|
Name |
Accession |
Description |
Interval |
E-value |
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
15-252 |
4.84e-30 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 114.18 E-value: 4.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 15 EISGLRFTYpgidghpppGSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGkhMVEPhmvrvlgrsafhDTGLTS 94
Cdd:COG4555 3 EVENLSKKY---------GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAG--LLKP------------DSGSIL 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 95 SG--DLCYLGGEWRRDVAFAGFEVPIQMDISAEKMI------FGVAGIDPQRR-DELIKVLDID--ISWRLHKVSDGQRR 163
Cdd:COG4555 60 IDgeDVRKEPREARRQIGVLPDERGLYDRLTVRENIryfaelYGLFDEELKKRiEELIELLGLEefLDRRVGELSTGMKK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 164 RVQICMGLLKPFKVLLLDEITVDLDVLARADLLKFLRkECEERGATIIYATHIFDGLEDWPTHIVYVANGKLQLALPMEK 243
Cdd:COG4555 140 KVALARALVHDPKVLLLDEPTNGLDVMARRLLREILR-ALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDE 218
|
250
....*....|
gi 7406423 244 VKE-TSKKSL 252
Cdd:COG4555 219 LREeIGEENL 228
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
14-246 |
3.53e-27 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 106.69 E-value: 3.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 14 VEISGLRFTYpgidghpppGSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGkhMVEPHM--VRVLGRSAFHDtg 91
Cdd:COG1131 1 IEVRGLTKRY---------GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLG--LLRPTSgeVRVLGEDVARD-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 92 ltssgdlcylGGEWRRDVAFAGFEVPIQMDISAEKM------IFGVAGIDPQRR-DELIKVLDID--ISWRLHKVSDGQR 162
Cdd:COG1131 68 ----------PAEVRRRIGYVPQEPALYPDLTVRENlrffarLYGLPRKEARERiDELLELFGLTdaADRKVGTLSGGMK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 163 RRVQICMGLLKPFKVLLLDEITVDLDVLARADLLKFLRKECEErGATIIYATHIFDGLEDWPTHIVYVANGKLQLALPME 242
Cdd:COG1131 138 QRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPD 216
|
....
gi 7406423 243 KVKE 246
Cdd:COG1131 217 ELKA 220
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
15-234 |
8.90e-27 |
|
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: 104.86 E-value: 8.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 15 EISGLRFTYPGidghpppGSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGkhMVEPH--MVRVLGRSAFHDTgl 92
Cdd:cd03225 1 ELKNLSFSYPD-------GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNG--LLGPTsgEVLVDGKDLTKLS-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 93 tssgdlcylGGEWRRDVAFAgFEVP---IQMDISAEKMIFGV--AGIDP----QRRDELIKVLDIDI--SWRLHKVSDGQ 161
Cdd:cd03225 70 ---------LKELRRKVGLV-FQNPddqFFGPTVEEEVAFGLenLGLPEeeieERVEEALELVGLEGlrDRSPFTLSGGQ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7406423 162 RRRVQI-CMGLLKPfKVLLLDEITVDLDVLARADLLKFLRKECEErGATIIYATHIFDGLEDWPTHIVYVANGK 234
Cdd:cd03225 140 KQRVAIaGVLAMDP-DILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
15-234 |
9.32e-25 |
|
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: 97.70 E-value: 9.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 15 EISGLRFTYpgidghpppGSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGkhMVEPHMVRVLgrsaFHDTGLTS 94
Cdd:cd00267 1 EIENLSFRY---------GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAG--LLKPTSGEIL----IDGKDIAK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 95 SGDLcylggEWRRDVAFagfevpiqmdisaekmifgvagidpqrrdelikvldidiswrLHKVSDGQRRRVQICMGLLKP 174
Cdd:cd00267 66 LPLE-----ELRRRIGY------------------------------------------VPQLSGGQRQRVALARALLLN 98
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 175 FKVLLLDEITVDLDVLARADLLKFLRKECEErGATIIYATHIFDGLEDWPTHIVYVANGK 234
Cdd:cd00267 99 PDLLLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
14-235 |
7.38e-24 |
|
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: 95.93 E-value: 7.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 14 VEISGLRFTYpgidghpppGSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGkhMVEPH--MVRVLGRSAFHDtg 91
Cdd:cd03230 1 IEVRNLSKRY---------GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILG--LLKPDsgEIKVLGKDIKKE-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 92 ltssgdlcylGGEWRRDVAFAGFEVPIQMDISAEKMIfgvagidpqrrdelikvldidiswrlhKVSDGQRRRVQICMGL 171
Cdd:cd03230 68 ----------PEEVKRRIGYLPEEPSLYENLTVRENL---------------------------KLSGGMKQRLALAQAL 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7406423 172 L-KPfKVLLLDEITVDLDVLARADLLKFLRKECEErGATIIYATHIFDGLEDWPTHIVYVANGKL 235
Cdd:cd03230 111 LhDP-ELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
14-235 |
8.04e-23 |
|
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: 94.71 E-value: 8.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 14 VEISGLRFTYPGidghpppgSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGkhMVEPH--MVRVLGRSafhdtg 91
Cdd:COG1122 1 IELENLSFSYPG--------GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNG--LLKPTsgEVLVDGKD------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 92 lTSSGDLcylgGEWRR--------------------DVAFAgfevPIQMDISAEKMIfgvagidpQRRDELIKVLDIDiS 151
Cdd:COG1122 65 -ITKKNL----RELRRkvglvfqnpddqlfaptveeDVAFG----PENLGLPREEIR--------ERVEEALELVGLE-H 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 152 WR---LHKVSDGQRRRVQICmGLL--KPfKVLLLDEITVDLDVLARADLLKFLrKECEERGATIIYATHIFDGLEDWPTH 226
Cdd:COG1122 127 LAdrpPHELSGGQKQRVAIA-GVLamEP-EVLVLDEPTAGLDPRGRRELLELL-KRLNKEGKTVIIVTHDLDLVAELADR 203
|
....*....
gi 7406423 227 IVYVANGKL 235
Cdd:COG1122 204 VIVLDDGRI 212
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
33-244 |
8.80e-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: 8.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 33 GSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGK-HMVEPHMVRVLGRSafhdtgltssgdlcyLGG----EWRR 107
Cdd:COG1119 14 GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDlPPTYGNDVRLFGER---------------RGGedvwELRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 108 DVAFAGFEV--PIQMDISAEKMI----FGVAGI-----DPQRR--DELIKVLDID--ISWRLHKVSDGQRRRVQICMGLL 172
Cdd:COG1119 79 RIGLVSPALqlRFPRDETVLDVVlsgfFDSIGLyreptDEQREraRELLELLGLAhlADRPFGTLSQGEQRRVLIARALV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7406423 173 KPFKVLLLDEITVDLDVLARADLLKFLRKECEERGATIIYATHifdGLEDWP---THIVYVANGKLQLALPMEKV 244
Cdd:COG1119 159 KDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTH---HVEEIPpgiTHVLLLKDGRVVAAGPKEEV 230
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
14-215 |
1.86e-22 |
|
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: 92.93 E-value: 1.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 14 VEISGLRFTYpgidghpppGSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGkhMVEPhmvrvlgrsafhdtglt 93
Cdd:COG4133 3 LEAENLSCRR---------GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAG--LLPP----------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 94 SSGDLCYLGG-------EWRRDVAFAGFEVPIQMDISAE---KMIFGVAGIDPQRR--DELIKVLDIDISWRL--HKVSD 159
Cdd:COG4133 55 SAGEVLWNGEpirdareDYRRRLAYLGHADGLKPELTVRenlRFWAALYGLRADREaiDEALEAVGLAGLADLpvRQLSA 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 7406423 160 GQRRRVQICMGLLKPFKVLLLDEITVDLDVLARADLLKFLRKECeERGATIIYATH 215
Cdd:COG4133 135 GQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHL-ARGGAVLLTTH 189
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
14-236 |
1.40e-21 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 91.63 E-value: 1.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 14 VEISGLRFTY------PGIDG------HPPPGSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGkhMVEPhmvrv 81
Cdd:cd03267 1 IEVSNLSKSYrvyskePGLIGslkslfKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSG--LLQP----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 82 lgrsafhdtgltSSGDLCYLGG-EWRRDVAFA-------GFEVPIQMDISAEK---MIFGVAGIDP----QRRDELIKVL 146
Cdd:cd03267 74 ------------TSGEVRVAGLvPWKRRKKFLrrigvvfGQKTQLWWDLPVIDsfyLLAAIYDLPParfkKRLDELSELL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 147 DI----DISWRlhKVSDGQRRRVQICMGLLKPFKVLLLDEITVDLDVLARADLLKFLRKECEERGATIIYATHIFDGLED 222
Cdd:cd03267 142 DLeellDTPVR--QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEA 219
|
250
....*....|....
gi 7406423 223 WPTHIVYVANGKLQ 236
Cdd:cd03267 220 LARRVLVIDKGRLL 233
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
14-244 |
8.02e-21 |
|
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: 92.66 E-value: 8.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 14 VEISGLRFTYPGidghpppGSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGkhmVEPHMVRVLGRSAFHDTGLT 93
Cdd:COG1123 5 LEVRDLSVRYPG-------GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMG---LLPHGGRISGEVLLDGRDLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 94 SSGDlcylgGEWRRDVAF-------AGFEVPIQMDISAEKMIFGVAGIDPQRR-DELIKVLDIDISWR--LHKVSDGQRR 163
Cdd:COG1123 75 ELSE-----ALRGRRIGMvfqdpmtQLNPVTVGDQIAEALENLGLSRAEARARvLELLEAVGLERRLDryPHQLSGGQRQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 164 RVQICMGLLKPFKVLLLDEITVDLDVLARADLLKFLRKECEERGATIIYATHIFDGLEDWPTHIVYVANGKLQLALPMEK 243
Cdd:COG1123 150 RVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEE 229
|
.
gi 7406423 244 V 244
Cdd:COG1123 230 I 230
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
14-215 |
6.99e-19 |
|
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: 83.71 E-value: 6.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 14 VEISGLRFTYPGidghpPPGSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGkhMVEPhmvrVLGRSAFHDTGLT 93
Cdd:cd03257 2 LEVKNLSVSFPT-----GGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILG--LLKP----TSGSIIFDGKDLL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 94 SsgdlcyLGGEWRRDvafagFEVPIQM----------------DISAEKMIFGVAGIDPQRRDE-----LIKV-LDIDIS 151
Cdd:cd03257 71 K------LSRRLRKI-----RRKEIQMvfqdpmsslnprmtigEQIAEPLRIHGKLSKKEARKEavlllLVGVgLPEEVL 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7406423 152 WRL-HKVSDGQRRRVQICMGL-LKPfKVLLLDEITVDLDVLARADLLKFLRKECEERGATIIYATH 215
Cdd:cd03257 140 NRYpHELSGGQRQRVAIARALaLNP-KLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITH 204
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
15-215 |
9.96e-19 |
|
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: 82.10 E-value: 9.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 15 EISGLRFTYpgidghpppGSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGKHMVEPHMVRVLGRSAFHdtglts 94
Cdd:cd03214 1 EVENLSVGY---------GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLAS------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 95 sgdlcYLGGEWRRDVAFagfeVPIQMDIsaekmiFGVAGIDPQRRDELikvldidiswrlhkvSDGQRRRVQICMGLLKP 174
Cdd:cd03214 66 -----LSPKELARKIAY----VPQALEL------LGLAHLADRPFNEL---------------SGGERQRVLLARALAQE 115
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 7406423 175 FKVLLLDEITVDLDVLARADLLKFLRKECEERGATIIYATH 215
Cdd:cd03214 116 PPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLH 156
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
38-215 |
1.18e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 84.75 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 38 IEDFSITLNSSDRCLLVGSNGAGKTTILKIL-------GGKhmvephmVRVLGRSAfhdtgltssgdlcylggeWRRDVA 110
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLtgilvptSGE-------VRVLGYVP------------------FKRRKE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 111 FAgfevpiqMDISaekMIFG--------------------VAGIDP----QRRDELIKVLDID--ISWRLHKVSDGQRRR 164
Cdd:COG4586 93 FA-------RRIG---VVFGqrsqlwwdlpaidsfrllkaIYRIPDaeykKRLDELVELLDLGelLDTPVRQLSLGQRMR 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 7406423 165 VQICMGLL-KPfKVLLLDEITVDLDVLARADLLKFLRKECEERGATIIYATH 215
Cdd:COG4586 163 CELAAALLhRP-KILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSH 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
14-215 |
9.29e-18 |
|
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: 81.24 E-value: 9.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 14 VEISGLRFTYpgidghpppGSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGkhMVEPH--MVRVLGRSAfhdTG 91
Cdd:COG1120 2 LEAENLSVGY---------GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAG--LLKPSsgEVLLDGRDL---AS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 92 LTSSgdlcylggEWRRDVAFAGFEVPIQMDISAE-----------KMIFGVAGIDPQRRDELIKVLDI-DISWR-LHKVS 158
Cdd:COG1120 68 LSRR--------ELARRIAYVPQEPPAPFGLTVRelvalgryphlGLFGRPSAEDREAVEEALERTGLeHLADRpVDELS 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 7406423 159 DGQRRRVQICMGLL-KPfKVLLLDEITVDLDVLARADLLKFLRKECEERGATIIYATH 215
Cdd:COG1120 140 GGERQRVLIARALAqEP-PLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLH 196
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
53-235 |
2.75e-17 |
|
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: 79.33 E-value: 2.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 53 LVGSNGAGKTTILKILGGkhMVEPH--MVRVLGRSAFHD-------TGLTSSGDLCYLGGEWRRDVA-FAGFevpiqmdi 122
Cdd:cd03266 36 LLGPNGAGKTTTLRMLAG--LLEPDagFATVDGFDVVKEpaearrrLGFVSDSTGLYDRLTARENLEyFAGL-------- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 123 saekmiFGVAGID-PQRRDELIKVLDID--ISWRLHKVSDGQRRRVQICMGLLKPFKVLLLDEITVDLDVLARADLLKFL 199
Cdd:cd03266 106 ------YGLKGDElTARLEELADRLGMEelLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFI 179
|
170 180 190
....*....|....*....|....*....|....*.
gi 7406423 200 RKECEErGATIIYATHIFDGLEDWPTHIVYVANGKL 235
Cdd:cd03266 180 RQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
14-215 |
3.64e-17 |
|
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: 81.87 E-value: 3.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 14 VEISGLRFTYPGidghPPPGSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGkhMVEPH--MVRVLGRsafhDTG 91
Cdd:COG1123 261 LEVRNLSKRYPV----RGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLG--LLRPTsgSILFDGK----DLT 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 92 LTSSGDLcylgGEWRRDVAFAgFEVPIQM--------DISAEKM-IFGVAGiDPQRRDELIKVLDI------DISWRLHK 156
Cdd:COG1123 331 KLSRRSL----RELRRRVQMV-FQDPYSSlnprmtvgDIIAEPLrLHGLLS-RAERRERVAELLERvglppdLADRYPHE 404
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 157 VSDGQRRRVQICMGL-LKPfKVLLLDEITVDLDVLARADLLKFLRKECEERGATIIYATH 215
Cdd:COG1123 405 LSGGQRQRVAIARALaLEP-KLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISH 463
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
14-236 |
5.75e-17 |
|
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: 78.32 E-value: 5.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 14 VEISGLRFTYPGidghpppGSKPLIEDFSITLNSSDrCL-LVGSNGAGKTTILKILGG------------KHMVEPHMVR 80
Cdd:cd03263 1 LQIRNLTKTYKK-------GTKPAVDDLSLNVYKGE-IFgLLGHNGAGKTTTLKMLTGelrptsgtayinGYSIRTDRKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 81 VLGRSAF---HDT---GLTSSgDLCYLggewrrdvaFAGFE-VPI-QMDISAEKMIFGVagidpqrrdELIKVLDidisW 152
Cdd:cd03263 73 ARQSLGYcpqFDAlfdELTVR-EHLRF---------YARLKgLPKsEIKEEVELLLRVL---------GLTDKAN----K 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 153 RLHKVSDGQRRRVQICMGLLKPFKVLLLDEITVDLDVLARADLLKFLRKECEERgaTIIYATHIFDGLEDWPTHIVYVAN 232
Cdd:cd03263 130 RARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMSD 207
|
....
gi 7406423 233 GKLQ 236
Cdd:cd03263 208 GKLR 211
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
13-235 |
6.36e-17 |
|
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: 81.35 E-value: 6.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 13 TVEISGLRFTYPGidghpppGSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGkhMVEPH--MVRVLGRSAFHdt 90
Cdd:COG4987 333 SLELEDVSFRYPG-------AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLR--FLDPQsgSITLGGVDLRD-- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 91 gltssgdlcYLGGEWRRDVAFAGFEVPIqMDIS-AEKMIFGVAGIDPqrrDELIKVLDIDiswRLHK------------- 156
Cdd:COG4987 402 ---------LDEDDLRRRIAVVPQRPHL-FDTTlRENLRLARPDATD---EELWAALERV---GLGDwlaalpdgldtwl 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 157 ------VSDGQRRRVQICMGLLKPFKVLLLDEITVDLDVLARADLLKFLRKECEERgaTIIYATHIFDGLEdWPTHIVYV 230
Cdd:COG4987 466 geggrrLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLAGLE-RMDRILVL 542
|
....*
gi 7406423 231 ANGKL 235
Cdd:COG4987 543 EDGRI 547
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
12-215 |
2.45e-16 |
|
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: 79.64 E-value: 2.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 12 STVEISGLRFTYPGIDghpppgskPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGkhMVEPH--MVRVLGRSAfhd 89
Cdd:TIGR02857 320 SSLEFSGVSVAYPGRR--------PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLG--FVDPTegSIAVNGVPL--- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 90 TGLTSSGdlcylggeWRRDVAFAGfEVPIQMDIS-AEKMIFGVAGIDPQ--RR-------DELIKVLDIDISWRL----H 155
Cdd:TIGR02857 387 ADADADS--------WRDQIAWVP-QHPFLFAGTiAENIRLARPDASDAeiREaleraglDEFVAALPQGLDTPIgeggA 457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 156 KVSDGQRRRVQICMGLLKPFKVLLLDEITVDLDVLARADLLKFLRKECeeRGATIIYATH 215
Cdd:TIGR02857 458 GLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA--QGRTVLLVTH 515
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
14-234 |
3.65e-16 |
|
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: 74.73 E-value: 3.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 14 VEISGLRFTYPGidghpppGSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGkhMVEPhmvrvlgrsafhdtglt 93
Cdd:cd03228 1 IEFKNVSFSYPG-------RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLR--LYDP----------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 94 SSGDLCYLG--------GEWRRDVAFagfeVPiQmdisaekmifgvagiDPQRRDELIK--VLdidiswrlhkvSDGQRR 163
Cdd:cd03228 55 TSGEILIDGvdlrdldlESLRKNIAY----VP-Q---------------DPFLFSGTIRenIL-----------SGGQRQ 103
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7406423 164 RVQICMGLLKPFKVLLLDEITVDLDVLARADLLKFLRKECEERgaTIIYATHIFDGLEDWpTHIVYVANGK 234
Cdd:cd03228 104 RIAIARALLRDPPILILDEATSALDPETEALILEALRALAKGK--TVIVIAHRLSTIRDA-DRIIVLDDGR 171
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
14-235 |
1.36e-15 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 75.13 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 14 VEISGLRFTYpgidghpppGSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILK-ILGgkhMVEPH--MVRVLGRSAFHDt 90
Cdd:COG1121 7 IELENLTVSY---------GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKaILG---LLPPTsgTVRLFGKPPRRA- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 91 gltssgdlcylggewRRDVAFagfeVP--IQMD----ISAEKMIfgVAGIDPQRR-------------DELIKVLDID-- 149
Cdd:COG1121 74 ---------------RRRIGY----VPqrAEVDwdfpITVRDVV--LMGRYGRRGlfrrpsradreavDEALERVGLEdl 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 150 ISWRLHKVSDGQRRRVQICMGLLKPFKVLLLDEITVDLDVLARADLLKFLRKECEErGATIIYATHIFDGLEDWPTHIVY 229
Cdd:COG1121 133 ADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLL 211
|
....*.
gi 7406423 230 VANGKL 235
Cdd:COG1121 212 LNRGLV 217
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
14-234 |
2.04e-15 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 72.10 E-value: 2.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 14 VEISGLRFTYpgidghpppGSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGKhmVEPHmvrvlgrsafhdtglt 93
Cdd:cd03221 1 IELENLSKTY---------GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGE--LEPD---------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 94 sSGDLcylggEWRRDVAFAGFEvpiQMdisaekmifgvagidpqrrdelikvldidiswrlhkvSDGQRRRVQICMGLLK 173
Cdd:cd03221 54 -EGIV-----TWGSTVKIGYFE---QL-------------------------------------SGGEKMRLALAKLLLE 87
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7406423 174 PFKVLLLDEITVDLDVLARADLLKFLRkecEERGaTIIYATHIFDGLEDWPTHIVYVANGK 234
Cdd:cd03221 88 NPNLLLLDEPTNHLDLESIEALEEALK---EYPG-TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
12-242 |
3.62e-15 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 75.11 E-value: 3.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 12 STVEISGLRFTYpgidghpppGSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGkhmvephmvrvlgrsaFHDtg 91
Cdd:COG3839 2 ASLELENVSKSY---------GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAG----------------LED-- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 92 lTSSGDLcYLGGE-------WRRDVAFAgFEVPI---QMDIsAEKMIFG--VAGIDPQRRDELIK-VLDI-DISWRLHK- 156
Cdd:COG3839 55 -PTSGEI-LIGGRdvtdlppKDRNIAMV-FQSYAlypHMTV-YENIAFPlkLRKVPKAEIDRRVReAAELlGLEDLLDRk 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 157 ---VSDGQRRRVQICMGLLKPFKVLLLDEITVDLDVLARADLLKFLRKECEERGATIIYATHifDGLE-----DwptHIV 228
Cdd:COG3839 131 pkqLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTH--DQVEamtlaD---RIA 205
|
250
....*....|....*
gi 7406423 229 YVANGKL-QLALPME 242
Cdd:COG3839 206 VMNDGRIqQVGTPEE 220
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
14-215 |
3.96e-15 |
|
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: 72.94 E-value: 3.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 14 VEISGLRFTYpgidghpppGSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGkhMVEPhmvrvlgrsafhdtglt 93
Cdd:cd03259 1 LELKGLSKTY---------GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAG--LERP----------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 94 SSGDLcYLGGE-------WRRDVAFAgFEVPIQMD-ISAEKMI-FG--VAGID----PQRRDELIKVLDIDI--SWRLHK 156
Cdd:cd03259 53 DSGEI-LIDGRdvtgvppERRNIGMV-FQDYALFPhLTVAENIaFGlkLRGVPkaeiRARVRELLELVGLEGllNRYPHE 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 7406423 157 VSDGQRRRVQICMGLLKPFKVLLLDEITVDLDVLARADLLKFLRKECEERGATIIYATH 215
Cdd:cd03259 131 LSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTH 189
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
53-235 |
1.92e-14 |
|
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: 71.25 E-value: 1.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 53 LVGSNGAGKTTILKILGGKHMVEPHMVRVLGRSAFHDTGlTSSGDLCYLGGEWRRDVAFAGFEvpiQMDISAEkmIFGVA 132
Cdd:cd03265 31 LLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPR-EVRRRIGIVFQDLSVDDELTGWE---NLYIHAR--LYGVP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 133 G-IDPQRRDELIKVLDI-DISWRLHKV-SDGQRRRVQICMGLLKPFKVLLLDEITVDLDVLARADLLKFLRKECEERGAT 209
Cdd:cd03265 105 GaERRERIDELLDFVGLlEAADRLVKTySGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMT 184
|
170 180
....*....|....*....|....*.
gi 7406423 210 IIYATHIFDGLEDWPTHIVYVANGKL 235
Cdd:cd03265 185 ILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
14-235 |
3.53e-14 |
|
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: 70.60 E-value: 3.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 14 VEISGLRFTYPGIDGhpppgSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGkhMVEPH--MVRVLGR--SAFHD 89
Cdd:cd03255 1 IELKNLSKTYGGGGE-----KVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGG--LDRPTsgEVRVDGTdiSKLSE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 90 TGLTssgdlcylggEWRRD---VAFAGFE-VPiqmDISAE---KMIFGVAGIDP-QRRDELIKVLD-IDISWRLHK---- 156
Cdd:cd03255 74 KELA----------AFRRRhigFVFQSFNlLP---DLTALenvELPLLLAGVPKkERRERAEELLErVGLGDRLNHypse 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7406423 157 VSDGQRRRVQICMGLLKPFKVLLLDEITVDLDVLARADLLKFLRKECEERGATIIYATHIFDgLEDWPTHIVYVANGKL 235
Cdd:cd03255 141 LSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPE-LAEYADRIIELRDGKI 218
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
15-215 |
3.73e-14 |
|
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: 70.25 E-value: 3.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 15 EISGLRFTYpgidghpppGSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILK-ILGgkhMVEPHM--VRVLGRSAFHDtg 91
Cdd:cd03235 1 EVEDLTVSY---------GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKaILG---LLKPTSgsIRVFGKPLEKE-- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 92 ltssgdlcylggewRRDVAFAG--FEVPIQMDISAE-----------KMIFGVAGIDPQRRDELIKVLDID--ISWRLHK 156
Cdd:cd03235 67 --------------RKRIGYVPqrRSIDRDFPISVRdvvlmglyghkGLFRRLSKADKAKVDEALERVGLSelADRQIGE 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 7406423 157 VSDGQRRRVQICMGLLKPFKVLLLDEITVDLDVLARADLLKFLRKECEErGATIIYATH 215
Cdd:cd03235 133 LSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTH 190
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
14-215 |
7.43e-14 |
|
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: 72.17 E-value: 7.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 14 VEISGLRFTYPgidghppPGSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGkhMVEPhmvrvlgrsafhdtglt 93
Cdd:COG2274 474 IELENVSFRYP-------GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLG--LYEP----------------- 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 94 SSGDLcYLGG---------EWRRDVAFagfeVPiQmDIS------AEKMIFGVAGIDpqrRDELIKVLDI-----DISwR 153
Cdd:COG2274 528 TSGRI-LIDGidlrqidpaSLRRQIGV----VL-Q-DVFlfsgtiRENITLGDPDAT---DEEIIEAARLaglhdFIE-A 596
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7406423 154 L-----HKVSD-------GQRRRVQICMGLLKPFKVLLLDEITVDLDVLARADLLKFLRKECeeRGATIIYATH 215
Cdd:COG2274 597 LpmgydTVVGEggsnlsgGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLL--KGRTVIIIAH 668
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
33-234 |
2.84e-13 |
|
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: 67.21 E-value: 2.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 33 GSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGkhMVEPhmvrVLGRSAFHDTGLTSSGDLCylgGEWRRDVA-- 110
Cdd:cd03229 11 GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAG--LEEP----DSGSILIDGEDLTDLEDEL---PPLRRRIGmv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 111 FAGFEVPIQMDIsAEKMIFGVAGidpqrrdelikvldidiswrlhkvsdGQRRRVQICMGLLKPFKVLLLDEITVDLDVL 190
Cdd:cd03229 82 FQDFALFPHLTV-LENIALGLSG--------------------------GQQQRVALARALAMDPDVLLLDEPTSALDPI 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 7406423 191 ARADLLKFLRKECEERGATIIYATHIFDGLEDWPTHIVYVANGK 234
Cdd:cd03229 135 TRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
33-237 |
3.37e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 70.09 E-value: 3.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 33 GSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGkhMVEPHMVRVlgrsaFHDTGLTssgdLCYL-----GGEWR- 106
Cdd:COG0488 9 GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAG--ELEPDSGEV-----SIPKGLR----IGYLpqeppLDDDLt 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 107 -RDVAFAGF----EVPIQMDISAEKMIFGVAGID-----------------PQRRDELIKVLDIDISWRLHKVSD---GQ 161
Cdd:COG0488 78 vLDTVLDGDaelrALEAELEELEAKLAEPDEDLErlaelqeefealggweaEARAEEILSGLGFPEEDLDRPVSElsgGW 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7406423 162 RRRVQICMGLLKPFKVLLLDEITVDLDVLARADLLKFLRKeceeRGATIIYATH--IFdgLEDWPTHIVYVANGKLQL 237
Cdd:COG0488 158 RRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKN----YPGTVLVVSHdrYF--LDRVATRILELDRGKLTL 229
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
33-215 |
7.68e-13 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 66.10 E-value: 7.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 33 GSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGkhmVEPHM---VRVLG---------RSAFHDTGLTSSGDLCY 100
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAG---VLRPTsgtVRRAGgarvayvpqRSEVPDSLPLTVRDLVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 101 LG-----GEWRRDVAFAgfevpiQMDISAEKMIFGVAGIDPQRRDELikvldidiswrlhkvSDGQRRRVQICMGLLKPF 175
Cdd:NF040873 80 MGrwarrGLWRRLTRDD------RAAVDDALERVGLADLAGRQLGEL---------------SGGQRQRALLAQGLAQEA 138
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 7406423 176 KVLLLDEITVDLDVLARADLLKFLRKECeERGATIIYATH 215
Cdd:NF040873 139 DLLLLDEPTTGLDAESRERIIALLAEEH-ARGATVVVVTH 177
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
14-235 |
9.68e-13 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 66.09 E-value: 9.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 14 VEISGLRFTYpgidghpppGSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILggkhmvephmvrvlgrsafhdTGLT 93
Cdd:cd03268 1 LKTNDLTKTY---------GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKII---------------------LGLI 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 94 --SSGDLCYLGGEWRRDVAFAG-----FEVPI-QMDISAE---KMIFGVAGIDPQRRDELIKV--LDIDISWRLHKVSDG 160
Cdd:cd03268 51 kpDSGEITFDGKSYQKNIEALRrigalIEAPGfYPNLTARenlRLLARLLGIRKKRIDEVLDVvgLKDSAKKKVKGFSLG 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7406423 161 QRRRVQICMGLLKPFKVLLLDEITVDLDVLARADLLKFLRKECEErGATIIYATHIFDGLEDWPTHIVYVANGKL 235
Cdd:cd03268 131 MKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
38-185 |
1.12e-12 |
|
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: 64.59 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 38 IEDFSITLNSSDRCLLVGSNGAGKTTILKILGGKHMVEPHMVRVLGRsAFHDTGLTSsgdlcylggeWRRDVAFAGFEVP 117
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQ-DLTDDERKS----------LRKEIGYVFQDPQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 118 IQMDISAEKMIFGVAGI-------DPQRRDELIKVLDID------ISWRLHKVSDGQRRRVQICMGLLKPFKVLLLDEIT 184
Cdd:pfam00005 70 LFPRLTVRENLRLGLLLkglskreKDARAEEALEKLGLGdladrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
.
gi 7406423 185 V 185
Cdd:pfam00005 150 A 150
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
10-235 |
1.63e-12 |
|
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: 67.86 E-value: 1.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 10 RNSTVEISGLRFTYPGidghpppgSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGkhMVEPhmvrvlgrsafhd 89
Cdd:COG4988 333 GPPSIELEDVSFSYPG--------GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLG--FLPP------------- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 90 tgltSSGDLcYLGG---------EWRRDVAFAG-----FEVPIqmdisAEKMIFGVAGIDPQ------RR---DELIKVL 146
Cdd:COG4988 390 ----YSGSI-LINGvdlsdldpaSWRRQIAWVPqnpylFAGTI-----RENLRLGRPDASDEeleaalEAaglDEFVAAL 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 147 ----DIDISWRLHKVSDGQRRRVQICMGLLKPFKVLLLDEITVDLDVLARADLLKFLRKECEERgaTIIYATHIFDGLED 222
Cdd:COG4988 460 pdglDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALLAQ 537
|
250
....*....|...
gi 7406423 223 WpTHIVYVANGKL 235
Cdd:COG4988 538 A-DRILVLDDGRI 549
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
11-234 |
1.93e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 66.30 E-value: 1.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 11 NSTVEISGLRFTYPGidghpppGSKPLiEDFSITLNSSDRCLLVGSNGAGKTTILKILGGKHMVEPHMVRVLGRSAFHDT 90
Cdd:PRK13647 2 DNIIEVEDLHFRYKD-------GTKAL-KGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAEN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 91 --------GLT--SSGDLCYLGGEWrRDVAFAgfevPIQMDISAEKMIfgvagidpQRRDELIKVLDIdisWRL-----H 155
Cdd:PRK13647 74 ekwvrskvGLVfqDPDDQVFSSTVW-DDVAFG----PVNMGLDKDEVE--------RRVEEALKAVRM---WDFrdkppY 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7406423 156 KVSDGQRRRVQICMGLLKPFKVLLLDEITVDLDVLARADLLKFLrKECEERGATIIYATHIFDGLEDWPTHIVYVANGK 234
Cdd:PRK13647 138 HLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEIL-DRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGR 215
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
33-216 |
4.28e-12 |
|
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: 64.30 E-value: 4.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 33 GSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGkhMVEPhmvrVLGRSAFHDTgltssgDLCYLGGEWRRDVAFA 112
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAG--LLRP----DSGEVRWNGT------PLAEQRDEPHENILYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 113 GFEVPIQMDISA-EKMIFGVAGIDPQRR---DELIKVLDIDISWRL-HKVSDGQRRRVQICMGLLKPFKVLLLDEITVDL 187
Cdd:TIGR01189 79 GHLPGLKPELSAlENLHFWAAIHGGAQRtieDALAAVGLTGFEDLPaAQLSAGQQRRLALARLWLSRRPLWILDEPTTAL 158
|
170 180
....*....|....*....|....*....
gi 7406423 188 DVLARADLLKFLRKECeERGATIIYATHI 216
Cdd:TIGR01189 159 DKAGVALLAGLLRAHL-ARGGIVLLTTHQ 186
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
8-215 |
5.39e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 65.01 E-value: 5.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 8 KKRNSTVEISGLRFTYPgidghppPGSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGkhMVEPHMVRVlgrsaF 87
Cdd:PRK13632 2 KNKSVMIKVENVSFSYP-------NSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTG--LLKPQSGEI-----K 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 88 HDTGLTSSGDLCYLggewRR---------DVAFAGfevpiqmdISAEKMI-FGVAG--IDPQRRDELIK--VLDIDISWR 153
Cdd:PRK13632 68 IDGITISKENLKEI----RKkigiifqnpDNQFIG--------ATVEDDIaFGLENkkVPPKKMKDIIDdlAKKVGMEDY 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7406423 154 L----HKVSDGQRRRVQICMGL-LKPfKVLLLDEITVDLDVLARADLLKFLRKECEERGATIIYATH 215
Cdd:PRK13632 136 LdkepQNLSGGQKQRVAIASVLaLNP-EIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITH 201
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
53-236 |
5.79e-12 |
|
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: 64.14 E-value: 5.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 53 LVGSNGAGKTTILKILGGkhMVEPhmvrVLGRSAFHDTGLTSSGDlcylggEWRRDVAFAGFEVPIQMDISAEKMIFGVA 132
Cdd:cd03264 30 LLGPNGAGKTTLMRILAT--LTPP----SSGTIRIDGQDVLKQPQ------KLRRRIGYLPQEFGVYPNFTVREFLDYIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 133 ---GIDPQRRDELI-KVLD-IDISWRLHK----VSDGQRRRVQICMGLLKPFKVLLLDEITVDLDVLARADLLKFLRKEC 203
Cdd:cd03264 98 wlkGIPSKEVKARVdEVLElVNLGDRAKKkigsLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELG 177
|
170 180 190
....*....|....*....|....*....|...
gi 7406423 204 EERgaTIIYATHIFDGLEDWPTHIVYVANGKLQ 236
Cdd:cd03264 178 EDR--IVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
10-218 |
6.25e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 65.21 E-value: 6.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 10 RNSTVEISGLRFTYPGidghpppGSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGkhMVEPH-----MVRVLGR 84
Cdd:PRK13640 2 KDNIVEFKHVSFTYPD-------SKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLING--LLLPDdnpnsKITVDGI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 85 SAFHDT--------GLT-SSGDLCYLGGEWRRDVAFaGFEvpiQMDISAEKMIFGVagidpqrRDELIKVLDID-ISWRL 154
Cdd:PRK13640 73 TLTAKTvwdirekvGIVfQNPDNQFVGATVGDDVAF-GLE---NRAVPRPEMIKIV-------RDVLADVGMLDyIDSEP 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7406423 155 HKVSDGQRRRVQICmGLL--KPfKVLLLDEITVDLDVLARADLLKFLRKECEERGATIIYATHIFD 218
Cdd:PRK13640 142 ANLSGGQKQRVAIA-GILavEP-KIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDID 205
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
14-237 |
1.10e-11 |
|
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: 62.72 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 14 VEISGLRFTYPgidghppPGSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILggkhmvephmvrvlgrsafhdtglt 93
Cdd:cd03247 1 LSINNVSFSYP-------EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLL------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 94 sSGDLCYLGGEwrrdVAFAGFEVPIQMDISAEKMifgvaGIDPQRRDELIKVLDIDISWRLhkvSDGQRRRVQICMGLLK 173
Cdd:cd03247 49 -TGDLKPQQGE----ITLDGVPVSDLEKALSSLI-----SVLNQRPYLFDTTLRNNLGRRF---SGGERQRLALARILLQ 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7406423 174 PFKVLLLDEITVDLDVLARADLLKFLRKECEERgaTIIYATHIFDGLEDWpTHIVYVANGKLQL 237
Cdd:cd03247 116 DAPIVLLDEPTVGLDPITERQLLSLIFEVLKDK--TLIWITHHLTGIEHM-DKILFLENGKIIM 176
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
14-199 |
1.69e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 64.70 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 14 VEISGLRFTYpgidghpppGSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGKhmVEP--------HMVRV---- 81
Cdd:COG0488 316 LELEGLSKSY---------GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGE--LEPdsgtvklgETVKIgyfd 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 82 -------LGRSAFhdtgltssgdlcylggEWRRDVAFAGFEVPI-QMdisAEKMIFgvagiDPQRRDELIKVLdidiswr 153
Cdd:COG0488 385 qhqeeldPDKTVL----------------DELRDGAPGGTEQEVrGY---LGRFLF-----SGDDAFKPVGVL------- 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 7406423 154 lhkvSDGQRRRVQICMGLLKPFKVLLLDEITVDLDVLARADLLKFL 199
Cdd:COG0488 434 ----SGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEAL 475
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
15-235 |
1.81e-11 |
|
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: 62.66 E-value: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 15 EISGLRFTYPGidghpppgSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGkhMVEPHMVRVLgrsafhdtglts 94
Cdd:cd03226 1 RIENISFSYKK--------GTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAG--LIKESSGSIL------------ 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 95 sgdlcyLGGEW------RRDVAFAGFEVPIQ--MDISAEKMIFGV--AGIDPQRRDELIKVLDIDI--SWRLHKVSDGQR 162
Cdd:cd03226 59 ------LNGKPikakerRKSIGYVMQDVDYQlfTDSVREELLLGLkeLDAGNEQAETVLKDLDLYAlkERHPLSLSGGQK 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7406423 163 RRVQICMGLLKPFKVLLLDEITVDLDvLARADLLKFLRKECEERGATIIYATHIFDGLEDWPTHIVYVANGKL 235
Cdd:cd03226 133 QRLAIAAALLSGKDLLIFDEPTSGLD-YKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
13-215 |
2.14e-11 |
|
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: 64.69 E-value: 2.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 13 TVEISGLRFTYPGidghpppgSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGkhMVEPHMVRVLgrsafhdtgL 92
Cdd:TIGR02868 334 TLELRDLSAGYPG--------APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAG--LLDPLQGEVT---------L 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 93 TSSGDLCYLGGEWRRDVAFAGFEVPIQMDISAEKMIFGVAGIDPQ------RR-------DELIKVLDIDISWRLHKVSD 159
Cdd:TIGR02868 395 DGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEelwaalERvgladwlRALPDGLDTVLGEGGARLSG 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 7406423 160 GQRRRVQICMGLLKPFKVLLLDEITVDLDVLARADLLKFLRKECEERgaTIIYATH 215
Cdd:TIGR02868 475 GERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGR--TVVLITH 528
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
33-236 |
2.42e-11 |
|
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: 62.27 E-value: 2.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 33 GSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGkhMVEPhmvrvlgrsafhdtgltSSGDLcYLGGE-------W 105
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAG--LEEP-----------------TSGRI-YIGGRdvtdlppK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 106 RRDVA--FAGFEVPIQMDIsAEKMIFGV-------AGIDpQRRDELIKVLDID--ISWRLHKVSDGQRRRVQICMGLLKP 174
Cdd:cd03301 71 DRDIAmvFQNYALYPHMTV-YDNIAFGLklrkvpkDEID-ERVREVAELLQIEhlLDRKPKQLSGGQRQRVALGRAIVRE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7406423 175 FKVLLLDEITVDLDVLARADLLKFLRKECEERGATIIYATHIFDGLEDWPTHIVYVANGKLQ 236
Cdd:cd03301 149 PKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
11-215 |
2.60e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 62.88 E-value: 2.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 11 NSTVEISGLRFTYPGidghpppgsKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGKHMvephmvrvlgrsafhdt 90
Cdd:PRK10575 9 DTTFALRNVSFRVPG---------RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQP----------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 91 glTSSGDLCYLG---GEWR-----RDVAFAGFEVPiqmdiSAEKMI------------------FGVAgiDPQRRDELIK 144
Cdd:PRK10575 63 --PSEGEILLDAqplESWSskafaRKVAYLPQQLP-----AAEGMTvrelvaigrypwhgalgrFGAA--DREKVEEAIS 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7406423 145 VLDID-ISWRL-HKVSDGQRRRVQICMGLLKPFKVLLLDEITVDLDVLARADLLKFLRKECEERGATIIYATH 215
Cdd:PRK10575 134 LVGLKpLAHRLvDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLH 206
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
14-235 |
2.82e-11 |
|
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: 62.13 E-value: 2.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 14 VEISGLRFTYpgidghpppGSKPLieDFSITLNSSDRCLLVGSNGAGKTTILKILGGKHMVEPHMVRVLGR--------- 84
Cdd:cd03298 1 VRLDKIRFSY---------GEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVdvtaappad 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 85 ----------------SAFHDTGLTSSGDLcYLGGEWRRdvafagfevpiQMDISAEKMifGVAGIDPQRRDELikvldi 148
Cdd:cd03298 70 rpvsmlfqennlfahlTVEQNVGLGLSPGL-KLTAEDRQ-----------AIEVALARV--GLAGLEKRLPGEL------ 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 149 diswrlhkvSDGQRRRVQICMGLLKPFKVLLLDEITVDLDVLARADLLKFLRKECEERGATIIYATHIFDGLEDWPTHIV 228
Cdd:cd03298 130 ---------SGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVV 200
|
....*..
gi 7406423 229 YVANGKL 235
Cdd:cd03298 201 FLDNGRI 207
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
33-235 |
3.35e-11 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 62.34 E-value: 3.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 33 GSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILggkhmvephmVRVL----GRSAFHDTGLTSSGDlcylgGEWRRD 108
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCF----------ARLLtpqsGTVFLGDKPISMLSS-----RQLARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 109 VAFAGFEVPIQMDISAEKMI----------FG-VAGIDPQRRDELIKVLDID--ISWRLHKVSDGQRRRVQICMGLLKPF 175
Cdd:PRK11231 78 LALLPQHHLTPEGITVRELVaygrspwlslWGrLSAEDNARVNQAMEQTRINhlADRRLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 176 KVLLLDEITVDLDVLARADLLKFLRkECEERGATIIYATHIFDGLEDWPTHIVYVANGKL 235
Cdd:PRK11231 158 PVVLLDEPTTYLDINHQVELMRLMR-ELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHV 216
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
11-218 |
4.62e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 62.34 E-value: 4.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 11 NSTVEISGLRFTYPGidghpppGSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGKHMVEPHMVRVLGRSAFHDT 90
Cdd:PRK13635 3 EEIIRVEHISFRYPD-------AATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEET 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 91 --------GLT-SSGDLCYLGGEWRRDVAFaGFE---VPiqmdisaekmifgvagidpqrRDELIKVLDidisWRLHKV- 157
Cdd:PRK13635 76 vwdvrrqvGMVfQNPDNQFVGATVQDDVAF-GLEnigVP---------------------REEMVERVD----QALRQVg 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7406423 158 ------------SDGQRRRVQICMGL-LKPfKVLLLDEITVDLDVLARADLLKFLRKECEERGATIIYATHIFD 218
Cdd:PRK13635 130 medflnrephrlSGGQKQRVAIAGVLaLQP-DIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLD 202
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
33-235 |
7.69e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 61.74 E-value: 7.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 33 GSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGkhMVEPHMVRVLGRSA------FHD----TGLT-SSGDLCYL 101
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNG--ILKPTSGSVLIRGEpitkenIREvrkfVGLVfQNPDDQIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 102 GGEWRRDVAFAgfevPIQMDISAEKMifgvagidPQRRDELIKVLDI-DISWRL-HKVSDGQRRRVQICMGLLKPFKVLL 179
Cdd:PRK13652 93 SPTVEQDIAFG----PINLGLDEETV--------AHRVSSALHMLGLeELRDRVpHHLSGGEKKRVAIAGVIAMEPQVLV 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 7406423 180 LDEITVDLDVLARADLLKFLRKECEERGATIIYATHIFDGLEDWPTHIVYVANGKL 235
Cdd:PRK13652 161 LDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRI 216
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
15-234 |
9.95e-11 |
|
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: 61.04 E-value: 9.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 15 EISGLRFTYPGidghpppgSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGkhMVEPhmvrVLGRSAFHDTGLTS 94
Cdd:cd03256 2 EVENLSKTYPN--------GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNG--LVEP----TSGSVLIDGTDINK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 95 sgdlcyLGGE----WRRDVA--FAGFEVPIQMDI------------SAEKMIFG-VAGIDPQRRDELIKVLDID--ISWR 153
Cdd:cd03256 68 ------LKGKalrqLRRQIGmiFQQFNLIERLSVlenvlsgrlgrrSTWRSLFGlFPKEEKQRALAALERVGLLdkAYQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 154 LHKVSDGQRRRVQICMGLLKPFKVLLLDEITVDLDVLARADLLKFLRKECEERGATIIYATHIFDGLEDWPTHIVYVANG 233
Cdd:cd03256 142 ADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDG 221
|
.
gi 7406423 234 K 234
Cdd:cd03256 222 R 222
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
33-216 |
1.36e-10 |
|
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: 59.81 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 33 GSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGkhMVEPHMVRVLgrsafhdtglTSSGDLCYLGGEWRRDVAFA 112
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAG--LSPPLAGRVL----------LNGGPLDFQRDSIARGLLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 113 GFEVPIQMDISA-EKMIFGVAGIDpqrRDELIKVLDiDISWR------LHKVSDGQRRRVQICMGLLKPFKVLLLDEITV 185
Cdd:cd03231 79 GHAPGIKTTLSVlENLRFWHADHS---DEQVEEALA-RVGLNgfedrpVAQLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170 180 190
....*....|....*....|....*....|.
gi 7406423 186 DLDVLARADLLKFLRKECeERGATIIYATHI 216
Cdd:cd03231 155 ALDKAGVARFAEAMAGHC-ARGGMVVLTTHQ 184
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
35-230 |
1.51e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 59.97 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 35 KPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGKHmvephmvrvlgrsafhdTGLTSSGDLCYLGGEWRRDVAFAGf 114
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAL-----------------KGTPVAGCVDVPDNQFGREASLID- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 115 EVPIQMDISAEKMIFGVAGI-DPQ--RRdelikvldidiswRLHKVSDGQRRRVQICMGLLKPFKVLLLDEITVDLD--- 188
Cdd:COG2401 105 AIGRKGDFKDAVELLNAVGLsDAVlwLR-------------RFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDrqt 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 7406423 189 --VLARAdllkfLRKECEERGATIIYATHIFDgLEDW--PTHIVYV 230
Cdd:COG2401 172 akRVARN-----LQKLARRAGITLVVATHHYD-VIDDlqPDLLIFV 211
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
40-236 |
1.53e-10 |
|
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: 60.00 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 40 DFSITLN---SSDRCLLVGSNGAGKTTILKILGGKHMVEPhmvrvlGRSAFHDTGLTSSGDLCYLGGEwRRDVAF----- 111
Cdd:cd03297 12 DFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDG------GTIVLNGTVLFDSRKKINLPPQ-QRKIGLvfqqy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 112 AGFEvpiQMDIsAEKMIFGVAGIDP----QRRDELIKVLDID--ISWRLHKVSDGQRRRVQICMGLLKPFKVLLLDEITV 185
Cdd:cd03297 85 ALFP---HLNV-RENLAFGLKRKRNredrISVDELLDLLGLDhlLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 7406423 186 DLDVLARADLLKFLRKECEERGATIIYATHIFDGLEDWPTHIVYVANGKLQ 236
Cdd:cd03297 161 ALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
53-218 |
2.32e-10 |
|
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: 58.21 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 53 LVGSNGAGKTTILKILGGkhMVEPhmvrvlgrsafhDTGltssgdlcylggewrrDVAFAGFEVPIQMDISAEKmifgvA 132
Cdd:cd03216 31 LLGENGAGKSTLMKILSG--LYKP------------DSG----------------EILVDGKEVSFASPRDARR-----A 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 133 GIdpqrrdELIkvldidiswrlHKVSDGQRRRVQICMGLLKPFKVLLLDEITVDLDVLARADLLKFLRKECeERGATIIY 212
Cdd:cd03216 76 GI------AMV-----------YQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLR-AQGVAVIF 137
|
....*.
gi 7406423 213 ATHIFD 218
Cdd:cd03216 138 ISHRLD 143
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
14-215 |
5.02e-10 |
|
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: 58.64 E-value: 5.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 14 VEISGLRFTYPGidghpPPGSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGKHMVEPHMVRVLGRSAF---HDT 90
Cdd:cd03293 1 LEVRNVSKTYGG-----GGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTgpgPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 91 GLTSSGDLCYlggEWR--RD-VAFaGFEVPiqmdisaekmifGVAGIDPQRR-DELIKVLDIDISWRL--HKVSDGQRRR 164
Cdd:cd03293 76 GYVFQQDALL---PWLtvLDnVAL-GLELQ------------GVPKAEARERaEELLELVGLSGFENAypHQLSGGMRQR 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 7406423 165 VQICMGL-LKPfKVLLLDEITVDLDVLARADLLKFLRKECEERGATIIYATH 215
Cdd:cd03293 140 VALARALaVDP-DVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTH 190
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
44-220 |
8.17e-10 |
|
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: 58.19 E-value: 8.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 44 TLNSSDRCLLVGSNGAGKTTILKILGGKhmVEPhmvrvlgrsafhdtgltSSGDLcylgGEWRRDVAFAGFEVPIQMDIS 123
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGV--LKP-----------------DEGDI----EIELDTVSYKPQYIKADYEGT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 124 AEKMIFGV---AGIDPQRRDELIKVLDID--ISWRLHKVSDGQRRRVQICMGLLKPFKVLLLDEITVDLDVLARADLLKF 198
Cdd:cd03237 78 VRDLLSSItkdFYTHPYFKTEIAKPLQIEqiLDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKV 157
|
170 180
....*....|....*....|....*....
gi 7406423 199 LRKECEERGAT-------IIYATHIFDGL 220
Cdd:cd03237 158 IRRFAENNEKTafvvehdIIMIDYLADRL 186
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
12-215 |
1.03e-09 |
|
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: 57.18 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 12 STVEISGLRFTYPGIDGhppPGSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGKHmvephmvrvlgrsafhdTG 91
Cdd:cd03213 2 VTLSFRNLTVTVKSSPS---KSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRR-----------------TG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 92 LTSSGDLcYLGG------EWRRDVAFagfeVPiQMDIsaekmifgvagidpqrrdeLIKVLDI----DISWRLHKVSDGQ 161
Cdd:cd03213 62 LGVSGEV-LINGrpldkrSFRKIIGY----VP-QDDI-------------------LHPTLTVretlMFAAKLRGLSGGE 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 7406423 162 RRRVQICMGLLKPFKVLLLDEITVDLDVLARADLLKFLRKECEErGATIIYATH 215
Cdd:cd03213 117 RKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIH 169
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
14-188 |
1.46e-09 |
|
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: 57.24 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 14 VEISGLRFTYPGiDGhpppgsKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGKHMVEPHMVRVLGRsafhdtglt 93
Cdd:cd03251 1 VEFKNVTFRYPG-DG------PPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGH--------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 94 ssgDLCYLG-GEWRRDVAFAGFEVPIQMDISAEKMIFGVAGIDPQR---------RDELIKVL----DIDISWRLHKVSD 159
Cdd:cd03251 65 ---DVRDYTlASLRRQIGLVSQDVFLFNDTVAENIAYGRPGATREEveeaaraanAHEFIMELpegyDTVIGERGVKLSG 141
|
170 180
....*....|....*....|....*....
gi 7406423 160 GQRRRVQICMGLLKPFKVLLLDEITVDLD 188
Cdd:cd03251 142 GQRQRIAIARALLKDPPILILDEATSALD 170
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
33-215 |
2.14e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 56.35 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 33 GSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGkhmvephmvrvLGRSAfhdtgltsSGDLCYLG-------GEW 105
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAG-----------LARPD--------AGEVLWQGepirrqrDEY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 106 RRDVAFAGFEVPIQMDISA-EKMIFGVAGIDPQRRDELIKVLD-IDISWRL----HKVSDGQRRRVQICMGLLKPFKVLL 179
Cdd:PRK13538 73 HQDLLYLGHQPGIKTELTAlENLRFYQRLHGPGDDEALWEALAqVGLAGFEdvpvRQLSAGQQRRVALARLWLTRAPLWI 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 7406423 180 LDEITVDLDVLARADLLKFLRKECeERGATIIYATH 215
Cdd:PRK13538 153 LDEPFTAIDKQGVARLEALLAQHA-EQGGMVILTTH 187
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
114-235 |
2.19e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 57.79 E-value: 2.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 114 FEVPIQMDIsaekmIFGVA--GIDPQ----RRDELIKVLDIDISWrLHK----VSDGQRRRVQICMGLLKPFKVLLLDEI 183
Cdd:PRK13651 119 FEQTIEKDI-----IFGPVsmGVSKEeakkRAAKYIELVGLDESY-LQRspfeLSGGQKRRVALAGILAMEPDFLVFDEP 192
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 7406423 184 TVDLDVLARADLLKFLrKECEERGATIIYATHIFDGLEDWPTHIVYVANGKL 235
Cdd:PRK13651 193 TAGLDPQGVKEILEIF-DNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKI 243
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
14-215 |
3.87e-09 |
|
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: 56.05 E-value: 3.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 14 VEISGLRFTYPGidghpPPGSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGKHMVEPHMVRVLGRsafhDTGLT 93
Cdd:cd03258 2 IELKNVSKVFGD-----TGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGT----DLTLL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 94 SSGDLCylggEWRRDVA--FAGFevpiqmDISAEKMIFG-------VAGID----PQRRDELIKVLDIDiswrlHKV--- 157
Cdd:cd03258 73 SGKELR----KARRRIGmiFQHF------NLLSSRTVFEnvalpleIAGVPkaeiEERVLELLELVGLE-----DKAday 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7406423 158 ----SDGQRRRVQICMGLLKPFKVLLLDEITVDLDVLARADLLKFLRKECEERGATIIYATH 215
Cdd:cd03258 138 paqlSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITH 199
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
33-238 |
5.47e-09 |
|
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: 55.36 E-value: 5.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 33 GSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGkhMVEPH--MVRVLGRSAFHDTGltssGDLCYLGGE---WRR 107
Cdd:cd03269 11 GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILG--IILPDsgEVLFDGKPLDIAAR----NRIGYLPEErglYPK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 108 dvafagfevpiqMDIsAEKMIF-----GVAGIDPQRR-DELIKVLDIDISW--RLHKVSDGQRRRVQICMGLLKPFKVLL 179
Cdd:cd03269 85 ------------MKV-IDQLVYlaqlkGLKKEEARRRiDEWLERLELSEYAnkRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 7406423 180 LDEITVDLDVLArADLLKFLRKECEERGATIIYATHIFDGLEDWPTHIVYVANGKLQLA 238
Cdd:cd03269 152 LDEPFSGLDPVN-VELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLY 209
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
40-238 |
7.57e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 55.80 E-value: 7.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 40 DFSITLNSSDRCLLVGSNGAGKTTILKILGGkhMVEPHMVRV-LGRSAFhdTGLTSSGDLCYLggewRRDVA----FAG- 113
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNG--LLQPTSGTVtIGERVI--TAGKKNKKLKPL----RKKVGivfqFPEh 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 114 --FEVPIQMDISAEKMIFGVAGIDPQRR-DELIKV--LDIDIswrLHK----VSDGQRRRVQICmGLL--KPfKVLLLDE 182
Cdd:PRK13634 97 qlFEETVEKDICFGPMNFGVSEEDAKQKaREMIELvgLPEEL---LARspfeLSGGQMRRVAIA-GVLamEP-EVLVLDE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 7406423 183 ITVDLDVLARADLLKFLRKECEERGATIIYATHIFDGLEDWPTHIVYVANGKLQLA 238
Cdd:PRK13634 172 PTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQ 227
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
32-236 |
7.89e-09 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 55.06 E-value: 7.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 32 PGSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGKHMVEPHMVRVLGRsafhDTGLTSSGDLCYLggewRRD--- 108
Cdd:COG2884 12 PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQ----DLSRLKRREIPYL----RRRigv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 109 ----------------VAFAgfevpiqmdisaekMIfgVAGIDPQR-RDELIKVLD-IDISWRLHK----VSDGQRRRVQ 166
Cdd:COG2884 84 vfqdfrllpdrtvyenVALP--------------LR--VTGKSRKEiRRRVREVLDlVGLSDKAKAlpheLSGGEQQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 167 ICMGLLKPFKVLLLDEITVDLDVLARADLLKFLrKECEERGATIIYATHIFDGLEDWPTHIVYVANGKLQ 236
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPETSWEIMELL-EEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
40-238 |
8.21e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 55.91 E-value: 8.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 40 DFSITLNSSDRCLLVGSNGAGKTTILKILGGKHMVEPHMVRVlgrsafHDTGLTSSG---DLCYLggewRRDVA----FA 112
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRV------DDTLITSTSknkDIKQI----RKKVGlvfqFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 113 G---FEVPIQMDISAEKMIFGVAGIDPQRRDELiKVLDIDISWRLH-----KVSDGQRRRVQICMGLLKPFKVLLLDEIT 184
Cdd:PRK13649 95 EsqlFEETVLKDVAFGPQNFGVSQEEAEALARE-KLALVGISESLFeknpfELSGGQMRRVAIAGILAMEPKILVLDEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 7406423 185 VDLDVLARADLLKfLRKECEERGATIIYATHIFDGLEDWPTHIVYVANGKLQLA 238
Cdd:PRK13649 174 AGLDPKGRKELMT-LFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLS 226
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
38-235 |
1.02e-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: 54.85 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 38 IEDFSITLNSSDRCLLVGSNGAGKTTILKILGGkhMVEPhmvrvlgrsafhDTG-LTSSGDLCYLggewrrdVAFAGFev 116
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAG--IYPP------------DSGtVTVRGRVSSL-------LGLGGG-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 117 pIQMDISAEKMIFGVA---GIDPQRRDELIK-VLDI-----DISWRLHKVSDGQRRRVQICMGLLKPFKVLLLDEitvdl 187
Cdd:cd03220 95 -FNPELTGRENIYLNGrllGLSRKEIDEKIDeIIEFselgdFIDLPVKTYSSGMKARLAFAIATALEPDILLIDE----- 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 7406423 188 dVLARADlLKFLRKeCEER-------GATIIYATHIFDGLEDWPTHIVYVANGKL 235
Cdd:cd03220 169 -VLAVGD-AAFQEK-CQRRlrellkqGKTVILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
35-218 |
1.07e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 54.58 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 35 KPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGKHmvePHMVRVLGRSAF-----HDTGLTSSGDLCYLGGEwrrDV 109
Cdd:cd03233 20 IPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRT---EGNVSVEGDIHYngipyKEFAEKYPGEIIYVSEE---DV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 110 AFAGFEVPIQMDISAEkmifgvagidpQRRDELIKvldidiswrlhKVSDGQRRRVQICMGLLKPFKVLLLDEITVDLDV 189
Cdd:cd03233 94 HFPTLTVRETLDFALR-----------CKGNEFVR-----------GISGGERKRVSIAEALVSRASVLCWDNSTRGLDS 151
|
170 180 190
....*....|....*....|....*....|....*..
gi 7406423 190 LARADLLKFLRKECEERGATIIYA--------THIFD 218
Cdd:cd03233 152 STALEILKCIRTMADVLKTTTFVSlyqasdeiYDLFD 188
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
13-244 |
1.44e-08 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 55.62 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 13 TVEISGLRFTYpgidghpppGSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGKHMVEPHMVRVLGRSAfHDTGL 92
Cdd:PRK09536 3 MIDVSDLSVEF---------GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDV-EALSA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 93 TSSGdlcylggewrRDVAFAGFEVPIQMDISAEKMI----------FGVAGIDPQR-------RDELIKVLDIDISwrlh 155
Cdd:PRK09536 73 RAAS----------RRVASVPQDTSLSFEFDVRQVVemgrtphrsrFDTWTETDRAaverameRTGVAQFADRPVT---- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 156 KVSDGQRRRVQICMGLLKPFKVLLLDEITVDLDVLARADLLKFLRKECEErGATIIYATHIFDGLEDWPTHIVYVANGKL 235
Cdd:PRK09536 139 SLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRV 217
|
....*....
gi 7406423 236 QLALPMEKV 244
Cdd:PRK09536 218 RAAGPPADV 226
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
14-188 |
1.69e-08 |
|
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: 55.49 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 14 VEISGLRFTYPGIDghpppgsKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILggKHMVEPhmvrvlgrsafhdtglt 93
Cdd:TIGR02203 331 VEFRNVTFRYPGRD-------RPALDSISLVIEPGETVALVGRSGSGKSTLVNLI--PRFYEP----------------- 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 94 SSGDLC--------YLGGEWRRDVAFAGFEVPIQMDISAEKMIFGVAGIDPQRR--------------DELIKVLDIDIS 151
Cdd:TIGR02203 385 DSGQILldghdladYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEQADRAEieralaaayaqdfvDKLPLGLDTPIG 464
|
170 180 190
....*....|....*....|....*....|....*..
gi 7406423 152 WRLHKVSDGQRRRVQICMGLLKPFKVLLLDEITVDLD 188
Cdd:TIGR02203 465 ENGVLLSGGQRQRLAIARALLKDAPILILDEATSALD 501
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
33-235 |
1.91e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 54.61 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 33 GSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILG-------------GKHMVEPHMVRVLGRSAFHDTGLTSSGDLC 99
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSrlmtpahghvwldGEHIQHYASKEVARRIGLLAQNATTPGDIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 100 Y-------------LGGEWRRDVAFAgfevpiqmdISAEKMIFGVAGIDPQRRDELikvldidiswrlhkvSDGQRRRVQ 166
Cdd:PRK10253 98 VqelvargryphqpLFTRWRKEDEEA---------VTKAMQATGITHLADQSVDTL---------------SGGQRQRAW 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7406423 167 ICMGLLKPFKVLLLDEITVDLDVLARADLLKFLRKECEERGATIIYATHIFDGLEDWPTHIVYVANGKL 235
Cdd:PRK10253 154 IAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKI 222
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
15-215 |
2.31e-08 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 54.32 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 15 EISGLRFTYPGidghpppgsKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGkhMVEPHM-------VRVLGRSA- 86
Cdd:PRK11248 3 QISHLYADYGG---------KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAG--FVPYQHgsitldgKPVEGPGAe 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 87 ----FHDTGLTSsgdlcylggeWRR---DVAF----AGFEVPiQMDISAEKMI--FGVAGIDpQRRdelikvldidiSWR 153
Cdd:PRK11248 72 rgvvFQNEGLLP----------WRNvqdNVAFglqlAGVEKM-QRLEIAHQMLkkVGLEGAE-KRY-----------IWQ 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7406423 154 LhkvSDGQRRRVQICMGLLKPFKVLLLDEITVDLDVLARADLLKFLRKECEERGATIIYATH 215
Cdd:PRK11248 129 L---SGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITH 187
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
155-215 |
2.81e-08 |
|
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: 54.29 E-value: 2.81e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7406423 155 HKVSDGQRRRVQICMGL-LKPfKVLLLDEITVDLDVLARADLLKFLRKECEERGATIIYATH 215
Cdd:COG0444 149 HELSGGMRQRVMIARALaLEP-KLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITH 209
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-189 |
3.13e-08 |
|
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: 54.94 E-value: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 5 EEEKKRNST---------------VEISGLRFTYpgidghpppGSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILG 69
Cdd:TIGR03719 299 QEFQKRNETaeiyippgprlgdkvIEAENLTKAF---------GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMIT 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 70 GKHMVEPHMVRV-----LG-----RSAFHDTG----LTSSG-DLCYLGgewrrdvafaGFEVPIQMDISAekmiFGVAGI 134
Cdd:TIGR03719 370 GQEQPDSGTIEIgetvkLAyvdqsRDALDPNKtvweEISGGlDIIKLG----------KREIPSRAYVGR----FNFKGS 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 7406423 135 DPQRRdelIKVLdidiswrlhkvSDGQRRRVQICMGLLKPFKVLLLDEITVDLDV 189
Cdd:TIGR03719 436 DQQKK---VGQL-----------SGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV 476
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
14-235 |
6.67e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 53.20 E-value: 6.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 14 VEISGLRFTYpgiDGHPPPGSKPLIeDFSITLNSSDRCLLVGSNGAGKTTILKILGGkhMVEPHMvrvlGRSAFHDTGLT 93
Cdd:PRK13643 2 IKFEKVNYTY---QPNSPFASRALF-DIDLEVKKGSYTALIGHTGSGKSTLLQHLNG--LLQPTE----GKVTVGDIVVS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 94 SSGDLCYLGGEWRR-DVAFAG-----FEVPIQMDISAEKMIFGVAGIDPQR-RDELIKVLDIDIS-WRLH--KVSDGQRR 163
Cdd:PRK13643 72 STSKQKEIKPVRKKvGVVFQFpesqlFEETVLKDVAFGPQNFGIPKEKAEKiAAEKLEMVGLADEfWEKSpfELSGGQMR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7406423 164 RVQICMGLLKPFKVLLLDEITVDLDVLARADLLKfLRKECEERGATIIYATHIFDGLEDWPTHIVYVANGKL 235
Cdd:PRK13643 152 RVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQ-LFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHI 222
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
53-215 |
7.14e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 53.76 E-value: 7.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 53 LVGSNGAGKTTILKILGGKHMVEPHMVRVLGRS-AFHDTgltssgdlcylggewrRDVAFAGFEVPIQ-------MDIsA 124
Cdd:PRK11288 35 LMGENGAGKSTLLKILSGNYQPDAGSILIDGQEmRFAST----------------TAALAAGVAIIYQelhlvpeMTV-A 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 125 EKMIFG----VAGIDPQR------RDELIKV-LDIDISWRLHKVSDGQRRRVQICMGLLKPFKVLLLDEITVDL-----D 188
Cdd:PRK11288 98 ENLYLGqlphKGGIVNRRllnyeaREQLEHLgVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLsareiE 177
|
170 180
....*....|....*....|....*..
gi 7406423 189 VLARadLLKFLRKEceerGATIIYATH 215
Cdd:PRK11288 178 QLFR--VIRELRAE----GRVILYVSH 198
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
17-218 |
7.83e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 52.70 E-value: 7.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 17 SGLRFTYpgidgHPPPGSKPLIEDFSITLNSSdrclLVGSNGAGKTTILKILGGkhMVEPHMVRVLGRSAFHDTgltSSG 96
Cdd:PRK13638 5 SDLWFRY-----QDEPVLKGLNLDFSLSPVTG----LVGANGCGKSTLFMNLSG--LLRPQKGAVLWQGKPLDY---SKR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 97 DLCYLggewRRDVAFAgFEVP--------IQMDISAEKMIFGVAGIDPQRR-DELIKVLDIDiSWR---LHKVSDGQRRR 164
Cdd:PRK13638 71 GLLAL----RQQVATV-FQDPeqqifytdIDSDIAFSLRNLGVPEAEITRRvDEALTLVDAQ-HFRhqpIQCLSHGQKKR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 7406423 165 VQICMGLLKPFKVLLLDEITVDLDVLARADLLKFLRKECEErGATIIYATHIFD 218
Cdd:PRK13638 145 VAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDID 197
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
53-228 |
8.11e-08 |
|
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: 52.18 E-value: 8.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 53 LVGSNGAGKTTILKILGGKHMVEPHmVRVLGRSAFHDTGLTSSGDLCYlggEWRRDVAFAgFE--VPIQMDIsAEKMIFG 130
Cdd:cd03260 31 LIGPSGCGKSTLLRLLNRLNDLIPG-APDEGEVLLDGKDIYDLDVDVL---ELRRRVGMV-FQkpNPFPGSI-YDNVAYG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 131 --VAGIDPQR-RDELIKV------LDIDISWRLH--KVSDGQRRRVQICMGL-LKPfKVLLLDEITVDLDVLARA---DL 195
Cdd:cd03260 105 lrLHGIKLKEeLDERVEEalrkaaLWDEVKDRLHalGLSGGQQQRLCLARALaNEP-EVLLLDEPTSALDPISTAkieEL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 7406423 196 LKFLRKEceergATIIYATH--------------IFDG--LEDWPTHIV 228
Cdd:cd03260 184 IAELKKE-----YTIVIVTHnmqqaarvadrtafLLNGrlVEFGPTEQI 227
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
29-218 |
8.90e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 52.54 E-value: 8.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 29 HPPPGSKPLiEDFSITLNSSDRCLLVGSNGAGKTTILKILGGkhMVEPHMVRVLGRSAFHDTGLTSSGDLCYLGGEWRRD 108
Cdd:PRK13636 14 NYSDGTHAL-KGININIKKGEVTAILGGNGAGKSTLFQNLNG--ILKPSSGRILFDGKPIDYSRKGLMKLRESVGMVFQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 109 VAFAGFEVPIQMDISAEKMIFGVAGIDPQRRDELIkVLDIDISWRLHK----VSDGQRRRVQICMGLLKPFKVLLLDEIT 184
Cdd:PRK13636 91 PDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNA-LKRTGIEHLKDKpthcLSFGQKKRVAIAGVLVMEPKVLVLDEPT 169
|
170 180 190
....*....|....*....|....*....|....
gi 7406423 185 VDLDVLARADLLKFLRKECEERGATIIYATHIFD 218
Cdd:PRK13636 170 AGLDPMGVSEIMKLLVEMQKELGLTIIIATHDID 203
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
53-215 |
1.06e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 52.45 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 53 LVGSNGAGKTTILKILGGkhMVEPHMvrvlGRSAFHDTGLTSSG---------------DLCYLGGEWRRDVAFaGFEvp 117
Cdd:PRK13648 40 IVGHNGSGKSTIAKLMIG--IEKVKS----GEIFYNNQAITDDNfeklrkhigivfqnpDNQFVGSIVKYDVAF-GLE-- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 118 iQMDISAEKMIFGVAgidpqrrdeliKVL-DIDISWRL----HKVSDGQRRRVQICMGLLKPFKVLLLDEITVDLDVLAR 192
Cdd:PRK13648 111 -NHAVPYDEMHRRVS-----------EALkQVDMLERAdyepNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDAR 178
|
170 180
....*....|....*....|...
gi 7406423 193 ADLLKFLRKECEERGATIIYATH 215
Cdd:PRK13648 179 QNLLDLVRKVKSEHNITIISITH 201
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
41-243 |
1.06e-07 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 51.68 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 41 FSITLNSSDRCLLVGSNGAGKTTILKILGGkhMVEPHmvrvlgrsafhdtgltsSGDLCYLGgewrRDVAFAGfevPIQM 120
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAG--FLPPD-----------------SGRILWNG----QDLTALP---PAER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 121 DISaekMIF---------GVA-----GIDPQRR---DELIKVLDI-------DISWRL-HKVSDGQRRRVQICMGLLKPF 175
Cdd:COG3840 72 PVS---MLFqennlfphlTVAqniglGLRPGLKltaEQRAQVEQAlervglaGLLDRLpGQLSGGQRQRVALARCLVRKR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7406423 176 KVLLLDEITVDLDVLARADLLKFLRKECEERGATIIYATHIFDGLEDWPTHIVYVANGKLQLALPMEK 243
Cdd:COG3840 149 PILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAA 216
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
14-215 |
1.38e-07 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 52.41 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 14 VEISGLRFTYpgidghpppGSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGkhMVEPhmvrvlgrsafhdtglt 93
Cdd:COG3842 6 LELENVSKRY---------GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAG--FETP----------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 94 SSGDLcYLGGE-------WRRDVA-----FAGFevPiQMDIsAEKMIFG--VAGIDPQRR----DELIKVLDIDiswRL- 154
Cdd:COG3842 58 DSGRI-LLDGRdvtglppEKRNVGmvfqdYALF--P-HLTV-AENVAFGlrMRGVPKAEIrarvAELLELVGLE---GLa 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7406423 155 ----HKVSDGQRRRVQICMGL-LKPfKVLLLDEITVDLDVLARADLLKFLRKECEERGATIIYATH 215
Cdd:COG3842 130 drypHQLSGGQQQRVALARALaPEP-RVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTH 194
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
35-188 |
1.71e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 51.63 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 35 KPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGKHMVEPHMVRVLGRsafhD-TGLTssgdlcylggEWRRdVAFAG 113
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGK----DvTKLP----------EYKR-AKYIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 114 --FEVPIQ-----MDIsAEKMI--------FGVA-GIDPQRRD---ELIKVLDIDISWRLH-KV---SDGQRRRVQICMG 170
Cdd:COG1101 84 rvFQDPMMgtapsMTI-EENLAlayrrgkrRGLRrGLTKKRRElfrELLATLGLGLENRLDtKVgllSGGQRQALSLLMA 162
|
170
....*....|....*...
gi 7406423 171 LLKPFKVLLLDEITVDLD 188
Cdd:COG1101 163 TLTKPKLLLLDEHTAALD 180
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
31-215 |
2.00e-07 |
|
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: 49.84 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 31 PPGSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGkhmVEPHmvrvlgrsafhdtgltSSGDLCYLGGEwrrDVA 110
Cdd:cd03223 10 TPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG---LWPW----------------GSGRIGMPEGE---DLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 111 FAgfevpiqmdisaekmifgvagidPQR--------RDELIKVLDidiswrlHKVSDGQRRRVQIC-MGLLKPfKVLLLD 181
Cdd:cd03223 68 FL-----------------------PQRpylplgtlREQLIYPWD-------DVLSGGEQQRLAFArLLLHKP-KFVFLD 116
|
170 180 190
....*....|....*....|....*....|....
gi 7406423 182 EITVDLDVlaraDLLKFLRKECEERGATIIYATH 215
Cdd:cd03223 117 EATSALDE----ESEDRLYQLLKELGITVISVGH 146
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
34-215 |
3.09e-07 |
|
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: 50.35 E-value: 3.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 34 SKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGkhmvephmvRVLGRSafhdtglTSSGDLCYLG-----GEWRRD 108
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISG---------RVEGGG-------TTSGQILFNGqprkpDQFQKC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 109 VAFagfeVPiQMDISA------EKMIFGV--------AGIDPQRRDELIKVLDIDIS----WRLHKVSDGQRRRVQICMG 170
Cdd:cd03234 83 VAY----VR-QDDILLpgltvrETLTYTAilrlprksSDAIRKKRVEDVLLRDLALTriggNLVKGISGGERRRVSIAVQ 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 7406423 171 LLKPFKVLLLDEITVDLDVLARADLLKFLRKECeERGATIIYATH 215
Cdd:cd03234 158 LLWDPKVLILDEPTSGLDSFTALNLVSTLSQLA-RRNRIVILTIH 201
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
33-215 |
3.33e-07 |
|
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: 50.42 E-value: 3.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 33 GSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGkhMVEPHMVRVL--GRSAfhdTGLTSSgdlcylggewRRDVA 110
Cdd:cd03296 13 GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAG--LERPDSGTILfgGEDA---TDVPVQ----------ERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 111 F-----AGFEvpiQMDIsAEKMIFGV-----------AGIDpQRRDELIKVLDID-ISWRL-HKVSDGQRRRVQICMGLL 172
Cdd:cd03296 78 FvfqhyALFR---HMTV-FDNVAFGLrvkprserppeAEIR-AKVHELLKLVQLDwLADRYpAQLSGGQRQRVALARALA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 7406423 173 KPFKVLLLDEITVDLDVLARADLLKFLRKECEERGATIIYATH 215
Cdd:cd03296 153 VEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTH 195
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
14-188 |
4.05e-07 |
|
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: 50.23 E-value: 4.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 14 VEISGLRFTYPgidghpppgSKP---LIEDFSITLNSSDRCLLVGSNGAGKTTILKIL-------GGKHMVEPHMVRVLg 83
Cdd:cd03249 1 IEFKNVSFRYP---------SRPdvpILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLerfydptSGEILLDGVDIRDL- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 84 rsafhdtgltssgDLCYLggewRRDVAFAGFEvPIQMDIS-AEKMIFGVAGIDPQRRDELIKVLDID---ISW------- 152
Cdd:cd03249 71 -------------NLRWL----RSQIGLVSQE-PVLFDGTiAENIRYGKPDATDEEVEEAAKKANIHdfiMSLpdgydtl 132
|
170 180 190
....*....|....*....|....*....|....*....
gi 7406423 153 ---RLHKVSDGQRRRVQICMGLLKPFKVLLLDEITVDLD 188
Cdd:cd03249 133 vgeRGSQLSGGQKQRIAIARALLRNPKILLLDEATSALD 171
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
139-215 |
4.23e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 51.24 E-value: 4.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 139 RDELIKVLD-IDI---SWRL----HKVSDGQRRRVQICMGLLKPFKVLLLDEITVDLDVLARADLLKFLRKECEERGATI 210
Cdd:PRK15134 131 RGEILNCLDrVGIrqaAKRLtdypHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGL 210
|
....*
gi 7406423 211 IYATH 215
Cdd:PRK15134 211 LFITH 215
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
33-222 |
4.84e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 49.49 E-value: 4.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 33 GSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGkhMVEPhmvrVLGRSAFH--DTGLTSSGDLC-YLGgewRRD- 108
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAG--LLPP----AAGTIKLDggDIDDPDVAEAChYLG---HRNa 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 109 ----------VAF-AGFEVPIQMDISAEKMIFGVAGIDPQRRDELikvldidiswrlhkvSDGQRRRVQICMGLLKPFKV 177
Cdd:PRK13539 84 mkpaltvaenLEFwAAFLGGEELDIAAALEAVGLAPLAHLPFGYL---------------SAGQKRRVALARLLVSNRPI 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 7406423 178 LLLDEITVDLDVLARADLLKFLRKECeERGATIIYATHIFDGLED 222
Cdd:PRK13539 149 WILDEPTAALDAAAVALFAELIRAHL-AQGGIVIAATHIPLGLPG 192
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
42-244 |
5.86e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.78 E-value: 5.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 42 SITLNSSDRCLLVGSNGAGKTTILKILGGKhmvephMVRVLGR--SAFHDTGLTSSGDLCYL-GGEWRR----------- 107
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGE------LPLLSGErqSQFSHITRLSFEQLQKLvSDEWQRnntdmlspged 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 108 DVAFAGFEVpIQMDISaekmifgvagiDPQRRDELIKVLDID--ISWRLHKVSDGQRRRVQICMGLLKPFKVLLLDEITV 185
Cdd:PRK10938 97 DTGRTTAEI-IQDEVK-----------DPARCEQLAQQFGITalLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 7406423 186 DLDVLARADLLKFLRKeCEERGATIIYATHIFDGLEDWPTHIVYVANGKLQLALPMEKV 244
Cdd:PRK10938 165 GLDVASRQQLAELLAS-LHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEI 222
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
35-215 |
7.16e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 49.18 E-value: 7.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 35 KPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGKHMVEPHMVRVLGRSAfhdtgltsSGDLCylggEWRRDVAFAGF 114
Cdd:PRK13540 14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI--------KKDLC----TYQKQLCFVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 115 EVPIQMDIS-AEKMIF------GVAGIDpqrrdELIKVLDID--ISWRLHKVSDGQRRRVQICMGLLKPFKVLLLDEITV 185
Cdd:PRK13540 82 RSGINPYLTlRENCLYdihfspGAVGIT-----ELCRLFSLEhlIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLV 156
|
170 180 190
....*....|....*....|....*....|..
gi 7406423 186 DLDVLAradLLKFLRKECEER--GATIIYATH 215
Cdd:PRK13540 157 ALDELS---LLTIITKIQEHRakGGAVLLTSH 185
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
9-221 |
7.38e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 50.21 E-value: 7.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 9 KRNSTVEISGLRFTYpgidghpppGSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGkhMVEPHM--VRVLG--- 83
Cdd:PRK13536 37 MSTVAIDLAGVSKSY---------GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILG--MTSPDAgkITVLGvpv 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 84 ----RSAFHDTGLTSSGDlcylggewRRDVAFAGFEvpiqmdisaEKMIFG-VAGIDPQRRDELIKV------LDIDISW 152
Cdd:PRK13536 106 paraRLARARIGVVPQFD--------NLDLEFTVRE---------NLLVFGrYFGMSTREIEAVIPSllefarLESKADA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7406423 153 RLHKVSDGQRRRVQICMGLLKPFKVLLLDEITVDLDVLARADLLKFLRkECEERGATIIYATHIFDGLE 221
Cdd:PRK13536 169 RVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLR-SLLARGKTILLTTHFMEEAE 236
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
14-215 |
7.41e-07 |
|
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: 49.13 E-value: 7.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 14 VEISGLRFTYPGIDghpppgsKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGkhMVEPHMVRVLgrsaFHDTGLT 93
Cdd:cd03245 3 IEFRNVSFSYPNQE-------IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAG--LYKPTSGSVL----LDGTDIR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 94 S------SGDLCYLG-------GEWRRDVAFAGFEVPIQMDISAEKMifgvAGIDPQRRDeLIKVLDIDISWRLHKVSDG 160
Cdd:cd03245 70 QldpadlRRNIGYVPqdvtlfyGTLRDNITLGAPLADDERILRAAEL----AGVTDFVNK-HPNGLDLQIGERGRGLSGG 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 7406423 161 QRRRVQICMGLLKPFKVLLLDEITVDLDVLARADLLKFLRKECEERgaTIIYATH 215
Cdd:cd03245 145 QRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDK--TLIIITH 197
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
40-215 |
8.65e-07 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 50.03 E-value: 8.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 40 DFSITLNSSDRCLLVGSNGAGKTTILKILGGKHMVephmvrvlgrsafhdtgltSSGDLcYLGGEWRRDVA--------- 110
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDI-------------------TSGDL-FIGEKRMNDVPpaergvgmv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 111 FAGFEVPIQMDIsAEKMIFGV--AGIDP----QRRDELIKVLDID--ISWRLHKVSDGQRRRVQICMGLLKPFKVLLLDE 182
Cdd:PRK11000 81 FQSYALYPHLSV-AENMSFGLklAGAKKeeinQRVNQVAEVLQLAhlLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDE 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 7406423 183 ITVDLD----VLARADLLKFLRKeceeRGATIIYATH 215
Cdd:PRK11000 160 PLSNLDaalrVQMRIEISRLHKR----LGRTMIYVTH 192
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
33-253 |
1.15e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 49.82 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 33 GSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGKHmvePHMvrvlgrsafhdtglTSSGDLCYLGGEWR----RD 108
Cdd:TIGR02633 12 GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY---PHG--------------TWDGEIYWSGSPLKasniRD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 109 VAFAGF-----EVPIQMDISAEKMIF--------GVAGIDPQ---RRDELIKVLDIDISWRLHKVSD---GQRRRVQICM 169
Cdd:TIGR02633 75 TERAGIviihqELTLVPELSVAENIFlgneitlpGGRMAYNAmylRAKNLLRELQLDADNVTRPVGDyggGQQQLVEIAK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 170 GLLKPFKVLLLDEITVDLDVLARADLLKFLRkECEERGATIIYATHIFDGLEDWPTHIVYVANGKLQLALPMEKVKETSK 249
Cdd:TIGR02633 155 ALNKQARLLILDEPSSSLTEKETEILLDIIR-DLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDI 233
|
....
gi 7406423 250 KSLM 253
Cdd:TIGR02633 234 ITMM 237
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
13-249 |
1.19e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 49.28 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 13 TVEISGLRFTY-PGIdghppPGSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGkhMVEPHMvrvlGRSAFHDTG 91
Cdd:PRK13637 2 SIKIENLTHIYmEGT-----PFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNG--LLKPTS----GKIIIDGVD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 92 LTSSG-DLcylgGEWRRDVA-------FAGFEVPIQMDISAEKMIFGVAGIDPQRR-DELIKVLDIDISWRLHK----VS 158
Cdd:PRK13637 71 ITDKKvKL----SDIRKKVGlvfqypeYQLFEETIEKDIAFGPINLGLSEEEIENRvKRAMNIVGLDYEDYKDKspfeLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 159 DGQRRRVQICmGLL--KPfKVLLLDEITVDLDVLARADLLKFLRKECEERGATIIYATHIFDGLEDWPTHIVYVANGKLQ 236
Cdd:PRK13637 147 GGQKRRVAIA-GVVamEP-KILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCE 224
|
250
....*....|....
gi 7406423 237 L-ALPMEKVKETSK 249
Cdd:PRK13637 225 LqGTPREVFKEVET 238
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
33-215 |
1.35e-06 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 49.31 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 33 GSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGkhmVEPHMVrvlGRSAFHDTgltssgDLCYLGGEWRRdVAF- 111
Cdd:PRK10851 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAG---LEHQTS---GHIRFHGT------DVSRLHARDRK-VGFv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 112 ----AGFEvpiQMDISaEKMIFGVAgIDPQRRDELIKVLDIDISWRLHKV-------------SDGQRRRVQICMGLLKP 174
Cdd:PRK10851 80 fqhyALFR---HMTVF-DNIAFGLT-VLPRRERPNAAAIKAKVTQLLEMVqlahladrypaqlSGGQKQRVALARALAVE 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 7406423 175 FKVLLLDEITVDLDVLARADLLKFLRKECEERGATIIYATH 215
Cdd:PRK10851 155 PQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTH 195
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
15-215 |
1.42e-06 |
|
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: 47.60 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 15 EISGLRFTYPGidghpppGSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGKHMVEPHMVRVLGRsAFHDTGLTS 94
Cdd:cd03246 2 EVENVSFRYPG-------AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGA-DISQWDPNE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 95 SGDLC-YLGgewRRDVAFAGfevpiqmdiSAEKMIFgvagidpqrrdelikvldidiswrlhkvSDGQRRRVQICMGLLK 173
Cdd:cd03246 74 LGDHVgYLP---QDDELFSG---------SIAENIL----------------------------SGGQRQRLGLARALYG 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 7406423 174 PFKVLLLDEITVDLDVL---ARADLLKFLRKeceeRGATIIYATH 215
Cdd:cd03246 114 NPRILVLDEPNSHLDVEgerALNQAIAALKA----AGATRIVIAH 154
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
34-218 |
1.74e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 48.55 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 34 SKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKilggkhmvepHMVRVLgrsafhdtgLTSSG-------DLCYLGGEWR 106
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAK----------HMNALL---------IPSEGkvyvdglDTSDEENLWD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 107 -RDVAFAGFEVP---IQMDISAEKMIFGVA--GIDPQ----RRDELIKVLDIDISWRL--HKVSDGQRRRVQICmGLL-- 172
Cdd:PRK13633 83 iRNKAGMVFQNPdnqIVATIVEEDVAFGPEnlGIPPEeireRVDESLKKVGMYEYRRHapHLLSGGQKQRVAIA-GILam 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 7406423 173 KPfKVLLLDEITVDLDVLARADLLKFLRKECEERGATIIYATHIFD 218
Cdd:PRK13633 162 RP-ECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYME 206
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
10-215 |
1.84e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 48.54 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 10 RNSTVEISGLRFTYPGidghpppgskPLIEDFSITLNSSDRCLLVGSNGAGKT-TILKILGgkhmVEPHMVRVLG----- 83
Cdd:PRK10418 1 MPQQIELRNIALQAAQ----------PLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALG----ILPAGVRQTAgrvll 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 84 ----------------------RSAF---HDTGLTSSGDLCYLGGEWRRDVAFAGFEvpiqmdisaekmifGVAGIDPQR 138
Cdd:PRK10418 67 dgkpvapcalrgrkiatimqnpRSAFnplHTMHTHARETCLALGKPADDATLTAALE--------------AVGLENAAR 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 139 rdelikVLdidiswRLH--KVSDGQRRRVQICMGLL--KPFkvLLLDEITVDLDVLARADLLKFLRKECEERGATIIYAT 214
Cdd:PRK10418 133 ------VL------KLYpfEMSGGMLQRMMIALALLceAPF--IIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVT 198
|
.
gi 7406423 215 H 215
Cdd:PRK10418 199 H 199
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
33-215 |
2.01e-06 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 48.53 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 33 GSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGkhMVEPHMvrvlGRSAFHDTGLTSsgdlcyLGGEWRRDvafa 112
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVG--LESPSQ----GNVSWRGEPLAK------LNRAQRKA---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 113 gFEVPIQM----------------DISAEKMIFgVAGIDPQ----RRDELIKVLDIDISW---RLHKVSDGQRRRVQICM 169
Cdd:PRK10419 87 -FRRDIQMvfqdsisavnprktvrEIIREPLRH-LLSLDKAerlaRASEMLRAVDLDDSVldkRPPQLSGGQLQRVCLAR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 7406423 170 GLLKPFKVLLLDEITVDLDVLARADLLKFLRKECEERGATIIYATH 215
Cdd:PRK10419 165 ALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITH 210
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
33-211 |
2.10e-06 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 48.23 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 33 GSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGKhmVEPhmvrvlgrsafhdtgltSSGDlCYLGG----EW--- 105
Cdd:PRK13548 13 GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGE--LSP-----------------DSGE-VRLNGrplaDWspa 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 106 ----RRDV-------AFAgF---EVpIQMdisaekmifGVA--GIDPQRRDELI-KVLDI----DISWRL-HKVSDGQRR 163
Cdd:PRK13548 73 elarRRAVlpqhsslSFP-FtveEV-VAM---------GRAphGLSRAEDDALVaAALAQvdlaHLAGRDyPQLSGGEQQ 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 7406423 164 RVQICMGLL------KPFKVLLLDEITVDLDVLARADLLKFLRKECEERGATII 211
Cdd:PRK13548 142 RVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVI 195
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-215 |
2.27e-06 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 48.79 E-value: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 4 TEEEKKRNSTVEISGLRFTYpgidghpppGSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGKHMVEPHMVRVLG 83
Cdd:PRK09452 5 NKQPSSLSPLVELRGISKSF---------DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 84 RsafhdtgltssgDLCYLGGEwRRDV-----AFAGFevPiQMDIsAEKMIFGV-------AGIDPQRRDELIKV-LDIDI 150
Cdd:PRK09452 76 Q------------DITHVPAE-NRHVntvfqSYALF--P-HMTV-FENVAFGLrmqktpaAEITPRVMEALRMVqLEEFA 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7406423 151 SWRLHKVSDGQRRRVQICMGLLKPFKVLLLDEITVDLDVLARADL---LKFLRKECeerGATIIYATH 215
Cdd:PRK09452 139 QRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMqneLKALQRKL---GITFVFVTH 203
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
14-247 |
2.44e-06 |
|
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: 47.88 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 14 VEISGLRFTYpgidghpppGSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGkhMVEPH--MVRVLGrsafHDTG 91
Cdd:cd03261 1 IELRGLTKSF---------GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVG--LLRPDsgEVLIDG----EDIS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 92 LTSSGDLCYLGGEW---------------RRDVAFagfevPIQM----------DISAEKM-IFGVAGIDPQRRDELikv 145
Cdd:cd03261 66 GLSEAELYRLRRRMgmlfqsgalfdsltvFENVAF-----PLREhtrlseeeirEIVLEKLeAVGLRGAEDLYPAEL--- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 146 ldidiswrlhkvSDGQRRRVQICMGL-LKPfKVLLLDEITVDLDVLARADLLKFLRKECEERGATIIYATHIFDGLEDWP 224
Cdd:cd03261 138 ------------SGGMKKRVALARALaLDP-ELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIA 204
|
250 260
....*....|....*....|...
gi 7406423 225 THIVYVANGKLQLALPMEKVKET 247
Cdd:cd03261 205 DRIAVLYDGKIVAEGTPEELRAS 227
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
155-215 |
2.75e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 48.18 E-value: 2.75e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7406423 155 HKVSDGQRRRVQICMGLLKPFKVLLLDEITVDLDVLARADLLKFLRKECEERGATIIYATH 215
Cdd:PRK09473 160 HEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITH 220
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
11-215 |
2.93e-06 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 48.95 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 11 NSTVEISGLRFTYPGIDGhpppgSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGKHMVEPHMVRVLGRsafhDT 90
Cdd:PRK10535 2 TALLELKDIRRSYPSGEE-----QVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQ----DV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 91 GLTSSGDLCYLggewRRD---------------VAFAGFEVPiqmdisaekMIFgvAGIDPQRR----DELIKVLDID-- 149
Cdd:PRK10535 73 ATLDADALAQL----RREhfgfifqryhllshlTAAQNVEVP---------AVY--AGLERKQRllraQELLQRLGLEdr 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7406423 150 ISWRLHKVSDGQRRRVQICMGLLKPFKVLLLDEITVDLDVLARADLLKFLrKECEERGATIIYATH 215
Cdd:PRK10535 138 VEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAIL-HQLRDRGHTVIIVTH 202
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
33-215 |
3.39e-06 |
|
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: 47.23 E-value: 3.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 33 GSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGkhMVEPhmvrvlgrsafhdtgltSSGDLcYLGGE-------W 105
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAG--FETP-----------------TSGEI-LLDGKditnlppH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 106 RRDV--AFAGFEVPIQMDIsAEKMIFG--VAGIDP----QRRDELIKVLDID--ISWRLHKVSDGQRRRVQICMGLLKPF 175
Cdd:cd03300 71 KRPVntVFQNYALFPHLTV-FENIAFGlrLKKLPKaeikERVAEALDLVQLEgyANRKPSQLSGGQQQRVAIARALVNEP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 7406423 176 KVLLLDEITVDLDVLARADLLKFLRKECEERGATIIYATH 215
Cdd:cd03300 150 KVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTH 189
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
26-244 |
3.64e-06 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 47.66 E-value: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 26 IDGHPPPGSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILG-------GKHMVEPHMVRVLgRSAFHDTGLTSSGDL 98
Cdd:PRK10619 9 IDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINflekpseGSIVVNGQTINLV-RDKDGQLKVADKNQL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 99 CYLggEWRRDVAFAGF-------------EVPIQM-----DISAEKMIFGVA--GIDPQRRDElikvldidisWRLHkVS 158
Cdd:PRK10619 88 RLL--RTRLTMVFQHFnlwshmtvlenvmEAPIQVlglskQEARERAVKYLAkvGIDERAQGK----------YPVH-LS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 159 DGQRRRVQICMGLLKPFKVLLLDEITVDLDVLARADLLKFLRKECEErGATIIYATHIFDGLEDWPTHIVYVANGKLQLA 238
Cdd:PRK10619 155 GGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEE 233
|
....*.
gi 7406423 239 LPMEKV 244
Cdd:PRK10619 234 GAPEQL 239
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
13-215 |
4.25e-06 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 48.24 E-value: 4.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 13 TVEISGLRFTYPGidghpppgSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGkhmvephmvrvlgrsaFHDtgl 92
Cdd:COG1132 339 EIEFENVSFSYPG--------DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLR----------------FYD--- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 93 TSSGDLcYLGG---------EWRRDVAFagfeVPiQmDIS------AEKMIFGVAGIDpqrRDELIKVLDI-----DISw 152
Cdd:COG1132 392 PTSGRI-LIDGvdirdltleSLRRQIGV----VP-Q-DTFlfsgtiRENIRYGRPDAT---DEEVEEAAKAaqaheFIE- 460
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7406423 153 RL------------HKVSDGQRRRVQICMGLLKPFKVLLLDEITVDLDVLARADLLKFLRKECEERgaTIIYATH 215
Cdd:COG1132 461 ALpdgydtvvgergVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGR--TTIVIAH 533
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-189 |
5.30e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.81 E-value: 5.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 3 VTEEEKKRNSTVEI---------------SGLRFTYpgidghpppGSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKI 67
Cdd:PRK11819 299 LSEEYQKRNETNEIfippgprlgdkvieaENLSKSF---------GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKM 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 68 LGGKHMVEPHMVRV-----LG-----RSAFhDTGLT-----SSG-DLCYLGgewrrdvafaGFEVPIQMDISAekmiFGV 131
Cdd:PRK11819 370 ITGQEQPDSGTIKIgetvkLAyvdqsRDAL-DPNKTvweeiSGGlDIIKVG----------NREIPSRAYVGR----FNF 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 7406423 132 AGIDPQRRdelIKVLdidiswrlhkvSDGQRRRVQICMGLLKPFKVLLLDEITVDLDV 189
Cdd:PRK11819 435 KGGDQQKK---VGVL-----------SGGERNRLHLAKTLKQGGNVLLLDEPTNDLDV 478
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-70 |
5.31e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.96 E-value: 5.31e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7406423 5 EEEKK--RNStVEISGLRFTYPGidghpppgsKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGG 70
Cdd:PRK15064 310 EQDKKlhRNA-LEVENLTKGFDN---------GPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVG 367
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
53-215 |
5.63e-06 |
|
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: 47.76 E-value: 5.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 53 LVGSNGAGKTTI-LKILGgkhmvephmvrvLgrsafhdtgLTSSGDLCYLGGEW-----------RRDvafagfevpIQM 120
Cdd:COG4172 317 LVGESGSGKSTLgLALLR------------L---------IPSEGEIRFDGQDLdglsrralrplRRR---------MQV 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 121 ----------------DISAEKMIFGVAGIDPQRRDELI-----KV-LDIDISWRL-HKVSDGQRRRVQICMGL-LKPfK 176
Cdd:COG4172 367 vfqdpfgslsprmtvgQIIAEGLRVHGPGLSAAERRARVaealeEVgLDPAARHRYpHEFSGGQRQRIAIARALiLEP-K 445
|
170 180 190
....*....|....*....|....*....|....*....
gi 7406423 177 VLLLDEITVDLDVLARADLLKFLRKECEERGATIIYATH 215
Cdd:COG4172 446 LLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISH 484
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
37-199 |
7.15e-06 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 46.43 E-value: 7.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 37 LIEDFSITLNSSDRCLLVGSNGAGKTTILkilggkHMVEPHMVRVLGRSAFHDTGLTssgdLCYLGGEWRRDVAFAGFEV 116
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTF------YMVVGIVPRDAGNIIIDDEDIS----LLPLHARARRGIGYLPQEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 117 PIQMDISAEKMIFGVAGI-----DPQRRD---ELIKVLDID-ISWRL-HKVSDGQRRRVQICMGLLKPFKVLLLDEITVD 186
Cdd:PRK10895 88 SIFRRLSVYDNLMAVLQIrddlsAEQREDranELMEEFHIEhLRDSMgQSLSGGERRRVEIARALAANPKFILLDEPFAG 167
|
170
....*....|...
gi 7406423 187 LDVLARADLLKFL 199
Cdd:PRK10895 168 VDPISVIDIKRII 180
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
33-70 |
7.44e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.58 E-value: 7.44e-06
10 20 30
....*....|....*....|....*....|....*...
gi 7406423 33 GSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGG 70
Cdd:PRK15064 12 GAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGG 49
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
14-215 |
9.69e-06 |
|
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: 46.07 E-value: 9.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 14 VEISGLRFTYpgidgHPppgSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILggkhmvephmVRvlgrsaFHDtglT 93
Cdd:cd03253 1 IEFENVTFAY-----DP---GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLL----------FR------FYD---V 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 94 SSGDLcYLGGEWRRDVAFAGFE-----VPIQMDISAEKMIFGVAGIDPQRRDELI----KVLDID---ISW--------- 152
Cdd:cd03253 54 SSGSI-LIDGQDIREVTLDSLRraigvVPQDTVLFNDTIGYNIRYGRPDATDEEVieaaKAAQIHdkiMRFpdgydtivg 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7406423 153 -RLHKVSDGQRRRVQICMGLLKPFKVLLLDEITVDLDVLARADLLKFLRKECEERgaTIIYATH 215
Cdd:cd03253 133 eRGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGR--TTIVIAH 194
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
41-222 |
1.15e-05 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 45.73 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 41 FSITLNSSDRCLLVGSNGAGKTTILKILGGkhmvephmvrvlgrsaFhdtgLT-SSGDLcYLGGEWRRDVAfagfevPIQ 119
Cdd:PRK10771 18 FDLTVERGERVAILGPSGAGKSTLLNLIAG----------------F----LTpASGSL-TLNGQDHTTTP------PSR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 120 MDISaekMIF---------GVA-----GIDP------QRRDELIKVLD----IDISWRL-HKVSDGQRRRVQICMGLLKP 174
Cdd:PRK10771 71 RPVS---MLFqennlfshlTVAqniglGLNPglklnaAQREKLHAIARqmgiEDLLARLpGQLSGGQRQRVALARCLVRE 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 7406423 175 FKVLLLDEITVDLDVLARADLLKFLRKECEERGATIIYATHifdGLED 222
Cdd:PRK10771 148 QPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSH---SLED 192
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
53-218 |
1.45e-05 |
|
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: 46.33 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 53 LVGSNGAGKTTILKILGGkhMVEPhmvrvlgrsafhdtgltSSGDLCY-LGGEW-------------------------- 105
Cdd:TIGR03269 315 IVGTSGAGKTTLSKIIAG--VLEP-----------------TSGEVNVrVGDEWvdmtkpgpdgrgrakryigilhqeyd 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 106 ---RRDV-----AFAGFEVPIQMDISAEKMIFGVAGIDPQRRDELIKVLDidiswrlHKVSDGQRRRVQICMGLLKPFKV 177
Cdd:TIGR03269 376 lypHRTVldnltEAIGLELPDELARMKAVITLKMVGFDEEKAEEILDKYP-------DELSEGERHRVALAQVLIKEPRI 448
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 7406423 178 LLLDEITVDLDVLARADLLKFLRKECEERGATIIYATHIFD 218
Cdd:TIGR03269 449 VILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMD 489
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-189 |
1.89e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.10 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 1 MAVTEEEKKRNSTVEISGLRFTYPGidghpppgsKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGKhmVEPhmvr 80
Cdd:PRK11147 307 MQVEEASRSGKIVFEMENVNYQIDG---------KQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQ--LQA---- 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 81 vlgrsafhDTGLTSSGDlcylggewRRDVAFagFEvpiQ-----------MDISAE-KMIFGVAGID------------- 135
Cdd:PRK11147 372 --------DSGRIHCGT--------KLEVAY--FD---QhraeldpektvMDNLAEgKQEVMVNGRPrhvlgylqdflfh 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 7406423 136 PQRRDELIKVLdidiswrlhkvSDGQRRRVQICMGLLKPFKVLLLDEITVDLDV 189
Cdd:PRK11147 431 PKRAMTPVKAL-----------SGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
33-215 |
2.08e-05 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 45.08 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 33 GSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILK-------ILGGKHMVEPhmVRVLGRSAfhdtgltssgDLCylggEW 105
Cdd:PRK09493 12 GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRcinkleeITSGDLIVDG--LKVNDPKV----------DER----LI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 106 RRD--VAFAGFEVPIQMdISAEKMIFG---VAGI-----DPQRRDELIKVldiDISWRLH----KVSDGQRRRVQICMGL 171
Cdd:PRK09493 76 RQEagMVFQQFYLFPHL-TALENVMFGplrVRGAskeeaEKQARELLAKV---GLAERAHhypsELSGGQQQRVAIARAL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 7406423 172 -LKPfKVLLLDEITVDLDVLARADLLKFLRKECEErGATIIYATH 215
Cdd:PRK09493 152 aVKP-KLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTH 194
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
38-211 |
2.19e-05 |
|
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: 45.12 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 38 IEDFSITLNSSDRCLLVGSNGAGKTTILKILGGKHM---------------VEPHMVRVLG--RSaFHDTGLTSSG---D 97
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRptsgsvlfdgeditgLPPHEIARLGigRT-FQIPRLFPELtvlE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 98 LCYLGGEWRRDVAFAGFEVPIQMDISAEKM--IFGVAGIDPqRRDELIKVLdidiswrlhkvSDGQRRRVQICMGL-LKP 174
Cdd:cd03219 95 NVMVAAQARTGSGLLLARARREEREARERAeeLLERVGLAD-LADRPAGEL-----------SYGQQRRLEIARALaTDP 162
|
170 180 190
....*....|....*....|....*....|....*..
gi 7406423 175 fKVLLLDEITVDLDVLARADLLKFLRkECEERGATII 211
Cdd:cd03219 163 -KLLLLDEPAAGLNPEETEELAELIR-ELRERGITVL 197
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-215 |
2.20e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 45.41 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 14 VEISGLRFTYpgidghpppGSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGKHMVEPHmVRVLGRSAFHDTGLT 93
Cdd:PRK14258 8 IKVNNLSFYY---------DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESE-VRVEGRVEFFNQNIY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 94 SSG-DLCYLggewRRDVAFAgFEVPIQMDISA-EKMIFGVAGIDPQRRDEL-------IKVLDI--DISWRLHK----VS 158
Cdd:PRK14258 78 ERRvNLNRL----RRQVSMV-HPKPNLFPMSVyDNVAYGVKIVGWRPKLEIddivesaLKDADLwdEIKHKIHKsaldLS 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 7406423 159 DGQRRRVQICMGL-LKPfKVLLLDEITVDLDVLARADLLKFLRKECEERGATIIYATH 215
Cdd:PRK14258 153 GGQQQRLCIARALaVKP-KVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSH 209
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
38-235 |
2.57e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 45.00 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 38 IEDFSITLNSSDRCLLVGSNGAGKTTILKILGGKHMVEphmvrvlgrsafhdTGLTSSGDLCYLGG--------EWRRDV 109
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISE--------------TGQTIVGDYAIPANlkkikevkRLRKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 110 AFAgFEVP--------IQMDISaekmiFGVAGIDPQRRD------ELIKVLDI--DISWRL-HKVSDGQRRRVQICMGLL 172
Cdd:PRK13645 93 GLV-FQFPeyqlfqetIEKDIA-----FGPVNLGENKQEaykkvpELLKLVQLpeDYVKRSpFELSGGQKRRVALAGIIA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7406423 173 KPFKVLLLDEITVDLDVLARADLLKFLRKECEERGATIIYATHIFDGLEDWPTHIVYVANGKL 235
Cdd:PRK13645 167 MDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKV 229
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
53-218 |
3.16e-05 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 45.39 E-value: 3.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 53 LVGSNGAGKTTILKILGGkhmVEPH---MVRVLGRS-AFHDTGL-TSSG--------DLC---------YLGGEWRRdva 110
Cdd:COG1129 35 LLGENGAGKSTLMKILSG---VYQPdsgEILLDGEPvRFRSPRDaQAAGiaiihqelNLVpnlsvaeniFLGREPRR--- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 111 fAGFevpiqmdISAEKMIfgvagidpQRRDELIKVLDIDISWRLhKVSD---GQRRRVQICMGLLKPFKVLLLDEITVDL 187
Cdd:COG1129 109 -GGL-------IDWRAMR--------RRARELLARLGLDIDPDT-PVGDlsvAQQQLVEIARALSRDARVLILDEPTASL 171
|
170 180 190
....*....|....*....|....*....|.
gi 7406423 188 DVLARADLLKFLRKECeERGATIIYATHIFD 218
Cdd:COG1129 172 TEREVERLFRIIRRLK-AQGVAIIYISHRLD 201
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
14-211 |
3.62e-05 |
|
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: 44.40 E-value: 3.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 14 VEISGLRFTYPgidghppPGSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGKHMVEPHMVRVLGrsafHDTGLT 93
Cdd:cd03252 1 ITFEHVRFRYK-------PDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDG----HDLALA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 94 SSGDL-----------CYLGGEWRRDVAFAGFEVPIQMDISAEKMIFGVAGIDpqrrdELIKVLDIDISWRLHKVSDGQR 162
Cdd:cd03252 70 DPAWLrrqvgvvlqenVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFIS-----ELPEGYDTIVGEQGAGLSGGQR 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 7406423 163 RRVQICMGLLKPFKVLLLDEITVDLDVLARADLLKFLRKECEERGATII 211
Cdd:cd03252 145 QRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIII 193
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
155-235 |
3.85e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 44.68 E-value: 3.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 155 HKVSDGQRRRVQICmGLL--KPfKVLLLDEITVDLDVLARADLLKFLrKECEERGATIIYATHIFDGLEDWPTHIVYVAN 232
Cdd:PRK13639 136 HHLSGGQKKRVAIA-GILamKP-EIIVLDEPTSGLDPMGASQIMKLL-YDLNKEGITIIISTHDVDLVPVYADKVYVMSD 212
|
...
gi 7406423 233 GKL 235
Cdd:PRK13639 213 GKI 215
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
33-215 |
4.14e-05 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 44.10 E-value: 4.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 33 GSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGkhMVEPHMVRVLgrSAFHDTGLTSSGDLCYLggewRRDVAFA 112
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICG--IERPSAGKIW--FSGHDITRLKNREVPFL----RRQIGMI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 113 GFEVPIQMD------ISAEKMIFGVAGIDPQRR--DELIKV--LDIDISWRLhKVSDGQRRRVQICMGLLKPFKVLLLDE 182
Cdd:PRK10908 85 FQDHHLLMDrtvydnVAIPLIIAGASGDDIRRRvsAALDKVglLDKAKNFPI-QLSGGEQQRVGIARAVVNKPAVLLADE 163
|
170 180 190
....*....|....*....|....*....|...
gi 7406423 183 ITVDLDVLARADLLKfLRKECEERGATIIYATH 215
Cdd:PRK10908 164 PTGNLDDALSEGILR-LFEEFNRVGVTVLMATH 195
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
36-188 |
4.38e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 44.07 E-value: 4.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 36 PLieDFSItlNSSDRCLLVGSNGAGKTTILKILGGKHMVEPHMVRVLGRSAFHdtgltssgdlcylgGEWRRDVAFAGFE 115
Cdd:PRK13543 29 PL--DFHV--DAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR--------------GDRSRFMAYLGHL 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7406423 116 VPIQMDISA-EKMIF--GVAGIDPQRR--DELIKVLDIDISWRL-HKVSDGQRRRVQICMGLLKPFKVLLLDEITVDLD 188
Cdd:PRK13543 91 PGLKADLSTlENLHFlcGLHGRRAKQMpgSALAIVGLAGYEDTLvRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
38-215 |
4.55e-05 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 44.61 E-value: 4.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 38 IEDFSITLNSsDRCLLVGSNGAGKTTILKILggKHMVEPHMVRVLGRSAFHDTGLTSSGDL---CYLGGEWRR---DVAF 111
Cdd:COG3593 14 IKDLSIELSD-DLTVLVGENNSGKSSILEAL--RLLLGPSSSRKFDEEDFYLGDDPDLPEIeieLTFGSLLSRllrLLLK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 112 AGFEVPIQMDISA--------------------EKMIFGVA---GIDPQRRDELIKVLDIDI----SWRLHKVSDGQRRR 164
Cdd:COG3593 91 EEDKEELEEALEElneelkealkalnellseylKELLDGLDlelELSLDELEDLLKSLSLRIedgkELPLDRLGSGFQRL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 7406423 165 VQICMGLL-------KPFKVLLLDEITVDLDVLARADLLKFLRKECEErGATIIYATH 215
Cdd:COG3593 171 ILLALLSAlaelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEK-PNQVIITTH 227
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
32-215 |
5.10e-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: 5.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 32 PGSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGG-------KHMVEPHM-VRVLGRSAFHDTGLTSSGDLCYLGG 103
Cdd:TIGR03719 15 PPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGvdkdfngEARPQPGIkVGYLPQEPQLDPTKTVRENVEEGVA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 104 EWRRDVA-----FAGF-EVPIQMDISAEKMIFGVAGIDPQRRDELIKVLDI--------DISWRLHKVSDGQRRRVQICM 169
Cdd:TIGR03719 95 EIKDALDrfneiSAKYaEPDADFDKLAAEQAELQEIIDAADAWDLDSQLEIamdalrcpPWDADVTKLSGGERRRVALCR 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 7406423 170 GLLKPFKVLLLDEITVDLDVLARADLLKFLRkeceERGATIIYATH 215
Cdd:TIGR03719 175 LLLSKPDMLLLDEPTNHLDAESVAWLERHLQ----EYPGTVVAVTH 216
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
14-218 |
6.39e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 43.95 E-value: 6.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 14 VEISGLRFTYPgidghpPPGSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGKHMVEPHMVRVLGR--------S 85
Cdd:PRK13650 5 IEVKNLTFKYK------EDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDllteenvwD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 86 AFHDTGLT-SSGDLCYLGGEWRRDVAFaGFEvpiQMDISAEKMIfgvagidpQRRDELIKVLDI-DISWRL-HKVSDGQR 162
Cdd:PRK13650 79 IRHKIGMVfQNPDNQFVGATVEDDVAF-GLE---NKGIPHEEMK--------ERVNEALELVGMqDFKEREpARLSGGQK 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 7406423 163 RRVQICMGL-LKPfKVLLLDEITVDLDVLARADLLKFLRKECEERGATIIYATHIFD 218
Cdd:PRK13650 147 QRVAIAGAVaMRP-KIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLD 202
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
32-235 |
7.24e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 43.66 E-value: 7.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 32 PGS---KPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGKHMVEPHMVRVLGrsaFHDTGLTSSGDLCYLggewRRD 108
Cdd:PRK13641 14 PGTpmeKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAG---YHITPETGNKNLKKL----RKK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 109 VAFAG-------FEVPIQMDISAEKMIFGVAgiDPQRRDELIKVL-DIDISWRL-----HKVSDGQRRRVQICMGLLKPF 175
Cdd:PRK13641 87 VSLVFqfpeaqlFENTVLKDVEFGPKNFGFS--EDEAKEKALKWLkKVGLSEDLiskspFELSGGQMRRVAIAGVMAYEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 176 KVLLLDEITVDLDVLARADLLKfLRKECEERGATIIYATHIFDGLEDWPTHIVYVANGKL 235
Cdd:PRK13641 165 EILCLDEPAAGLDPEGRKEMMQ-LFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
133-215 |
7.33e-05 |
|
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: 44.29 E-value: 7.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 133 GI-DPQRRdelikvldidISWRLHKVSDGQRRRVQICMGLL-KPfKVLLLDEITVDLDVLARA---DLLKFLRKeceERG 207
Cdd:COG4172 142 GIpDPERR----------LDAYPHQLSGGQRQRVMIAMALAnEP-DLLIADEPTTALDVTVQAqilDLLKDLQR---ELG 207
|
....*...
gi 7406423 208 ATIIYATH 215
Cdd:COG4172 208 MALLLITH 215
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
35-234 |
7.43e-05 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 44.27 E-value: 7.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 35 KPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGK---------------HMVEPHMVRVlgRSAF---HDT---GLT 93
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRspkgvkgsgsvllngMPIDAKEMRA--ISAYvqqDDLfipTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 94 SSGDLCYLggewrrdvafAGFEVPIQMDISaEKMifgvagidpQRRDELIKVLD--------IDISWRLHKVSDGQRRRV 165
Cdd:TIGR00955 116 VREHLMFQ----------AHLRMPRRVTKK-EKR---------ERVDEVLQALGlrkcantrIGVPGRVKGLSGGERKRL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7406423 166 QICMGLLKPFKVLLLDEITVDLDVLARADLLKFLRKECeERGATIIYATH-----IFDGLedwpTHIVYVANGK 234
Cdd:TIGR00955 176 AFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLA-QKGKTIICTIHqpsseLFELF----DKIILMAEGR 244
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-235 |
8.02e-05 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 44.05 E-value: 8.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 4 TEEEKKRNSTVEISGLRFTYPGidghpppGSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGKHMVEPHMVRVLG 83
Cdd:PRK11160 329 TSTAAADQVSLTLNNVSFTYPD-------QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNG 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 84 R--SAFHDTGLTS------------SGDLcylggewRRDVAFAgfevpiQMDISAEKMIfgvagiDPQRRDELIKVLDID 149
Cdd:PRK11160 402 QpiADYSEAALRQaisvvsqrvhlfSATL-------RDNLLLA------APNASDEALI------EVLQQVGLEKLLEDD 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 150 I---SW-----RlhKVSDGQRRRVQICMGLLKPFKVLLLDEITVDLDVLARADLLKFLRKECEERgaTIIYATHIFDGLE 221
Cdd:PRK11160 463 KglnAWlgeggR--QLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNK--TVLMITHRLTGLE 538
|
250
....*....|....*.
gi 7406423 222 --DwptHIVYVANGKL 235
Cdd:PRK11160 539 qfD---RICVMDNGQI 551
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
31-215 |
8.39e-05 |
|
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: 42.62 E-value: 8.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 31 PPGSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGKhmvephmvrvlgrsafhDTGLTSSGDLcYLGGEwRRDVA 110
Cdd:cd03232 16 KGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGR-----------------KTAGVITGEI-LINGR-PLDKN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 111 FA---GFeVPiQMDISAEKMIFGVAgidpqrrdelikvldIDISWRLHKVSDGQRRRVQICMGLL-KPFkVLLLDEITVD 186
Cdd:cd03232 77 FQrstGY-VE-QQDVHSPNLTVREA---------------LRFSALLRGLSVEQRKRLTIGVELAaKPS-ILFLDEPTSG 138
|
170 180
....*....|....*....|....*....
gi 7406423 187 LDVLARADLLKFLRKECEErGATIIYATH 215
Cdd:cd03232 139 LDSQAAYNIVRFLKKLADS-GQAILCTIH 166
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
38-68 |
1.10e-04 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 43.06 E-value: 1.10e-04
10 20 30
....*....|....*....|....*....|..
gi 7406423 38 IEDFSITLNSSDR-CLLVGSNGAGKTTILKIL 68
Cdd:COG3950 14 FEDLEIDFDNPPRlTVLVGENGSGKTTLLEAI 45
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
129-244 |
1.29e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 43.32 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 129 FGVAGIDPQRRDELIKVLDID-----ISWRLhkvSDGQRRRVQICMGLLKPFKVLLLDEITVDLDVLARADLLKFLRKEC 203
Cdd:PRK11144 99 YGMAKSMVAQFDKIVALLGIEplldrYPGSL---SGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLA 175
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 7406423 204 EERGATIIYATHIFDGLEDWPTHIVYVANGKLQLALPMEKV 244
Cdd:PRK11144 176 REINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
54-215 |
1.34e-04 |
|
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: 43.62 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 54 VGSNGAGKTTILKILGGkhMVEPhmvrvlgrsafhDTGLTSSGDlcylggewrrDVAFAGFEVPIQMDISAEKMIFGVAG 133
Cdd:COG1245 372 VGPNGIGKTTFAKILAG--VLKP------------DEGEVDEDL----------KISYKPQYISPDYDGTVEEFLRSANT 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 134 ID---PQRRDELIKVLDIDiswRLH--KVSD---GQRRRVQICMGLLKPFKVLLLDEITVDLDVLARADLLKFLRKECEE 205
Cdd:COG1245 428 DDfgsSYYKTEIIKPLGLE---KLLdkNVKDlsgGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAEN 504
|
170
....*....|
gi 7406423 206 RGATIIYATH 215
Cdd:COG1245 505 RGKTAMVVDH 514
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
4-199 |
1.62e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.31 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 4 TEEEKKRNSTVEISGLRFTYPGidghPPPGSKPLieDFSITLNSsdRCLLVGSNGAGKTTILKILGGKhmVEP------- 76
Cdd:PLN03073 499 TPDDRPGPPIISFSDASFGYPG----GPLLFKNL--NFGIDLDS--RIAMVGPNGIGKSTILKLISGE--LQPssgtvfr 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 77 -HMVRVLGRSAFHDTGLT-SSGDLCYLGGewrrdvAFAGfeVPIQmDISAEKMIFGVAG---IDPqrrdelikvldidis 151
Cdd:PLN03073 569 sAKVRMAVFSQHHVDGLDlSSNPLLYMMR------CFPG--VPEQ-KLRAHLGSFGVTGnlaLQP--------------- 624
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 7406423 152 wrLHKVSDGQRRRVQICMGLLKPFKVLLLDEITVDLDVLARADLLKFL 199
Cdd:PLN03073 625 --MYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGL 670
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
136-235 |
1.65e-04 |
|
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that maintains replication in the presence of DNA damage. When replication is prematurely disrupted by DNA damage, several recF pathway gene products play critical roles processing the arrested replication fork, allowing it to resume and complete its task. This CD represents the nucleotide binding domain of RecF. RecF belongs to a large superfamily of ABC transporters 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 with 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: 213209 [Multi-domain] Cd Length: 270 Bit Score: 42.67 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 136 PQRRDELIKVLDIDISWRlhkVSDGQRRRVQICMGL---------LKPFKVLLLDEITVDLDVLARADLLKFLrkecEER 206
Cdd:cd03242 166 PHRDDLLFFLNDKPAADF---GSQGQQRTLALALKLaeiqlikevSGEYPVLLLDDVLAELDLGRQAALLDAI----EGR 238
|
90 100 110
....*....|....*....|....*....|.
gi 7406423 207 GATIIYATHI--FDGLEDWPTHIVYVANGKL 235
Cdd:cd03242 239 VQTFVTTTDLadFDALWLRRAQIFRVDAGTL 269
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
33-234 |
1.78e-04 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 42.49 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 33 GSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGKHMVEPHMVRVLGRSafhdtgltssgdlcyLGGEWRRDVAFA 112
Cdd:PRK13537 18 GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEP---------------VPSRARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 113 GFeVPiQMD-------ISAEKMIFG-VAGIDPQRRDELIKVL------DIDISWRLHKVSDGQRRRVQICMGLLKPFKVL 178
Cdd:PRK13537 83 GV-VP-QFDnldpdftVRENLLVFGrYFGLSAAAARALVPPLlefaklENKADAKVGELSGGMKRRLTLARALVNDPDVL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 7406423 179 LLDEITVDLDVLARADLLKFLRkECEERGATIIYATHIFDGLEDWPTHIVYVANGK 234
Cdd:PRK13537 161 VLDEPTTGLDPQARHLMWERLR-SLLARGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
38-242 |
1.86e-04 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 42.71 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 38 IEDFSITLNSSDRCLLVGSNGAGKTTILKILggKHMVEPHMVRVLGRSAfhDTGLTSSGDLcylgGEWRRD---VAFAGF 114
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLL--NRLIEPTRGQVLIDGV--DIAKISDAEL----REVRRKkiaMVFQSF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 115 EVPIQMDIsAEKMIFG--VAGIDPQRRDEliKVLD----IDISWRLH----KVSDGQRRRVQICMGLLKPFKVLLLDEIT 184
Cdd:PRK10070 116 ALMPHMTV-LDNTAFGmeLAGINAEERRE--KALDalrqVGLENYAHsypdELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 7406423 185 VDLDVLARADLLKFLRKECEERGATIIYATHIFDGLEDWPTHIVYVANGK-LQLALPME 242
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEvVQVGTPDE 251
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
155-215 |
2.14e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 42.92 E-value: 2.14e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7406423 155 HKVSDGQRRRVQICMGLLKPFKVLLLDEITVDLDVLARADLLKFLRKECEERGATIIYATH 215
Cdd:PRK10261 167 HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITH 227
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
36-223 |
2.56e-04 |
|
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: 41.55 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 36 PLIEDFSITLNSSDRCLLVGSNGAGKTTIL-KILGgkhmvepHMVRVLGRsAFHDTGLTSSGDLCYLGGEWRRDVAFAGf 114
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLlAILG-------EMQTLEGK-VHWSNKNESEPSFEATRSRNRYSVAYAA- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 115 EVPIQMDISAEKMIFGVAGIDPQRRDELIKVL----DID---------ISWRLHKVSDGQRRRVQICMGLLKPFKVLLLD 181
Cdd:cd03290 86 QKPWLLNATVEENITFGSPFNKQRYKAVTDACslqpDIDllpfgdqteIGERGINLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 7406423 182 EITVDLDV-----LARADLLKFLRkeceERGATIIYATHIFDGL--EDW 223
Cdd:cd03290 166 DPFSALDIhlsdhLMQEGILKFLQ----DDKRTLVLVTHKLQYLphADW 210
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
40-87 |
2.93e-04 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 41.61 E-value: 2.93e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 7406423 40 DFSITLNSSDRCLLVGSNGAGKTTILKILGGkhMVEPH--MVRVLGRSAF 87
Cdd:COG1134 44 DVSFEVERGESVGIIGRNGAGKSTLLKLIAG--ILEPTsgRVEVNGRVSA 91
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
38-182 |
3.22e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 41.64 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 38 IEDFSITLNSSD-RCLlVGSNGAGKTTILKILGGKhmVEPHMVRVLgrsaFHDTGLTssgdlcylggewRRD---VAFAG 113
Cdd:COG4674 26 LNDLSLYVDPGElRVI-IGPNGAGKTTLMDVITGK--TRPDSGSVL----FGGTDLT------------GLDeheIARLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 114 ----FEVP-----------IQMDISAEKMIFGV--AGIDPQRRDELIKVLD-IDISWRLHKV----SDGQRRRVQICMGL 171
Cdd:COG4674 87 igrkFQKPtvfeeltvfenLELALKGDRGVFASlfARLTAEERDRIEEVLEtIGLTDKADRLagllSHGQKQWLEIGMLL 166
|
170
....*....|.
gi 7406423 172 LKPFKVLLLDE 182
Cdd:COG4674 167 AQDPKLLLLDE 177
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
33-70 |
3.91e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 42.24 E-value: 3.91e-04
10 20 30
....*....|....*....|....*....|....*...
gi 7406423 33 GSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGG 70
Cdd:PRK11147 14 SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNG 51
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
42-242 |
3.94e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 41.62 E-value: 3.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 42 SITLNSSDRCLLVGSNGAGKTTILKILGGKHMVEPHMVRVLGRSAFHDT--------GLT-SSGDLCYLGGEWRRDVAFa 112
Cdd:PRK13642 27 SFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENvwnlrrkiGMVfQNPDNQFVGATVEDDVAF- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 113 GFEvpiQMDISAEKMIfgvagidpQRRDE-LIKVLDIDISWRL-HKVSDGQRRRVQIC-MGLLKPfKVLLLDEITVDLDV 189
Cdd:PRK13642 106 GME---NQGIPREEMI--------KRVDEaLLAVNMLDFKTREpARLSGGQKQRVAVAgIIALRP-EIIILDESTSMLDP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 7406423 190 LARADLLKFLRKECEERGATIIYATHIFDGLEDWPTHIVYVANGKLQLALPME 242
Cdd:PRK13642 174 TGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSE 226
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
156-259 |
7.98e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 40.53 E-value: 7.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 156 KVSDGQRRRVQICMGLLKPFKVLLLDEITVDLDVLARADLLKFLRKECEERGATIIYATHIFDGLEDWPTHIVYVANGKL 235
Cdd:PRK13646 145 QMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
90 100
....*....|....*....|....*..
gi 7406423 236 qlalpmekVKETSKKSLMRT---VESW 259
Cdd:PRK13646 225 --------VSQTSPKELFKDkkkLADW 243
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
35-215 |
8.40e-04 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 40.59 E-value: 8.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 35 KPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGkhMVEPhmvrvlgrsafhdtgltSSGDLCYLGgewrRDVA-FAG 113
Cdd:PRK11607 32 QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAG--FEQP-----------------TAGQIMLDG----VDLShVPP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 114 FEVPIQM---------DISAEKMI-FGVagidpqRRDELIKVldiDISWRL-----------------HKVSDGQRRRVQ 166
Cdd:PRK11607 89 YQRPINMmfqsyalfpHMTVEQNIaFGL------KQDKLPKA---EIASRVnemlglvhmqefakrkpHQLSGGQRQRVA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 7406423 167 ICMGLLKPFKVLLLDEITVDLDVLARaDLLKFLRKECEER-GATIIYATH 215
Cdd:PRK11607 160 LARSLAKRPKLLLLDEPMGALDKKLR-DRMQLEVVDILERvGVTCVMVTH 208
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
12-215 |
2.22e-03 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 39.10 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 12 STVEISGLRFTYPgiDGHPPpgskplIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGkhmvephMVRVlgrsafhdtg 91
Cdd:PRK15056 5 AGIVVNDVTVTWR--NGHTA------LRDASFTVPGGSIAALVGVNGSGKSTLFKALMG-------FVRL---------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 92 ltSSGDLCYLGGEWRRD-----VAFA--GFEVPIQMDISAEKMI----FGVAGI-------DPQRRDELIKVLDI-DISW 152
Cdd:PRK15056 60 --ASGKISILGQPTRQAlqknlVAYVpqSEEVDWSFPVLVEDVVmmgrYGHMGWlrrakkrDRQIVTAALARVDMvEFRH 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7406423 153 R-LHKVSDGQRRRVQICMGLLKPFKVLLLDEITVDLDVLARADLLKFLRkECEERGATIIYATH 215
Cdd:PRK15056 138 RqIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLR-ELRDEGKTMLVSTH 200
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
158-215 |
3.27e-03 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 38.91 E-value: 3.27e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7406423 158 SDGQRRRVQICMGL-LKPfKVLLLDEITVDLD------VLaraDLLKFLRKeceERGATIIYATH 215
Cdd:COG1135 142 SGGQKQRVGIARALaNNP-KVLLCDEATSALDpettrsIL---DLLKDINR---ELGLTIVLITH 199
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
158-215 |
3.31e-03 |
|
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: 38.28 E-value: 3.31e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7406423 158 SDGQRRRVQICMGL-LKPfKVLLLDEITVDLD------VLaraDLLKFLRKEceerGATIIYATH 215
Cdd:cd03262 137 SGGQQQRVAIARALaMNP-KVMLFDEPTSALDpelvgeVL---DVMKDLAEE----GMTMVVVTH 193
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
33-251 |
4.46e-03 |
|
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: 37.89 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 33 GSKPLIEDFSITLNSSDRCLLVGSNGAGKTTILKILGGKHMVEPhmvrVLGRSAFHDTGLTSsgdlcyLGGEWR-RDVAF 111
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEV----TEGEILFKGEDITD------LPPEERaRLGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7406423 112 AGFEVPIQMDisaekmifGVAGIDPQRrdelikvlDIDISWrlhkvSDGQRRRVQIC-MGLLKPfKVLLLDEITVDLDVL 190
Cdd:cd03217 81 LAFQYPPEIP--------GVKNADFLR--------YVNEGF-----SGGEKKRNEILqLLLLEP-DLAILDEPDSGLDID 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7406423 191 AR---ADLLKFLRKEceerGATIIYATH---IFDGLEDWPTHIVYvaNGKLQLALPMEKVKETSKKS 251
Cdd:cd03217 139 ALrlvAEVINKLREE----GKSVLIITHyqrLLDYIKPDRVHVLY--DGRIVKSGDKELALEIEKKG 199
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
155-215 |
7.77e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 37.64 E-value: 7.77e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7406423 155 HKVSDGQRRRVQICMGL-LKPfKVLLLDEITVDLDVLARADLLKFLRKECEERGATIIYATH 215
Cdd:PRK11308 153 HMFSGGQRQRIAIARALmLDP-DVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISH 213
|
|
| |
