMRLLAGLPEAGTAVVFATHD-PQALETARTVY 216
Cdd:COG0410 171 IVEEIFEIIRRLNREGVTILLVEQNaRFALEIADRAY 207
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
16-218 |
2.52e-13 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 68.60 E-value: 2.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 16 IRREKPFnaVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQLselrNRTMGICTQs 95
Cdd:TIGR00958 490 NRPDVPV--LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYL----HRQVALVGQ- 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 96 QSLLASLNALDNAILPATLYSKASSETAftrALELFEALEIKHLTEAYPNE-------LSGGEMRRVAIARALVNHPQVF 168
Cdd:TIGR00958 563 EPVLFSGSVRENIAYGLTDTPDEEIMAA---AKAANAHDFIMEFPNGYDTEvgekgsqLSGGQKQRIAIARALVRKPRVL 639
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 307615102 169 IADEPTGDLDAQSTelvmRLLAGLPEAG--TAVVFAthdpQALETARTVYEI 218
Cdd:TIGR00958 640 ILDEATSALDAECE----QLLQESRSRAsrTVLLIA----HRLSTVERADQI 683
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
22-221 |
2.67e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 67.34 E-value: 2.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 22 FNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVrVAGQNLAELGDRQLSELRN--RTMGICTQSQSLL 99
Cdd:PRK13645 24 FKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQT-IVGDYAIPANLKKIKEVKRlrKEIGLVFQFPEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 100 ASLNALDNAILPATLYSKASSETAFTRALELfeaLEIKHLTEAY----PNELSGGEMRRVAIARALVNHPQVFIADEPTG 175
Cdd:PRK13645 103 LFQETIEKDIAFGPVNLGENKQEAYKKVPEL---LKLVQLPEDYvkrsPFELSGGQKRRVALAGIIAMDGNTLVLDEPTG 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 307615102 176 DLDAQSTELVMRLLAGL-PEAGTAVVFATHD-PQALETARTVYEINAG 221
Cdd:PRK13645 180 GLDPKGEEDFINLFERLnKEYKKRIIMVTHNmDQVLRIADEVIVMHEG 227
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
17-202 |
2.71e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 68.21 E-value: 2.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 17 RREKPfnAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDrqlSELRNrtmGICTQSQ 96
Cdd:PRK10790 351 RDDNL--VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSH---SVLRQ---GVAMVQQ 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 97 sllaslnalDNAILPATLYSKAS-----SETAFTRALelfEALEIKHLTEAYP-----------NELSGGEMRRVAIARA 160
Cdd:PRK10790 423 ---------DPVVLADTFLANVTlgrdiSEEQVWQAL---ETVQLAELARSLPdglytplgeqgNNLSVGQKQLLALARV 490
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 307615102 161 LVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFA 202
Cdd:PRK10790 491 LVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIA 532
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
25-212 |
3.31e-13 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 65.97 E-value: 3.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 25 VENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKP---TSGEVRVAGQNLAELGDRQlselrnRTMGICTQSQSLLAS 101
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQ------RRIGILFQDDLLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 102 LNALDNAI--LPATLYSKASSEtaftRALELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNHPQVFIADEPTGDLDA 179
Cdd:COG4136 91 LSVGENLAfaLPPTIGRAQRRA----RVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDA 166
|
170 180 190
....*....|....*....|....*....|....
gi 307615102 180 QSTELVMRL-LAGLPEAGTAVVFATHDPQALETA 212
Cdd:COG4136 167 ALRAQFREFvFEQIRQRGIPALLVTHDEEDAPAA 200
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-204 |
3.81e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.89 E-value: 3.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 1 MSELVIEAKQLTREFirreKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQ 80
Cdd:PRK09700 1 MATPYISMAGIGKSF----GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 81 LSELrnrTMGICTQSQSLLASLNALDNAIL-----------PATLYSKASSetaftRALELFEALEIKHLTEAYPNELSG 149
Cdd:PRK09700 77 AAQL---GIGIIYQELSVIDELTVLENLYIgrhltkkvcgvNIIDWREMRV-----RAAMMLLRVGLKVDLDEKVANLSI 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 307615102 150 GEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATH 204
Cdd:PRK09700 149 SHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISH 203
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-205 |
4.47e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 67.07 E-value: 4.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 1 MSELVIEakQLTREFIRREKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLL----KPTSGEVRVAGQNLAEL 76
Cdd:PRK11022 1 MALLNVD--KLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQDLQRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 77 GDRQLSELRNRTMGICTQSQslLASLN---ALDNAILPA-TLYSKASSETAFTRALELFEALEIKHLT---EAYPNELSG 149
Cdd:PRK11022 79 SEKERRNLVGAEVAMIFQDP--MTSLNpcyTVGFQIMEAiKVHQGGNKKTRRQRAIDLLNQVGIPDPAsrlDVYPHQLSG 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 150 GEMRRVAIARALVNHPQVFIADEPTGDLD----AQSTELVMRLLAglpEAGTAVVFATHD 205
Cdd:PRK11022 157 GMSQRVMIAMAIACRPKLLIADEPTTALDvtiqAQIIELLLELQQ---KENMALVLITHD 213
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
24-187 |
4.68e-13 |
|
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: 65.51 E-value: 4.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 24 AVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGdrqLSELRNRtMGICTQSQSLLASln 103
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIP---LEDLRSS-LTIIPQDPTLFSG-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 104 ALDNAILPATLYSKAssetaftralELFEALEIKhltEAYPNeLSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTE 183
Cdd:cd03369 97 TIRSNLDPFDEYSDE----------EIYGALRVS---EGGLN-LSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDA 162
|
....
gi 307615102 184 LVMR 187
Cdd:cd03369 163 LIQK 166
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
6-207 |
6.28e-13 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 65.55 E-value: 6.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 6 IEAKQLTreFIRREKPFNAvenvNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAEL--GDRQLSE 83
Cdd:COG3840 2 LRLDDLT--YRYGDFPLRF----DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALppAERPVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 84 LrnrtmgicTQSQSLLASLNALDN---AILPATLYSKASSEtaftralELFEALE---IKHLTEAYPNELSGGEMRRVAI 157
Cdd:COG3840 76 L--------FQENNLFPHLTVAQNiglGLRPGLKLTAEQRA-------QVEQALErvgLAGLLDRLPGQLSGGQRQRVAL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 307615102 158 ARALVNHPQVFIADEPTGDLD-AQSTELvMRLLAGL-PEAGTAVVFATHDPQ 207
Cdd:COG3840 141 ARCLVRKRPILLLDEPFSALDpALRQEM-LDLVDELcRERGLTVLMVTHDPE 191
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-223 |
9.87e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 66.63 E-value: 9.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 4 LVIEAKQLTREFirREKPFnaVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVaGQNLaelgdrqlse 83
Cdd:COG0488 314 KVLELEGLSKSY--GDKTL--LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV---------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 84 lrnrTMGICTQSQSLL-ASLNALDNaILPatlYSKASSETAFTRALE--LFEALEIkhltEAYPNELSGGEMRRVAIARA 160
Cdd:COG0488 379 ----KIGYFDQHQEELdPDKTVLDE-LRD---GAPGGTEQEVRGYLGrfLFSGDDA----FKPVGVLSGGEKARLALAKL 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 307615102 161 LVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPeaGTaVVFATHDPQALE-TARTVYEINAGVL 223
Cdd:COG0488 447 LLSPPNVLLLDEPTNHLDIETLEALEEALDDFP--GT-VLLVSHDRYFLDrVATRILEFEDGGV 507
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-204 |
1.64e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 65.62 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 1 MSELVIEAKQLTREFirREKPfnAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGqnlAELGDRq 80
Cdd:PRK13536 37 MSTVAIDLAGVSKSY--GDKA--VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG---VPVPAR- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 81 lSELRNRTMGICTQSQSLLASLNALDNAILPATLY--SKASSETAFTRALElFEALEIKhlTEAYPNELSGGEMRRVAIA 158
Cdd:PRK13536 109 -ARLARARIGVVPQFDNLDLEFTVRENLLVFGRYFgmSTREIEAVIPSLLE-FARLESK--ADARVSDLSGGMKRRLTLA 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 307615102 159 RALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATH 204
Cdd:PRK13536 185 RALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTH 230
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
5-223 |
1.66e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 65.26 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 5 VIEAKQLTREF-IRREKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRV----AGQNLAELGD- 78
Cdd:PRK13631 21 ILRVKNLYCVFdEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyIGDKKNNHELi 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 79 --------RQLSELRnRTMGICTQSQSLLASLNALDNAILPATLYSKASSETAFTRALELFEALEIKH-LTEAYPNELSG 149
Cdd:PRK13631 101 tnpyskkiKNFKELR-RRVSMVFQFPEYQLFKDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDsYLERSPFGLSG 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 307615102 150 GEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATHD-PQALETARTVYEINAGVL 223
Cdd:PRK13631 180 GQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTmEHVLEVADEVIVMDKGKI 254
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
22-205 |
4.85e-12 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 64.09 E-value: 4.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 22 FNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELgdrqlsELRNRTMGICTQSQSLLAS 101
Cdd:PRK11650 17 TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNEL------EPADRDIAMVFQNYALYPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 102 LN-------ALDNAILPATLYSKASSETAftRALELFEALEIKhlteayPNELSGGEMRRVAIARALVNHPQVFIADEPT 174
Cdd:PRK11650 91 MSvrenmayGLKIRGMPKAEIEERVAEAA--RILELEPLLDRK------PRELSGGQRQRVAMGRAIVREPAVFLFDEPL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 307615102 175 GDLDA----QstelvMRL--------LaglpeaGTAVVFATHD 205
Cdd:PRK11650 163 SNLDAklrvQ-----MRLeiqrlhrrL------KTTSLYVTHD 194
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
30-221 |
4.90e-12 |
|
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: 62.90 E-value: 4.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 30 LEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNL--AELGDRQLSELrnrtmgicTQSQSLLASLNALDN 107
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVtaAPPADRPVSML--------FQENNLFAHLTVEQN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 108 AILPAT--LYSKASSETAFTRALelfEALEIKHLTEAYPNELSGGEMRRVAIARALVNHPQVFIADEPTGDLD----AQS 181
Cdd:cd03298 91 VGLGLSpgLKLTAEDRQAIEVAL---ARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDpalrAEM 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 307615102 182 TELVMRLLAglpEAGTAVVFATHDPQ-ALETARTVYEINAG 221
Cdd:cd03298 168 LDLVLDLHA---ETKMTVLMVTHQPEdAKRLAQRVVFLDNG 205
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-205 |
4.99e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 63.95 E-value: 4.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 5 VIEAKQLTREFIRREKPF-----------------NAVENVNLEIAPHDLVAIVGRSGNGKTTLLnlltgllK------- 60
Cdd:COG4586 1 IIEVENLSKTYRVYEKEPglkgalkglfrreyrevEAVDDISFTIEPGEIVGFIGPNGAGKSTTI-------Kmltgilv 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 61 PTSGEVRVAGQNLAElgdRQLSELRNRT--MGictQSQSLLASLNALDNAILPATLYSkaSSETAFTRAL-ELFEALEIK 137
Cdd:COG4586 74 PTSGEVRVLGYVPFK---RRKEFARRIGvvFG---QRSQLWWDLPAIDSFRLLKAIYR--IPDAEYKKRLdELVELLDLG 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 307615102 138 HLTEAYPNELSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGL-PEAGTAVVFATHD 205
Cdd:COG4586 146 ELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLTSHD 214
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
136-221 |
5.69e-12 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 61.31 E-value: 5.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 136 IKHLTEAYPNELSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPeaGTaVVFATHDPQAL-ETART 214
Cdd:cd03221 60 GSTVKIGYFEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYP--GT-VILVSHDRYFLdQVATK 136
|
....*..
gi 307615102 215 VYEINAG 221
Cdd:cd03221 137 IIELEDG 143
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
3-203 |
6.56e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 63.27 E-value: 6.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 3 ELVIEAKQLTREFIRREKPF-----NAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLaELG 77
Cdd:PRK15112 2 ETLLEVRNLSKTFRYRTGWFrrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-HFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 78 DRQLSELRNRTMgictqSQSLLASLNA-------LDnaiLPATLYSKASSEtafTRALELFEALEIKHL----TEAYPNE 146
Cdd:PRK15112 81 DYSYRSQRIRMI-----FQDPSTSLNPrqrisqiLD---FPLRLNTDLEPE---QREKQIIETLRQVGLlpdhASYYPHM 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 307615102 147 LSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPEA-GTAVVFAT 203
Cdd:PRK15112 150 LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVT 207
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-213 |
8.82e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 62.64 E-value: 8.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 1 MSELVIEAKQLTREFIRRekpfNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQ 80
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPR----KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 81 LSELRNRTM-----GICTQS--QSLLASLNALDNA-----ILPATLYSKASSEtaftrALELFEALEI--KHLTEAyPNE 146
Cdd:PRK11701 78 LSEAERRRLlrtewGFVHQHprDGLRMQVSAGGNIgerlmAVGARHYGDIRAT-----AGDWLERVEIdaARIDDL-PTT 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 307615102 147 LSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGL-PEAGTAVVFATHDpqaLETAR 213
Cdd:PRK11701 152 FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHD---LAVAR 216
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
147-212 |
9.03e-12 |
|
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: 63.61 E-value: 9.03e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 307615102 147 LSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATHDPQALETA 212
Cdd:COG4618 468 LSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAAV 533
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
25-205 |
1.43e-11 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 61.95 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 25 VENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQLSelrnRTMGICTQSQ-------- 96
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA----RRLALLPQHHltpegitv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 97 ------------SLLASLNALDNAILpatlyskassetafTRALelfEALEIKHLTEAYPNELSGGEMRRVAIARALVNH 164
Cdd:PRK11231 94 relvaygrspwlSLWGRLSAEDNARV--------------NQAM---EQTRINHLADRRLTDLSGGQRQRAFLAMVLAQD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 307615102 165 PQVFIADEPTGDLD-AQSTELvMRLLAGLPEAGTAVVFATHD 205
Cdd:PRK11231 157 TPVVLLDEPTTYLDiNHQVEL-MRLMRELNTQGKTVVTVLHD 197
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
27-178 |
1.83e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 62.58 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 27 NVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRvagqnlaeLGDRQLSELRN--------RTMGICTQSQSL 98
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIV--------LNGRVLFDAEKgiclppekRRIGYVFQDARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 99 LASLNALDNailpaTLYSKASSETA-FTRALELfeaLEIKHLTEAYPNELSGGEMRRVAIARALVNHPQVFIADEPTGDL 177
Cdd:PRK11144 88 FPHYKVRGN-----LRYGMAKSMVAqFDKIVAL---LGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASL 159
|
.
gi 307615102 178 D 178
Cdd:PRK11144 160 D 160
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-204 |
3.08e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 61.96 E-value: 3.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 2 SELVIEAKQLTREF--IRrekpfnAVENVNLEIAPHDLVAIVGRSGNGKttllnlltgllKPTSGEVRVAGQNLAELGDR 79
Cdd:COG1129 1 AEPLLEMRGISKSFggVK------ALDGVSLELRPGEVHALLGENGAGKstlmkilsgvyQPDSGEILLDGEPVRFRSPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 80 QLSELrnrtmGICT--QSQSLLASLNALDNaILPATLYSKA---SSETAFTRALELFEALEIKHLTEAYPNELSGGEMRR 154
Cdd:COG1129 75 DAQAA-----GIAIihQELNLVPNLSVAEN-IFLGREPRRGgliDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 307615102 155 VAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATH 204
Cdd:COG1129 149 VEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISH 198
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
25-205 |
4.10e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 61.78 E-value: 4.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 25 VENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQLSELrnrtmgICTQSQSLLASLNA 104
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRR------VASVPQDTSLSFEF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 105 LDNAILPA------TLYSKASS--ETAFTRALElfeALEIKHLTEAYPNELSGGEMRRVAIARALVNHPQVFIADEPTGD 176
Cdd:PRK09536 93 DVRQVVEMgrtphrSRFDTWTEtdRAAVERAME---RTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTAS 169
|
170 180
....*....|....*....|....*....
gi 307615102 177 LDAQSTELVMRLLAGLPEAGTAVVFATHD 205
Cdd:PRK09536 170 LDINHQVRTLELVRRLVDDGKTAVAAIHD 198
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-210 |
4.87e-11 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 61.95 E-value: 4.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 5 VIEAKQLTREFIRREKPfnAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAElgdrQLSEL 84
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSSP--AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT----NISDV 2010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 85 rNRTMGICTQSQSLLASLNALDNAILPATLYSKASSETAFTRALELfEALEIKHLTEAYPNELSGGEMRRVAIARALVNH 164
Cdd:TIGR01257 2011 -HQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSI-QSLGLSLYADRLAGTYSGGNKRKLSTAIALIGC 2088
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 307615102 165 PQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATHDPQALE 210
Cdd:TIGR01257 2089 PPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECE 2134
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
24-202 |
4.89e-11 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 61.52 E-value: 4.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 24 AVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGdrqLSELRnRTMGICTQSQSLLASLN 103
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT---RASLR-RNIAVVFQDAGLFNRSI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 104 AlDNAILPATLYSKASSETAFTR--ALELFEALEIKHLTEA--YPNELSGGEMRRVAIARALVNHPQVFIADEPTGDLDA 179
Cdd:PRK13657 426 E-DNIRVGRPDATDEEMRAAAERaqAHDFIERKPDGYDTVVgeRGRQLSGGERQRLAIARALLKDPPILILDEATSALDV 504
|
170 180
....*....|....*....|...
gi 307615102 180 QSTELVMRLLAGLPEAGTAVVFA 202
Cdd:PRK13657 505 ETEAKVKAALDELMKGRTTFIIA 527
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
5-173 |
6.95e-11 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 60.04 E-value: 6.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 5 VIEAKQLTREFIRREkpfnAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNL--------AEL 76
Cdd:COG1137 3 TLEAENLVKSYGKRT----VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIthlpmhkrARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 77 GdrqlselrnrtMGICTQSQSLLASLNALDN--AILPATLYSKASSETaftRALELFEALEIKHLTEAYPNELSGGEMRR 154
Cdd:COG1137 79 G-----------IGYLPQEASIFRKLTVEDNilAVLELRKLSKKEREE---RLEELLEEFGITHLRKSKAYSLSGGERRR 144
|
170
....*....|....*....
gi 307615102 155 VAIARALVNHPQVFIADEP 173
Cdd:COG1137 145 VEIARALATNPKFILLDEP 163
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
129-205 |
8.71e-11 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 59.69 E-value: 8.71e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 307615102 129 ELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATHD 205
Cdd:cd03236 122 ELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHD 198
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-207 |
8.82e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 60.05 E-value: 8.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 25 VENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKpTSGEVRVAG------QNLAElgdRQLSELRNRTMGICTQSQSL 98
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGrveffnQNIYE---RRVNLNRLRRQVSMVHPKPN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 99 LASLNALDNAILPATLYS-------KASSETAFtRALELFEalEIKHLTEAYPNELSGGEMRRVAIARALVNHPQVFIAD 171
Cdd:PRK14258 99 LFPMSVYDNVAYGVKIVGwrpkleiDDIVESAL-KDADLWD--EIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMD 175
|
170 180 190
....*....|....*....|....*....|....*...
gi 307615102 172 EPTGDLDAQSTELVMRLLAGLP-EAGTAVVFATHD-PQ 207
Cdd:PRK14258 176 EPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNlHQ 213
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
27-216 |
1.11e-10 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 60.45 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 27 NVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKP---TSGEVRVAGQNLaelgdrQLSELRNRTmGICTQSQSLLASLN 103
Cdd:TIGR00955 43 NVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPI------DAKEMRAIS-AYVQQDDLFIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 104 ALDNAILPATLYSKA--SSETAFTRALELFEALEIK---HLTEAYPNE---LSGGEMRRVAIARALVNHPQVFIADEPTG 175
Cdd:TIGR00955 116 VREHLMFQAHLRMPRrvTKKEKRERVDEVLQALGLRkcaNTRIGVPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 307615102 176 DLDAQSTELVMRLLAGLPEAGTAVVFATHDPQA-----------LETARTVY 216
Cdd:TIGR00955 196 GLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSelfelfdkiilMAEGRVAY 247
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
28-226 |
1.43e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 59.18 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 28 VNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLkPTSGEVRVAGQNLAELGDRQLSELRnrtmGICTQSQSLLaslnaldn 107
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHR----AYLSQQQTPP-------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 108 AILPA----TLYSKASSETAFTRAL--ELFEALEIKHLTEAYPNELSGGEMRRVAIA-------RALVNHPQVFIADEPT 174
Cdd:PRK03695 82 FAMPVfqylTLHQPDKTRTEAVASAlnEVAEALGLDDKLGRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPM 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 307615102 175 GDLD-AQSTELvMRLLAGLPEAGTAVVFATHD-PQALETARTVYEINAGVLSRQ 226
Cdd:PRK03695 162 NSLDvAQQAAL-DRLLSELCQQGIAVVMSSHDlNHTLRHADRVWLLKQGKLLAS 214
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-226 |
2.06e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 59.04 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 1 MSELVIEAKQLTREFIRREKPfnAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQ 80
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPDSKKP--ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 81 LSELRNRtMGICTQSQsllaslnalDNAILPATLyskaSSETAF---TRALELFEALEIKH----------LTEAYPNEL 147
Cdd:PRK13640 79 VWDIREK-VGIVFQNP---------DNQFVGATV----GDDVAFgleNRAVPRPEMIKIVRdvladvgmldYIDSEPANL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 148 SGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFA-THDPQALETARTVYEINAGVLSRQ 226
Cdd:PRK13640 145 SGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISiTHDIDEANMADQVLVLDDGKLLAQ 224
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
145-205 |
2.44e-10 |
|
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: 59.56 E-value: 2.44e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 307615102 145 NELSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPeaGTaVVFATHD 205
Cdd:TIGR03719 160 TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYP--GT-VVAVTHD 217
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
25-221 |
2.46e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 58.87 E-value: 2.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 25 VENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLaELGDRQLSELRNRTMGICTQSQSLLASLNa 104
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRGLLALRQQVATVFQDPEQQIFYTD- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 105 LDNAIlPATLYSKASSETAFTR----ALELFEALEIKHlteaYPNE-LSGGEMRRVAIARALVNHPQVFIADEPTGDLDA 179
Cdd:PRK13638 95 IDSDI-AFSLRNLGVPEAEITRrvdeALTLVDAQHFRH----QPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 307615102 180 QSTELVMRLLAGLPEAGTAVVFATHDPQAL-ETARTVYEINAG 221
Cdd:PRK13638 170 AGRTQMIAIIRRIVAQGNHVIISSHDIDLIyEISDAVYVLRQG 212
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
142-206 |
2.64e-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: 2.64e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 307615102 142 AYP--NELSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAglpEAGTAVVFATHDP 206
Cdd:cd03223 85 IYPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLK---ELGITVISVGHRP 148
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
29-200 |
3.53e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.87 E-value: 3.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 29 NLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQLSEL------RNRTMGIctqsqsllaSL 102
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLvsdewqRNNTDML---------SP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 103 NALDNAILPATLYSKASSETAftRALELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQST 182
Cdd:PRK10938 94 GEDDTGRTTAEIIQDEVKDPA--RCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASR 171
|
170
....*....|....*...
gi 307615102 183 ELVMRLLAGLPEAGTAVV 200
Cdd:PRK10938 172 QQLAELLASLHQSGITLV 189
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
24-204 |
5.66e-10 |
|
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: 58.30 E-value: 5.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 24 AVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLK--PTSGEVRVAGQnlaELGDRQLSELRNRTMGICTQSQSLLAS 101
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGS---PLKASNIRDTERAGIVIIHQELTLVPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 102 LNALDNAIL--PATLYSKASSETAFT-RALELFEALEIKHLTEAYP-NELSGGEMRRVAIARALVNHPQVFIADEPTGDL 177
Cdd:TIGR02633 93 LSVAENIFLgnEITLPGGRMAYNAMYlRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQARLLILDEPSSSL 172
|
170 180
....*....|....*....|....*..
gi 307615102 178 DAQSTELVMRLLAGLPEAGTAVVFATH 204
Cdd:TIGR02633 173 TEKETEILLDIIRDLKAHGVACVYISH 199
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-205 |
5.91e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 57.45 E-value: 5.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 1 MSELVIEAKQLTREFiRREKPFnAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVagQNLAeLGDRQ 80
Cdd:PRK13648 3 DKNSIIVFKNVSFQY-QSDASF-TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFY--NNQA-ITDDN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 81 LSELRnRTMGICTQS--QSLLASLNA------LDNAILPatlYSKASSETAftralELFEALEIKHLTEAYPNELSGGEM 152
Cdd:PRK13648 78 FEKLR-KHIGIVFQNpdNQFVGSIVKydvafgLENHAVP---YDEMHRRVS-----EALKQVDMLERADYEPNALSGGQK 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 307615102 153 RRVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFA-THD 205
Cdd:PRK13648 149 QRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISiTHD 202
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
32-208 |
6.61e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 58.35 E-value: 6.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 32 IAPHDLVAIVGRSGNGKTTLLNLLTGllkptsgevRVAGQNLAE---LGDRQLSELRNRTMGICTQSQSLLASLNALDNA 108
Cdd:PLN03211 91 ASPGEILAVLGPSGSGKSTLLNALAG---------RIQGNNFTGtilANNRKPTKQILKRTGFVTQDDILYPHLTVRETL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 109 I------LPATLYSKASSETAFTRALEL-FEALEIKHLTEAYPNELSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQS 181
Cdd:PLN03211 162 VfcsllrLPKSLTKQEKILVAESVISELgLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATA 241
|
170 180
....*....|....*....|....*..
gi 307615102 182 TELVMRLLAGLPEAGTAVVFATHDPQA 208
Cdd:PLN03211 242 AYRLVLTLGSLAQKGKTIVTSMHQPSS 268
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
27-181 |
7.42e-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: 58.29 E-value: 7.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 27 NVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELgdRQLSeLRnRTMGICTQsqsllaslnalD 106
Cdd:COG5265 376 GVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDV--TQAS-LR-AAIGIVPQ-----------D 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 107 NAILPATLY----------SKASSETAFTRA-LELFealeIKHLTEAYPNE-------LSGGEMRRVAIARALVNHPQVF 168
Cdd:COG5265 441 TVLFNDTIAyniaygrpdaSEEEVEAAARAAqIHDF----IESLPDGYDTRvgerglkLSGGEKQRVAIARTLLKNPPIL 516
|
170
....*....|...
gi 307615102 169 IADEPTGDLDAQS 181
Cdd:COG5265 517 IFDEATSALDSRT 529
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
27-174 |
9.10e-10 |
|
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: 56.76 E-value: 9.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 27 NVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLaelgDRQLSELR-NRTMGICTQSQSLLASLNAL 105
Cdd:TIGR03410 18 GVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDI----TKLPPHERaRAGIAYVPQGREIFPRLTVE 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 106 DNAILPATLYSKASSETAfTRALELFEAL-EIKHLTEAypnELSGGEMRRVAIARALVNHPQVFIADEPT 174
Cdd:TIGR03410 94 ENLLTGLAALPRRSRKIP-DEIYELFPVLkEMLGRRGG---DLSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
19-180 |
1.23e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 57.83 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 19 EKPfnAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGdrQLSELRNRTMgictqsqsl 98
Cdd:PLN03130 629 ERP--TLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVIRGTVAYVP--QVSWIFNATV--------- 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 99 laSLNALDNAILPATLYSKASSETAFTRALELFEALEIKHLTEAYPNeLSGGEMRRVAIARALVNHPQVFIADEPTGDLD 178
Cdd:PLN03130 696 --RDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
..
gi 307615102 179 AQ 180
Cdd:PLN03130 773 AH 774
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
22-207 |
1.29e-09 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 56.58 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 22 FNAVENVNLEIAPHDLVAIVGRSGNGKTtllnlltgllkpT-----------------SGEVRVAGQNLAElGDRQLSEL 84
Cdd:COG1117 24 KQALKDINLDIPENKVTALIGPSGCGKS------------TllrclnrmndlipgarvEGEILLDGEDIYD-PDVDVVEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 85 RnRTMGICTQSqsllasLNAL-----DNAILPATLYSKASS-------ETAFTRAlelfeAL--EIKHLTEAYPNELSGG 150
Cdd:COG1117 91 R-RRVGMVFQK------PNPFpksiyDNVAYGLRLHGIKSKseldeivEESLRKA-----ALwdEVKDRLKKSALGLSGG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 307615102 151 EMRRVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTaVVFATHDPQ 207
Cdd:COG1117 159 QQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYT-IVIVTHNMQ 214
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
138-205 |
1.49e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 56.28 E-value: 1.49e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 307615102 138 HLTEAYPNELSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGL-PEAGTAVVFATHD 205
Cdd:PRK09544 112 HLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLrRELDCAVLMVSHD 180
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-203 |
1.52e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 56.95 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 3 ELVIEAKQLTREfirrekpfNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQnlaelgdrqls 82
Cdd:COG1129 254 EVVLEVEGLSVG--------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGK----------- 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 83 ELRNRT--------MGICT---QSQSLLASLNALDNAILPA-TLYSKA---SSETAFTRALELFEALEIKHLTEAYP-NE 146
Cdd:COG1129 315 PVRIRSprdairagIAYVPedrKGEGLVLDLSIRENITLASlDRLSRGgllDRRRERALAEEYIKRLRIKTPSPEQPvGN 394
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 307615102 147 LSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFAT 203
Cdd:COG1129 395 LSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVIS 451
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
120-206 |
1.52e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 57.12 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 120 SETAFTRAlELFEALE-------IKHLTEAYP--NELSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLA 190
Cdd:COG4178 451 TAEAFSDA-ELREALEavglghlAERLDEEADwdQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLR 529
|
90
....*....|....*..
gi 307615102 191 G-LPeaGTAVVFATHDP 206
Cdd:COG4178 530 EeLP--GTTVISVGHRS 544
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-207 |
1.66e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 56.21 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 25 VENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGD-RQLSELRNRT-MGICTQSQSLLASL 102
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDiFQIDAIKLRKeVGMVFQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 103 NALDNAILPatLYSKASSETAFTRALeLFEAL-------EIKHLTEAYPNELSGGEMRRVAIARALVNHPQVFIADEPTG 175
Cdd:PRK14246 106 SIYDNIAYP--LKSHGIKEKREIKKI-VEECLrkvglwkEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190
....*....|....*....|....*....|..
gi 307615102 176 DLDAQSTELVMRLLAGLPEAgTAVVFATHDPQ 207
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNE-IAIVIVSHNPQ 213
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
17-206 |
2.44e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 55.35 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 17 RREKPFNAVENVNLEIAPHDLVAIVGRSGNGKTT--LLNLLTGLLKPTSGEVrvagqnlaELGDRQLSElrnrtmgictq 94
Cdd:COG2401 38 LRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTllRLLAGALKGTPVAGCV--------DVPDNQFGR----------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 95 sqsllaslnalDNAILPAtLYSKASSETAftralelFEALEIKHLTEAY-----PNELSGGEMRRVAIARALVNHPQVFI 169
Cdd:COG2401 99 -----------EASLIDA-IGRKGDFKDA-------VELLNAVGLSDAVlwlrrFKELSTGQKFRFRLALLLAERPKLLV 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 307615102 170 ADEPTGDLDAQSTELVMRLLAGLP-EAGTAVVFATHDP 206
Cdd:COG2401 160 IDEFCSHLDRQTAKRVARNLQKLArRAGITLVVATHHY 197
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
147-205 |
2.73e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.28 E-value: 2.73e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 307615102 147 LSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPeaGTaVVFATHD 205
Cdd:PRK11819 164 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYP--GT-VVAVTHD 219
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
132-208 |
3.68e-09 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 54.56 E-value: 3.68e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 307615102 132 EALEIkhltEAYPNELSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATHDPQA 208
Cdd:cd03232 98 EALRF----SALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSA 170
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
24-205 |
3.71e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 55.27 E-value: 3.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 24 AVENVNLEIAPHDLVAIVGRSGNGKTTLLnlltgllKPTSGEVRVAGQNLAELGDRQLSELRNRTMGICTQSQSLLASLN 103
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLF-------KALMGFVRLASGKISILGQPTRQALQKNLVAYVPQSEEVDWSFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 104 ALDNAILPATLY--------SKASSETAFTRALELFEALEIKHLTEAypnELSGGEMRRVAIARALVNHPQVFIADEPTG 175
Cdd:PRK15056 95 VLVEDVVMMGRYghmgwlrrAKKRDRQIVTAALARVDMVEFRHRQIG---ELSGGQKKRVFLARAIAQQGQVILLDEPFT 171
|
170 180 190
....*....|....*....|....*....|
gi 307615102 176 DLDAQSTELVMRLLAGLPEAGTAVVFATHD 205
Cdd:PRK15056 172 GVDVKTEARIISLLRELRDEGKTMLVSTHN 201
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-204 |
4.16e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 55.80 E-value: 4.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 1 MSELVIEAKQLTREFirreKPFNAVENVNLEIAPHDLVAIVGRSGNGKttllnlltgllKPTSGEVRVAGQNLaelgdrq 80
Cdd:COG3845 1 MMPPALELRGITKRF----GGVVANDDVSLTVRPGEIHALLGENGAGKstlmkilyglyQPDSGEILIDGKPV------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 81 lsELRN----RTMGICTQSQ--SLLASLNALDNAILpatlyskaSSETAFTRALELFEAL-EIKHLTEAY-----PN--- 145
Cdd:COG3845 70 --RIRSprdaIALGIGMVHQhfMLVPNLTVAENIVL--------GLEPTKGGRLDRKAARaRIRELSERYgldvdPDakv 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 146 -ELSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATH 204
Cdd:COG3845 140 eDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITH 199
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
126-205 |
4.33e-09 |
|
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: 55.95 E-value: 4.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 126 RALELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATHD 205
Cdd:COG1245 192 KLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEHD 271
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
5-226 |
6.13e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 54.71 E-value: 6.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 5 VIEAKQLTREFiRREKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAElgdRQLSEL 84
Cdd:PRK13642 4 ILEVENLVFKY-EKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTA---ENVWNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 85 RnRTMGICTQSQsllaslnalDNAILPATLYSKAS---------SETAFTRALELFEALEIKHLTEAYPNELSGGEMRRV 155
Cdd:PRK13642 80 R-RKIGMVFQNP---------DNQFVGATVEDDVAfgmenqgipREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 307615102 156 AIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFA-THDPQALETARTVYEINAGVLSRQ 226
Cdd:PRK13642 150 AVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSiTHDLDEAASSDRILVMKAGEIIKE 221
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-180 |
8.08e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 55.37 E-value: 8.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 17 RREKPfnAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELgdRQLSELRNRTMgictqsq 96
Cdd:PLN03232 627 KTSKP--TLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRGSVAYV--PQVSWIFNATV------- 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 97 sllaSLNALDNAILPATLYSKASSETAFTRALELFEALEIKHLTEAYPNeLSGGEMRRVAIARALVNHPQVFIADEPTGD 176
Cdd:PLN03232 696 ----RENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDIYIFDDPLSA 770
|
....
gi 307615102 177 LDAQ 180
Cdd:PLN03232 771 LDAH 774
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
25-185 |
1.01e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 54.95 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 25 VENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGdrqLSELRNRtMGICTQSQSLLASlnA 104
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIG---LHDLRFK-ITIIPQDPVLFSG--S 1375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 105 LDNAILPATLYSKAssetaftralELFEALEIKHL---TEAYPNE-----------LSGGEMRRVAIARALVNHPQVFIA 170
Cdd:TIGR00957 1376 LRMNLDPFSQYSDE----------EVWWALELAHLktfVSALPDKldhecaeggenLSVGQRQLVCLARALLRKTKILVL 1445
|
170
....*....|....*
gi 307615102 171 DEPTGDLDAQSTELV 185
Cdd:TIGR00957 1446 DEATAAVDLETDNLI 1460
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
63-185 |
1.31e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 54.65 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 63 SGEVRVAGQNLAelgDRQLSELRNrTMGICTQsQSLLASLNALDNAIL---PATLySKASSETAFTRALELFEALEIKHL 139
Cdd:PTZ00265 1276 SGKILLDGVDIC---DYNLKDLRN-LFSIVSQ-EPMLFNMSIYENIKFgkeDATR-EDVKRACKFAAIDEFIESLPNKYD 1349
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 307615102 140 TEA--YPNELSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELV 185
Cdd:PTZ00265 1350 TNVgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLI 1397
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
24-221 |
1.40e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 53.34 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 24 AVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAelgDRQLSELRNRTMGICTQSQSLLASLN 103
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDIT---DWQTAKIMREAVAIVPEGRRVFSRMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 104 ALDNAILPATLYSKASSETAFTRALELFEALEIKHLTEAypNELSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTE 183
Cdd:PRK11614 97 VEENLAMGGFFAERDQFQERIKWVYELFPRLHERRIQRA--GTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQ 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 307615102 184 LVMRLLAGLPEAGTAVVFATHDP-QALETARTVYEINAG 221
Cdd:PRK11614 175 QIFDTIEQLREQGMTIFLVEQNAnQALKLADRGYVLENG 213
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
145-205 |
2.58e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.42 E-value: 2.58e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 307615102 145 NELSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELvmrLLAGLPEAGTAVVFATHD 205
Cdd:PRK11147 155 SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEW---LEGFLKTFQGSIIFISHD 212
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
26-221 |
2.89e-08 |
|
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: 52.09 E-value: 2.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 26 ENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGqnlaelgdrqlselrnrTMGICTQSQSLL-ASL-- 102
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-----------------SIAYVSQEPWIQnGTIre 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 103 NALDNAILPATLYSKASSETAFTRALELFEALEikhLTEAypNE----LSGGEMRRVAIARALVNHPQVFIADEPTGDLD 178
Cdd:cd03250 85 NILFGKPFDEERYEKVIKACALEPDLEILPDGD---LTEI--GEkginLSGGQKQRISLARAVYSDADIYLLDDPLSAVD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 307615102 179 AQ-STELVMRLLAGLPEAGTAVVFATHDPQALETARTVYEINAG 221
Cdd:cd03250 160 AHvGRHIFENCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
9-210 |
3.44e-08 |
|
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: 52.15 E-value: 3.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 9 KQLTREFIRREKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQ--NLAELGdrqlselrn 86
Cdd:cd03220 22 KLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRvsSLLGLG--------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 87 rtMGictqsqsLLASLNALDNAILPATLY--SKASSETAFTRALElFEALEiKHLTEAYpNELSGGEMRRVAIARALVNH 164
Cdd:cd03220 93 --GG-------FNPELTGRENIYLNGRLLglSRKEIDEKIDEIIE-FSELG-DFIDLPV-KTYSSGMKARLAFAIATALE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 307615102 165 PQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATHDPQALE 210
Cdd:cd03220 161 PDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIK 206
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-204 |
6.83e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 52.24 E-value: 6.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 1 MSELVIEAKQLTREFirreKPFNAVENVNLEIAPHDLVAIVGRSGNGKTtllnlltgllkpT--------------SGEV 66
Cdd:PRK13549 1 MMEYLLEMKNITKTF----GGVKALDNVSLKVRAGEIVSLCGENGAGKS------------TlmkvlsgvyphgtyEGEI 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 67 RVAGQnlaELGDRQLSELRNRTMGICTQSQSLLASLNALDNAILPA--TLYSKASSETAFTRALELFEALEIkHLTEAYP 144
Cdd:PRK13549 65 IFEGE---ELQASNIRDTERAGIAIIHQELALVKELSVLENIFLGNeiTPGGIMDYDAMYLRAQKLLAQLKL-DINPATP 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 307615102 145 -NELSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATH 204
Cdd:PRK13549 141 vGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISH 201
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
129-178 |
7.66e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.12 E-value: 7.66e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 307615102 129 ELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNHPQVFIADEPTGDLD 178
Cdd:PRK13409 195 EVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
25-210 |
8.81e-08 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 50.60 E-value: 8.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 25 VENVNLEIAPHDLVAIVGRSGNGKTTLLNLLT--GLLKPTSGEVRVAGQNLAELgdrqLSELRNRtMGIctqsqsllasl 102
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMghPKYEVTEGEILFKGEDITDL----PPEERAR-LGI----------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 103 naldnailpaTLyskassetAFTRALElFEALEIKHLTEaYPNE-LSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQS 181
Cdd:cd03217 80 ----------FL--------AFQYPPE-IPGVKNADFLR-YVNEgFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDA 139
|
170 180
....*....|....*....|....*....
gi 307615102 182 TELVMRLLAGLPEAGTAVVFATHDPQALE 210
Cdd:cd03217 140 LRLVAEVINKLREEGKSVLIITHYQRLLD 168
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
129-178 |
1.67e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.96 E-value: 1.67e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 307615102 129 ELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNHPQVFIADEPTGDLD 178
Cdd:PRK13409 436 EIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
26-205 |
1.75e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 50.37 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 26 ENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQLSelrnRTMGICTQS---------Q 96
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA----RRIGLLAQNattpgditvQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 97 SLLASLNALDNAILpaTLYSKaSSETAFTRALelfEALEIKHLTEAYPNELSGGEMRRVAIARALVNHPQVFIADEPTGD 176
Cdd:PRK10253 100 ELVARGRYPHQPLF--TRWRK-EDEEAVTKAM---QATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190
....*....|....*....|....*....|
gi 307615102 177 LDAQSTELVMRLLAGLP-EAGTAVVFATHD 205
Cdd:PRK10253 174 LDISHQIDLLELLSELNrEKGYTLAAVLHD 203
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
9-212 |
1.92e-07 |
|
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: 50.02 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 9 KQLTREFIRREKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQlSELRNR- 87
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEA-TRSRNRy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 88 TMGICTQSQSLLASlnALDNAILPATLYSKASSEtAFTRALELFEALEI------KHLTEAYPNeLSGGEMRRVAIARAL 161
Cdd:cd03290 80 SVAYAAQKPWLLNA--TVEENITFGSPFNKQRYK-AVTDACSLQPDIDLlpfgdqTEIGERGIN-LSGGQRQRICVARAL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 307615102 162 VNHPQVFIADEPTGDLDAQSTELVMR--LLAGLPEAGTAVVFATHDPQALETA 212
Cdd:cd03290 156 YQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLPHA 208
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
32-187 |
2.40e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 50.74 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 32 IAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGdrqLSELRnRTMGICTQSQSLLASLNALDnaILP 111
Cdd:PLN03232 1259 VSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFG---LTDLR-RVLSIIPQSPVLFSGTVRFN--IDP 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 112 ATLYSKAssetaftralELFEALEIKHLTEAYPN--------------ELSGGEMRRVAIARALVNHPQVFIADEPTGDL 177
Cdd:PLN03232 1333 FSEHNDA----------DLWEALERAHIKDVIDRnpfgldaevseggeNFSVGQRQLLSLARALLRRSKILVLDEATASV 1402
|
170
....*....|
gi 307615102 178 DAQSTELVMR 187
Cdd:PLN03232 1403 DVRTDSLIQR 1412
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
22-207 |
2.47e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 50.17 E-value: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 22 FNAVENVNLEIAPHDLVAIVGRSGNGKTTL-----LNLLTGLLKPTSGEVRVAGQNLAElGDRQLSELRNRtMGICTQSQ 96
Cdd:PRK14243 23 FLAVKNVWLDIPKNQITAFIGPSGCGKSTIlrcfnRLNDLIPGFRVEGKVTFHGKNLYA-PDVDPVEVRRR-IGMVFQKP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 97 SLLASlNALDN-AILPATLYSKASSETAFTRALELfEAL--EIKHLTEAYPNELSGGEMRRVAIARALVNHPQVFIADEP 173
Cdd:PRK14243 101 NPFPK-SIYDNiAYGARINGYKGDMDELVERSLRQ-AALwdEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190
....*....|....*....|....*....|....
gi 307615102 174 TGDLDAQSTELVMRLLAGLPEAGTaVVFATHDPQ 207
Cdd:PRK14243 179 CSALDPISTLRIEELMHELKEQYT-IIIVTHNMQ 211
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-210 |
2.57e-07 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 49.69 E-value: 2.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 1 MSElVIEAKQLTREFIRREKP------------------FNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPT 62
Cdd:COG1134 1 MSS-MIEVENVSKSYRLYHEPsrslkelllrrrrtrreeFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 63 SGEVRVAGQ--NLAELGdrqlselrnrtMGictqsqsLLASLNALDNAILPATLYSKASSET--------AFTralELFE 132
Cdd:COG1134 80 SGRVEVNGRvsALLELG-----------AG-------FHPELTGRENIYLNGRLLGLSRKEIdekfdeivEFA---ELGD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 133 ALE--IKHLTeaypnelSGgeMR-RVAIARALVNHPQVFIADE--PTGDLDAQstELVMRLLAGLPEAGTAVVFATHDPQ 207
Cdd:COG1134 139 FIDqpVKTYS-------SG--MRaRLAFAVATAVDPDILLVDEvlAVGDAAFQ--KKCLARIRELRESGRTVIFVSHSMG 207
|
...
gi 307615102 208 ALE 210
Cdd:COG1134 208 AVR 210
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
5-205 |
3.23e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 49.73 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 5 VIEAKQLTREFIR-REKPfnAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAElgdRQLSE 83
Cdd:PRK13650 4 IIEVKNLTFKYKEdQEKY--TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTE---ENVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 84 LRnRTMGICTQSQsllaslnalDNAILPAT--------LYSKA-SSETAFTRALELFEALEIKHLTEAYPNELSGGEMRR 154
Cdd:PRK13650 79 IR-HKIGMVFQNP---------DNQFVGATveddvafgLENKGiPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQR 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 307615102 155 VAIARALVNHPQVFIADEPTGDLDAQST-ELVMRLLAGLPEAGTAVVFATHD 205
Cdd:PRK13650 149 VAIAGAVAMRPKIIILDEATSMLDPEGRlELIKTIKGIRDDYQMTVISITHD 200
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
129-178 |
3.31e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 50.17 E-value: 3.31e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 307615102 129 ELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNHPQVFIADEPTGDLD 178
Cdd:COG1245 438 EIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-204 |
3.56e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 50.00 E-value: 3.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 19 EKPF---NAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQLSElrnRTMGICTQS 95
Cdd:PRK10762 11 DKAFpgvKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQE---AGIGIIHQE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 96 QSLLASLNALDNAIL---PATLYSKASSETAFTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNHPQVFIADE 172
Cdd:PRK10762 88 LNLIPQLTIAENIFLgreFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDE 167
|
170 180 190
....*....|....*....|....*....|..
gi 307615102 173 PTGDLDAQSTELVMRLLAGLPEAGTAVVFATH 204
Cdd:PRK10762 168 PTDALTDTETESLFRVIRELKSQGRGIVYISH 199
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
34-206 |
4.77e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 49.84 E-value: 4.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 34 PHDLVAIVGRSGNGKTTLLNLLTGLLKP--TSGEVRVAGqnlaeLGDRQlsELRNRTMGICTQSQSLLASLNALDNAILP 111
Cdd:PLN03140 905 PGVLTALMGVSGAGKTTLMDVLAGRKTGgyIEGDIRISG-----FPKKQ--ETFARISGYCEQNDIHSPQVTVRESLIYS 977
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 112 ATLY--SKASSETAFTRALELFEALEIKHLTEA---YP--NELSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTEL 184
Cdd:PLN03140 978 AFLRlpKEVSKEEKMMFVDEVMELVELDNLKDAivgLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAI 1057
|
170 180
....*....|....*....|..
gi 307615102 185 VMRLLAGLPEAGTAVVFATHDP 206
Cdd:PLN03140 1058 VMRTVRNTVDTGRTVVCTIHQP 1079
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
29-178 |
6.01e-07 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 48.42 E-value: 6.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 29 NLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQlselrnRTMGICTQSQSLLASLNALDNA 108
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSR------RPVSMLFQENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 307615102 109 IL---PATLYSKASSETAFTRALELFealeIKHLTEAYPNELSGGEMRRVAIARALVNHPQVFIADEPTGDLD 178
Cdd:PRK10771 93 GLglnPGLKLNAAQREKLHAIARQMG----IEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-207 |
8.41e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 48.23 E-value: 8.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 1 MSELVIEAKQLTREFIRREkpfnAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLK-----PTSGEVRVAGQNLae 75
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKKK----ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNI-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 76 LGDRQLS-ELRnRTMGICTQsQSLLASLNALDNAILP---ATLYSKASSETAFTRALE---LFEalEIKHLTEAYPNELS 148
Cdd:PRK14239 75 YSPRTDTvDLR-KEIGMVFQ-QPNPFPMSIYENVVYGlrlKGIKDKQVLDEAVEKSLKgasIWD--EVKDRLHDSALGLS 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 307615102 149 GGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVfATHDPQ 207
Cdd:PRK14239 151 GGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLL-VTRSMQ 208
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
145-216 |
8.45e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 49.26 E-value: 8.45e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 307615102 145 NELSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLP--EAGTAVVFAtHDPQALETARTVY 216
Cdd:PTZ00265 578 SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIA-HRLSTIRYANTIF 650
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-174 |
9.10e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 48.97 E-value: 9.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 2 SELVIEAKQLTREFirreKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQnlaELGDRQL 81
Cdd:NF033858 263 DEPAIEARGLTMRF----GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQ---PVDAGDI 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 82 sELRNRtMGICTQSQSLLASLNALDNAILPATLYSKASSETAfTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARAL 161
Cdd:NF033858 336 -ATRRR-VGYMSQAFSLYGELTVRQNLELHARLFHLPAAEIA-ARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAV 412
|
170
....*....|...
gi 307615102 162 VNHPQVFIADEPT 174
Cdd:NF033858 413 IHKPELLILDEPT 425
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
25-217 |
9.61e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 47.64 E-value: 9.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 25 VENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAElgDRqlselrnrtmgiCTQSQSLL----- 99
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK--DL------------CTYQKQLCfvghr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 100 ASLNAldNAILPATLYSKASSETAFTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNHPQVFIADEPTGDLDA 179
Cdd:PRK13540 83 SGINP--YLTLRENCLYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDE 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 307615102 180 QSTELVMRLLAGLPEAGTAVVFATHdpQALETARTVYE 217
Cdd:PRK13540 161 LSLLTIITKIQEHRAKGGAVLLTSH--QDLPLNKADYE 196
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-205 |
1.14e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 48.17 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 25 VENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGeVRVAGQNLaeLGDRQLSELRN-----RTMGICTQSQSLL 99
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSG-YRYSGDVL--LGGRSIFNYRDvlefrRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 100 AsLNALDNAILPATLYS----KASSETAFTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNHPQVFIADEPTG 175
Cdd:PRK14271 114 P-MSIMDNVLAGVRAHKlvprKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTS 192
|
170 180 190
....*....|....*....|....*....|
gi 307615102 176 DLDAQSTELVMRLLAGLPEAGTaVVFATHD 205
Cdd:PRK14271 193 ALDPTTTEKIEEFIRSLADRLT-VIIVTHN 221
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
13-226 |
1.16e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 48.56 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 13 REFIRREKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELgdrQLSELRNRtMGIC 92
Cdd:PRK10789 319 RQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL---QLDSWRSR-LAVV 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 93 TQSQSLLASLNAlDNAILPATLYSKASSETAfTRALELFEalEIKHLTEAYPNE-------LSGGEMRRVAIARALVNHP 165
Cdd:PRK10789 395 SQTPFLFSDTVA-NNIALGRPDATQQEIEHV-ARLASVHD--DILRLPQGYDTEvgergvmLSGGQKQRISIARALLLNA 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 307615102 166 QVFIADEPTGDLDAQSTELVMRLLAGLPEAGTaVVFATHDPQALETARTVYEINAGVLSRQ 226
Cdd:PRK10789 471 EILILDDALSAVDGRTEHQILHNLRQWGEGRT-VIISAHRLSALTEASEILVMQHGHIAQR 530
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
147-204 |
1.44e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.09 E-value: 1.44e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 307615102 147 LSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGL-PEAGTAVVFATH 204
Cdd:PRK10938 402 LSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLiSEGETQLLFVSH 460
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
147-221 |
1.98e-06 |
|
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: 46.55 E-value: 1.98e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 307615102 147 LSGGEMRRVAIARALVNHPQ--VFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATHDPQALETARTVYEINAG 221
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSSADWIIDFGPG 164
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
28-185 |
2.24e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 47.81 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 28 VNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGdrqLSELRNRtMGICTQSQSLLAS---LNa 104
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFG---LMDLRKV-LGIIPQAPVLFSGtvrFN- 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 105 LDnailPATLYSKAssetaftralELFEALEIKHL---------------TEAYPNeLSGGEMRRVAIARALVNHPQVFI 169
Cdd:PLN03130 1333 LD----PFNEHNDA----------DLWESLERAHLkdvirrnslgldaevSEAGEN-FSVGQRQLLSLARALLRRSKILV 1397
|
170
....*....|....*.
gi 307615102 170 ADEPTGDLDAQSTELV 185
Cdd:PLN03130 1398 LDEATAAVDVRTDALI 1413
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
147-207 |
2.65e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 47.64 E-value: 2.65e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 307615102 147 LSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPeaGTaVVFATHDPQ 207
Cdd:PRK11147 441 LSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQ--GT-VLLVSHDRQ 498
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
129-205 |
2.84e-06 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 46.63 E-value: 2.84e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 307615102 129 ELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFAT-HD 205
Cdd:cd03237 98 EIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVeHD 175
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-200 |
3.36e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 47.09 E-value: 3.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 3 ELVIEAKQLTRefirreKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGqnlAELGDRQLS 82
Cdd:PRK09700 263 ETVFEVRNVTS------RDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNG---KDISPRSPL 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 83 ELRNRTMGICTQSQ---------SL---LASLNALDNAILPATLYSKASSETAFTrALELFEALEIK-HLTEAYPNELSG 149
Cdd:PRK09700 334 DAVKKGMAYITESRrdngffpnfSIaqnMAISRSLKDGGYKGAMGLFHEVDEQRT-AENQRELLALKcHSVNQNITELSG 412
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 307615102 150 GEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVV 200
Cdd:PRK09700 413 GNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVIL 463
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
24-204 |
3.47e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.03 E-value: 3.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 24 AVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQnlaELGDRQLSELRNRTMGICTQSQSLLASLN 103
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGK---EIDFKSSKEALENGISMVHQELNLVLQRS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 104 ALDNAIL-------PATLYSKASSETAftralELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNHPQVFIADEPTGD 176
Cdd:PRK10982 90 VMDNMWLgryptkgMFVDQDKMYRDTK-----AIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSS 164
|
170 180
....*....|....*....|....*...
gi 307615102 177 LDAQSTELVMRLLAGLPEAGTAVVFATH 204
Cdd:PRK10982 165 LTEKEVNHLFTIIRKLKERGCGIVYISH 192
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
129-209 |
6.41e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 46.64 E-value: 6.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 129 ELFEALEIKHLTEAY---PNE-LSGGEMRRVAIARALVNHPQ--VFIaDEPTGDLDAQSTELVMRLLAGLPEAGTAVVFA 202
Cdd:TIGR00956 880 EVIKLLEMESYADAVvgvPGEgLNVEQRKRLTIGVELVAKPKllLFL-DEPTSGLDSQTAWSICKLMRKLADHGQAILCT 958
|
....*..
gi 307615102 203 THDPQAL 209
Cdd:TIGR00956 959 IHQPSAI 965
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
27-205 |
1.14e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 45.43 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 27 NVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGDRQ--------LSELRnrtmgictQSQSL 98
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrlarglvyLPEDR--------QSSGL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 99 L--ASLN----ALDNAILPatLYSKASSETAftrALELF-EALEIK--HLTEAYpNELSGGEMRRVAIARALVNHPQVFI 169
Cdd:PRK15439 353 YldAPLAwnvcALTHNRRG--FWIKPARENA---VLERYrRALNIKfnHAEQAA-RTLSGGNQQKVLIAKCLEASPQLLI 426
|
170 180 190
....*....|....*....|....*....|....*.
gi 307615102 170 ADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATHD 205
Cdd:PRK15439 427 VDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSD 462
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
147-178 |
1.50e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 44.99 E-value: 1.50e-05
10 20 30
....*....|....*....|....*....|..
gi 307615102 147 LSGGEMRRVAIARALVNHPQVFIADEPTGDLD 178
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
146-205 |
2.10e-05 |
|
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: 44.93 E-value: 2.10e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 307615102 146 ELSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQStelvMRLL--AGLPEAGTAVVFaTHD 205
Cdd:TIGR03719 443 QLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVET----LRALeeALLNFAGCAVVI-SHD 499
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
20-223 |
2.51e-05 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 44.13 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 20 KPfnAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELgdrQLSELRNRtMGICTQsqsll 99
Cdd:cd03288 34 KP--VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKL---PLHTLRSR-LSIILQ----- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 100 aslnalDNAILPATLYSKASSETAFTRAlELFEALEI---KHLTEAYPNEL-----------SGGEMRRVAIARALVNHP 165
Cdd:cd03288 103 ------DPILFSGSIRFNLDPECKCTDD-RLWEALEIaqlKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKS 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 307615102 166 QVFIADEPTGDLDaQSTELVMRLLAGLPEAGTAVVFATHDPQALETARTVYEINAGVL 223
Cdd:cd03288 176 SILIMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGIL 232
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
28-214 |
2.75e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 43.68 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 28 VNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNlAELGDRqlselrNRTMGICTQSQSLLASLNALDN 107
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKT-ATRGDR------SRFMAYLGHLPGLKADLSTLEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 108 AILPATLYSKASSETAFTralelfeALEIKHLT---EAYPNELSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTEL 184
Cdd:PRK13543 103 LHFLCGLHGRRAKQMPGS-------ALAIVGLAgyeDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITL 175
|
170 180 190
....*....|....*....|....*....|
gi 307615102 185 VMRLLAGLPEAGTAVVFATHDPQALETART 214
Cdd:PRK13543 176 VNRMISAHLRGGGAALVTTHGAYAAPPVRT 205
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
20-204 |
3.01e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 44.27 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 20 KPFNAVE---NVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAelgdrQLSELRNRTMGI--CTQ 94
Cdd:PRK15439 19 KQYSGVEvlkGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCA-----RLTPAKAHQLGIylVPQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 95 SQSLLASLNALDNailpaTLYSKASSETAFTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNHPQVFIADEPT 174
Cdd:PRK15439 94 EPLLFPNLSVKEN-----ILFGLPKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPT 168
|
170 180 190
....*....|....*....|....*....|
gi 307615102 175 GDLDAQSTELVMRLLAGLPEAGTAVVFATH 204
Cdd:PRK15439 169 ASLTPAETERLFSRIRELLAQGVGIVFISH 198
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
24-204 |
3.62e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 44.13 E-value: 3.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 24 AVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQnlaELGDRQLSELRNRTMGICTQSQSLLASLN 103
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQ---EMRFASTTAALAAGVAIIYQELHLVPEMT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 104 ALDNaILPATLYSKA---SSETAFTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQ 180
Cdd:PRK11288 96 VAEN-LYLGQLPHKGgivNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAR 174
|
170 180
....*....|....*....|....
gi 307615102 181 STELVMRLLAGLPEAGTAVVFATH 204
Cdd:PRK11288 175 EIEQLFRVIRELRAEGRVILYVSH 198
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
147-204 |
3.99e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 44.00 E-value: 3.99e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 147 LSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELVMR--LLAGLpeAGTAVVFATH 204
Cdd:PTZ00243 783 LSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEecFLGAL--AGKTRVLATH 840
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
133-218 |
5.03e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.05 E-value: 5.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 133 ALEIKHLTEAYP-NELSGGEMRRVAIARALVN---HPQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATHDPQA 208
Cdd:PRK00635 795 SLGLDYLPLGRPlSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHV 874
|
90
....*....|
gi 307615102 209 LETARTVYEI 218
Cdd:PRK00635 875 VKVADYVLEL 884
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
70-221 |
5.87e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.66 E-value: 5.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 70 GQNLAELGDRQLSELRNRTMGICTQSQSLLASLNALDNAIlpATLYSKASSETAFTRALelfealeikhlteaypNELSG 149
Cdd:PRK00635 418 GKTFAEFQQMSLQELFIFLSQLPSKSLSIEEVLQGLKSRL--SILIDLGLPYLTPERAL----------------ATLSG 479
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 307615102 150 GEMRRVAIARALVNHPQ--VFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATHDPQALETARTVYEINAG 221
Cdd:PRK00635 480 GEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMISLADRIIDIGPG 553
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
27-215 |
8.20e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 42.17 E-value: 8.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 27 NVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNlaelgdrqLSELRNRTMGICTQSQSLLASLNALD 106
Cdd:PRK13541 18 DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCN--------INNIAKPYCTYIGHNLGLKLEMTVFE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 107 NAILPATLYSKASSETAFTRALELFEALEIKHLTeaypneLSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELVM 186
Cdd:PRK13541 90 NLKFWSEIYNSAETLYAAIHYFKLHDLLDEKCYS------LSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLN 163
|
170 180
....*....|....*....|....*....
gi 307615102 187 RLLAGLPEAGTAVVFATHDPQALETARTV 215
Cdd:PRK13541 164 NLIVMKANSGGIVLLSSHLESSIKSAQIL 192
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
147-223 |
1.41e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 41.47 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 147 LSGGEMRRVAIARAL------VnhpqVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATHDPQALETARTVYEI-- 218
Cdd:cd03270 138 LSGGEAQRIRLATQIgsgltgV----LYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHVIDIgp 213
|
....*
gi 307615102 219 NAGVL 223
Cdd:cd03270 214 GAGVH 218
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
119-212 |
1.54e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 42.03 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 119 SSETAFTRALELFEALEIKHLTEAYPNELSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTA 198
Cdd:NF000106 117 SRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGAT 196
|
90
....*....|....
gi 307615102 199 VVFAThdpQALETA 212
Cdd:NF000106 197 VLLTT---QYMEEA 207
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
147-201 |
1.62e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 42.22 E-value: 1.62e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 307615102 147 LSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVF 201
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIV 460
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
146-205 |
1.64e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 41.02 E-value: 1.64e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 307615102 146 ELSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFAT-HD 205
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVeHD 131
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
28-178 |
1.72e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 42.07 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 28 VNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQNLAELGdrqLSELRnRTMGICTQSQSLLASLNALDn 107
Cdd:PTZ00243 1329 VSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYG---LRELR-RQFSMIPQDPVLFDGTVRQN- 1403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 108 aILPatlYSKASSEtaftralELFEALEIKHLTEAYPNELSG--------------GEMRRVAIARALVNHPQVFI-ADE 172
Cdd:PTZ00243 1404 -VDP---FLEASSA-------EVWAALELVGLRERVASESEGidsrvleggsnysvGQRQLMCMARALLKKGSGFIlMDE 1472
|
....*.
gi 307615102 173 PTGDLD 178
Cdd:PTZ00243 1473 ATANID 1478
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
147-218 |
1.81e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 40.81 E-value: 1.81e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 307615102 147 LSGGEMRRVAIARALVNHP----QVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATHDPQALETARTVYEI 218
Cdd:cd03227 78 LSGGEKELSALALILALASlkprPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELADKLIHI 153
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
147-223 |
2.26e-04 |
|
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: 41.73 E-value: 2.26e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 307615102 147 LSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATHD-PQALETARTVYEINAGVL 223
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSElAEVLGLSDRVLVIGEGKL 481
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
145-221 |
2.72e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.54 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 145 NELSGGEMRRVAIAR----ALVNhpQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATHDPQALETARTVYEINA 220
Cdd:TIGR00630 487 GTLSGGEAQRIRLATqigsGLTG--VLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVIDIGP 564
|
.
gi 307615102 221 G 221
Cdd:TIGR00630 565 G 565
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
147-188 |
2.79e-04 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 40.71 E-value: 2.79e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 307615102 147 LSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQST-ELVMRL 188
Cdd:cd03233 119 ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTAlEILKCI 161
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
147-212 |
4.78e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.77 E-value: 4.78e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 307615102 147 LSGGEMRRVAIARAL---VNHPQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATHDPQALETA 212
Cdd:TIGR00630 830 LSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVIKTA 898
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
25-206 |
8.68e-04 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 39.42 E-value: 8.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 25 VENVNLEIAPHDLVAIVGRSGNGKTTLLNL--------LTGLLKPTSGEVRVAGQNLAELGDRQLSELRnrtmGICTQSQ 96
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKAlagdltggGAPRGARVTGDVTLNGEPLAAIDAPRLARLR----AVLPQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 97 SLLASLNALDNAILPATLYSKASSETAF------TRALEL--FEALEIKHLTeaypnELSGGEMRRVAIARALVN----- 163
Cdd:PRK13547 93 QPAFAFSAREIVLLGRYPHARRAGALTHrdgeiaWQALALagATALVGRDVT-----TLSGGELARVQFARVLAQlwpph 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 307615102 164 ----HPQVFIADEPTGDLD-AQSTELVMRLLAGLPEAGTAVVFATHDP 206
Cdd:PRK13547 168 daaqPPRYLLLDEPTAALDlAHQHRLLDTVRRLARDWNLGVLAIVHDP 215
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
24-224 |
1.00e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 39.57 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 24 AVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQnlaELGDRQLSELRNRTMGICTQ----SQSLL 99
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGK---PVTAEQPEDYRKLFSAVFTDfhlfDQLLG 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 100 ASLNALDNAILPATLyskassetaftRALELFEALEIKHLTEAYPNeLSGGEMRRVAIARALVNHPQVFIADEPTGDLDA 179
Cdd:PRK10522 415 PEGKPANPALVEKWL-----------ERLKMAHKLELEDGRISNLK-LSKGQKKRLALLLALAEERDILLLDEWAADQDP 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 307615102 180 Q-STELVMRLLAGLPEAGTAVVFATHDPQALETARTVYEINAGVLS 224
Cdd:PRK10522 483 HfRREFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQLS 528
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
147-205 |
1.66e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.07 E-value: 1.66e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 307615102 147 LSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTElvmRLLAGLPEAGTAVVFATHD 205
Cdd:PLN03073 628 LSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVE---ALIQGLVLFQGGVLMVSHD 683
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
91-210 |
1.88e-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: 38.52 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 91 ICTQSQSLLASLNALDNAILPATLYSKASSETAFTRALELFEALEIKHLTEAYPNELSGGeMRRV-----AIARALVNHP 165
Cdd:pfam13304 181 LKELLQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGGELPAFELSDG-TKRLlallaALLSALPKGG 259
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 307615102 166 QVFIaDEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATHDPQALE 210
Cdd:pfam13304 260 LLLI-DEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPLLLD 303
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
146-205 |
2.03e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 38.56 E-value: 2.03e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 307615102 146 ELSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQStelvMRLL--AGLPEAGTAVVFaTHD 205
Cdd:PRK11819 445 VLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVET----LRALeeALLEFPGCAVVI-SHD 501
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
147-206 |
2.61e-03 |
|
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: 37.63 E-value: 2.61e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 147 LSGGEMRRVAIARALVNHPQV----------FIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATHDP 206
Cdd:cd03279 124 LSGGETFLASLSLALALSEVLqnrggarleaLFIDEGFGTLDPEALEAVATALELIRTENRMVGVISHVE 193
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
147-221 |
3.21e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 38.27 E-value: 3.21e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 307615102 147 LSGGEMRRVAIARALV---NHPQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATHDPQALETARTVYEINAG 221
Cdd:PRK00635 1700 LSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDPALLKQADYLIEMGPG 1777
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
6-209 |
3.55e-03 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 37.53 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 6 IEAKQLTREFIrrEKPFNAVENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKpTSGEVRVAGQNLAELgdrQLSELR 85
Cdd:cd03289 3 MTVKDLTAKYT--EGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSV---PLQKWR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 86 nRTMGICTQ-----SQSLLASLNAldnailpatlYSKASSETAFTRAlelfEALEIKHLTEAYPNE-----------LSG 149
Cdd:cd03289 77 -KAFGVIPQkvfifSGTFRKNLDP----------YGKWSDEEIWKVA----EEVGLKSVIEQFPGQldfvlvdggcvLSH 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 150 GEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGlPEAGTAVVFATHDPQAL 209
Cdd:cd03289 142 GHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQ-AFADCTVILSEHRIEAM 200
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
147-205 |
4.52e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 37.58 E-value: 4.52e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 307615102 147 LSGGEMRRVAIARALVNHPQVFIADEPTGDLDAQSTELVMRLLAGLPEAGTAVVFATHD 205
Cdd:PRK11288 397 LSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSD 455
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
25-178 |
5.96e-03 |
|
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: 37.14 E-value: 5.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 25 VENVNLEIAPHDLVAIVGRSGNGKTTLLNLLTGLLKPTSGEVRVAGQnlaelgdrqlselrnrtMGICTQSqsllaslna 104
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-----------------ISFSSQF--------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307615102 105 ldNAILPATLYSKASSETAFT--RALELFEALEIKHLTEAYPNE-----------LSGGEMRRVAIARALVNHPQVFIAD 171
Cdd:cd03291 107 --SWIMPGTIKENIIFGVSYDeyRYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLD 184
|
....*..
gi 307615102 172 EPTGDLD 178
Cdd:cd03291 185 SPFGYLD 191
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
145-178 |
6.62e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 37.15 E-value: 6.62e-03
10 20 30
....*....|....*....|....*....|....
gi 307615102 145 NELSGGEMRRVAIARALVNHPQVFIADEPTGDLD 178
Cdd:PLN03073 343 KTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| |
