|
Name |
Accession |
Description |
Interval |
E-value |
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
31-237 |
7.65e-31 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 115.16 E-value: 7.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 31 DFNLDLPAGSRCLLVGANGSGKTTLLKILAG-KHMVGGKnvVQVLDRSAFHDTELVCSgDLSYLggswsktagsAGDIPL 109
Cdd:COG1131 18 GVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGlLRPTSGE--VRVLGEDVARDPAEVRR-RIGYV----------PQEPAL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 110 QGDFSA-EHMIF--GVEGIDPFRREKLID-LLDI-NLQWRMHKV----SDGQRRRVQICMGLLHPFKVLLLDEVTVDLDV 180
Cdd:COG1131 85 YPDLTVrENLRFfaRLYGLPRKEARERIDeLLELfGLTDAADRKvgtlSGGMKQRLGLALALLHDPELLILDEPTSGLDP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15240093 181 VARMDLLEFFKEECEQrGATIVYATHIFDGLETWASHLAYINGGELKLSAKLDEIKD 237
Cdd:COG1131 165 EARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKA 220
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
13-244 |
7.28e-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: 112.64 E-value: 7.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 13 IRVSGMQFSYDvQDPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAGKhMVGGKNVVQVLDRSAFHDTELVcSGDLSY 92
Cdd:COG4555 2 IEVENLSKKYG-KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGL-LKPDSGSILIDGEDVRKEPREA-RRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 93 LGGswsktagsagDIPLQGDFSAEHMI------FGVEGID-PFRREKLIDLLDIN--LQWRMHKVSDGQRRRVQICMGLL 163
Cdd:COG4555 79 LPD----------ERGLYDRLTVRENIryfaelYGLFDEElKKRIEELIELLGLEefLDRRVGELSTGMKKKVALARALV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 164 HPFKVLLLDEVTVDLDVVARMDLLEFFKeECEQRGATIVYATHIFDGLETWASHLAYINGGELKLSAKLDEIKDLKTSPN 243
Cdd:COG4555 149 HDPKVLLLDEPTNGLDVMARRLLREILR-ALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEEN 227
|
.
gi 15240093 244 L 244
Cdd:COG4555 228 L 228
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
13-226 |
2.06e-29 |
|
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: 109.41 E-value: 2.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 13 IRVSGMQFSYDVQdPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAGkhmvggknvvqVLDRSafhdtelvcSGDLSY 92
Cdd:cd03230 1 IEVRNLSKRYGKK-TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILG-----------LLKPD---------SGEIKV 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 93 LGGSWSKTAGSAgdiplqgdfsaeHMIFGV--EGIDPFRREKLIDLLdinlqwrmhKVSDGQRRRVQICMGLLHPFKVLL 170
Cdd:cd03230 60 LGKDIKKEPEEV------------KRRIGYlpEEPSLYENLTVRENL---------KLSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15240093 171 LDEVTVDLDVVARMDLLEFFKEECeQRGATIVYATHIFDGLETWASHLAYINGGEL 226
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELK-KEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
13-226 |
8.19e-26 |
|
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: 101.64 E-value: 8.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 13 IRVSGMQFSYDVQD--------------------PIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAGK-HMVGGKnvV 71
Cdd:cd03267 1 IEVSNLSKSYRVYSkepgligslkslfkrkyrevEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLlQPTSGE--V 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 72 QVLD------RSAFHDTELVCSGDLSYLggSWsktagsagDIPLQGDFSAEHMIFGvegIDPF----RREKLIDLLDIN- 140
Cdd:cd03267 79 RVAGlvpwkrRKKFLRRIGVVFGQKTQL--WW--------DLPVIDSFYLLAAIYD---LPPArfkkRLDELSELLDLEe 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 141 -LQWRMHKVSDGQRRRVQICMGLLHPFKVLLLDEVTVDLDVVARMDLLEFFKEECEQRGATIVYATHIFDGLETWASHLA 219
Cdd:cd03267 146 lLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVL 225
|
....*..
gi 15240093 220 YINGGEL 226
Cdd:cd03267 226 VIDKGRL 232
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
20-225 |
8.37e-25 |
|
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: 98.31 E-value: 8.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 20 FSYDVQD-PIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAG-KHMVGGKnvVQVLDRSAFHDTelvcsgdlsylGGSW 97
Cdd:cd03225 7 FSYPDGArPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGlLGPTSGE--VLVDGKDLTKLS-----------LKEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 98 SKTAGSAgdipLQgdfSAEHMIFG--VE----------GIDPFRREKLID------LLDINLQWRMHKVSDGQRRRVQIC 159
Cdd:cd03225 74 RRKVGLV----FQ---NPDDQFFGptVEeevafglenlGLPEEEIEERVEealelvGLEGLRDRSPFTLSGGQKQRVAIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15240093 160 MGLLHPFKVLLLDEVTVDLDVVARMDLLEFFKEECEQrGATIVYATHIFDGLETWASHLAYINGGE 225
Cdd:cd03225 147 GVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
14-225 |
2.15e-24 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 95.77 E-value: 2.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 14 RVSGMQFSYDvQDPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAGKhmvggknvvqvldrsafhdtELVCSGDLSYL 93
Cdd:cd00267 1 EIENLSFRYG-GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGL--------------------LKPTSGEILID 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 94 GGSWSKtagsagdiplqgdfsaehmifgvegIDPFRREKLIDLLdinlqwrmHKVSDGQRRRVQICMGLLHPFKVLLLDE 173
Cdd:cd00267 60 GKDIAK-------------------------LPLEELRRRIGYV--------PQLSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15240093 174 VTVDLDVVARMDLLEFFKEECeQRGATIVYATHIFDGLETWASHLAYINGGE 225
Cdd:cd00267 107 PTSGLDPASRERLLELLRELA-EEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
13-206 |
7.90e-24 |
|
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: 95.62 E-value: 7.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 13 IRVSGMQFSYDvQDPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILA-------GKHMVGGKNVVQvlDRSAFHdtelv 85
Cdd:COG4133 3 LEAENLSCRRG-ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAgllppsaGEVLWNGEPIRD--AREDYR----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 86 csGDLSYLGgswsktagsaGDIPLQGDFSA-EHMIF-----GVegidPFRREKLIDLLD-INLQWRMHK----VSDGQRR 154
Cdd:COG4133 75 --RRLAYLG----------HADGLKPELTVrENLRFwaalyGL----RADREAIDEALEaVGLAGLADLpvrqLSAGQKR 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15240093 155 RVQICMGLLHPFKVLLLDEVTVDLDVVARMDLLEFFKEECEQRGAtIVYATH 206
Cdd:COG4133 139 RVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGA-VLLTTH 189
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
13-235 |
1.39e-22 |
|
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: 93.17 E-value: 1.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 13 IRVSGMQFSYDVQDPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAG--KHMVGgknVVQVLDRSafhdtelVCSGDL 90
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGllKPTSG---EVLVDGKD-------ITKKNL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 91 SYLggswSKTAGsagdIPLQgdfSAEHMIFG--VE----------GIDPFRREK----------LIDLLDINLqwrmHKV 148
Cdd:COG1122 71 REL----RRKVG----LVFQ---NPDDQLFAptVEedvafgpenlGLPREEIRErveealelvgLEHLADRPP----HEL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 149 SDGQRRRVQICmGLL--HPfKVLLLDEVTVDLDVVARMDLLEFFKeECEQRGATIVYATHIFDGLETWASHLAYINGGEL 226
Cdd:COG1122 136 SGGQKQRVAIA-GVLamEP-EVLVLDEPTAGLDPRGRRELLELLK-RLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRI 212
|
....*....
gi 15240093 227 KLSAKLDEI 235
Cdd:COG1122 213 VADGTPREV 221
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
31-237 |
1.81e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 88.99 E-value: 1.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 31 DFNLDLPAGSRCLLVGANGSGKTTLLKILAG-KHMVGGKnvVQVLDRSAFHD-TEL-----VCSGDLSYLggSWsktags 103
Cdd:COG4586 40 DISFTIEPGEIVGFIGPNGAGKSTTIKMLTGiLVPTSGE--VRVLGYVPFKRrKEFarrigVVFGQRSQL--WW------ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 104 agDIPLQGDFSAEHMIFGVEGiDPFRR--EKLIDLLDIN--LQWRMHKVSDGQRRRVQICMGLLHPFKVLLLDEVTVDLD 179
Cdd:COG4586 110 --DLPAIDSFRLLKAIYRIPD-AEYKKrlDELVELLDLGelLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLD 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15240093 180 VVARMDLLEFFKEECEQRGATIVYATHIFDGLETWASHLAYINGGELKLSAKLDEIKD 237
Cdd:COG4586 187 VVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKE 244
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
12-226 |
2.64e-20 |
|
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: 87.41 E-value: 2.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 12 AIRVSGMQFSYDvQDPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAGKH-------MVGGKNVVQvLDRSAF----- 79
Cdd:COG1120 1 MLEAENLSVGYG-GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLkpssgevLLDGRDLAS-LSRRELarria 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 80 -----HDT-------ELVCSGDLSYLG--GSWSKTagsagDiplqgdfsaEHMIfgvegidpfrrEKLIDLLDI-NLQWR 144
Cdd:COG1120 79 yvpqePPApfgltvrELVALGRYPHLGlfGRPSAE-----D---------REAV-----------EEALERTGLeHLADR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 145 -MHKVSDGQRRRVQICMGLLHPFKVLLLDEVTVDLDVVARMDLLEFFKEECEQRGATIVYATHifDgLE---TWASHLAY 220
Cdd:COG1120 134 pVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLH--D-LNlaaRYADRLVL 210
|
....*.
gi 15240093 221 INGGEL 226
Cdd:COG1120 211 LKDGRI 216
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
27-206 |
8.73e-20 |
|
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: 85.91 E-value: 8.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 27 PIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAGKHMVGGKNVVQVLDR-----SAFhdtEL-----VCSGDLsylggs 96
Cdd:COG1119 17 TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRLFGErrggeDVW---ELrkrigLVSPAL------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 97 wsktagsAGDIPlqGDFSAEHMI----FGVegIDPFRR---------EKLIDLLDIN--LQWRMHKVSDGQRRRVQICMG 161
Cdd:COG1119 88 -------QLRFP--RDETVLDVVlsgfFDS--IGLYREptdeqreraRELLELLGLAhlADRPFGTLSQGEQRRVLIARA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15240093 162 LLHPFKVLLLDEVTVDLDVVARMDLLEFFKEECEQRGATIVYATH 206
Cdd:COG1119 157 LVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTH 201
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
12-235 |
1.88e-19 |
|
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: 87.65 E-value: 1.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 12 AIRVSGMQFSYDVQD-PIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAG----KHMVGGKnvVQVLDRSAFHDTELVC 86
Cdd:COG1123 4 LLEVRDLSVRYPGGDvPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllphGGRISGE--VLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 87 SGDLSYLGGSwsktAGSAGDIPLQGDFSAEHMIfgVEGIDPF-RREKLIDLLD-INLQWRM----HKVSDGQRRRVQICM 160
Cdd:COG1123 82 GRRIGMVFQD----PMTQLNPVTVGDQIAEALE--NLGLSRAeARARVLELLEaVGLERRLdrypHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15240093 161 GLLHPFKVLLLDEVTVDLDVVARMDLLEFFKEECEQRGATIVYATHIFDGLETWASHLAYINGGELKLSAKLDEI 235
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
12-224 |
5.17e-19 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 83.60 E-value: 5.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 12 AIRVSGMQFSYDvQDPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKIL-------AGKHMVGGKNVVQVLDR-------S 77
Cdd:COG1121 6 AIELENLTVSYG-GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAIlgllpptSGTVRLFGKPPRRARRRigyvpqrA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 78 AFHDT------ELVCSGDLSYLGgswsktagsagdipLQGDFSAEHmifgvegidpfrREKLIDLLD-INLQ----WRMH 146
Cdd:COG1121 85 EVDWDfpitvrDVVLMGRYGRRG--------------LFRRPSRAD------------REAVDEALErVGLEdladRPIG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15240093 147 KVSDGQRRRVQICMGLLHPFKVLLLDEVTVDLDVVARMDLLEFFKEECeQRGATIVYATHIFDGLETWASHLAYINGG 224
Cdd:COG1121 139 ELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELR-REGKTILVVTHDLGAVREYFDRVLLLNRG 215
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
13-206 |
5.44e-19 |
|
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: 82.92 E-value: 5.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 13 IRVSGMQFSYDVQD---PIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAGkhmvggknvvqvLDRSAfhdtelvcSGD 89
Cdd:cd03255 1 IELKNLSKTYGGGGekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGG------------LDRPT--------SGE 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 90 LSYLGgswsKTAGSAGDIPLqGDFSAEHM--IF----------------------GVEGIDpfRREKLIDLLD-INLQWR 144
Cdd:cd03255 61 VRVDG----TDISKLSEKEL-AAFRRRHIgfVFqsfnllpdltalenvelplllaGVPKKE--RRERAEELLErVGLGDR 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15240093 145 MHK----VSDGQRRRVQICMGLLHPFKVLLLDEVTVDLDVVARMDLLEFFKEECEQRGATIVYATH 206
Cdd:cd03255 134 LNHypseLSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTH 199
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
31-236 |
5.89e-19 |
|
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: 82.94 E-value: 5.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 31 DFNLDLPAGSrCL-LVGANGSGKTTLLKILAGKH-------MVGGKNVVQvlDRSAFHDTELVCSGDlsylggswsktag 102
Cdd:cd03263 20 DLSLNVYKGE-IFgLLGHNGAGKTTTLKMLTGELrptsgtaYINGYSIRT--DRKAARQSLGYCPQF------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 103 sagDIpLQGDFSA-EHMIF-----GV-EGIDPFRREKLIDLLDINLQW--RMHKVSDGQRRRVQICMGLLHPFKVLLLDE 173
Cdd:cd03263 84 ---DA-LFDELTVrEHLRFyarlkGLpKSEIKEEVELLLRVLGLTDKAnkRARTLSGGMKRKLSLAIALIGGPSVLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15240093 174 VTVDLDVVARMDLLEFFKEecEQRGATIVYATHIFDGLETWASHLAYINGGELKLSAKLDEIK 236
Cdd:cd03263 160 PTSGLDPASRRAIWDLILE--VRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
14-206 |
3.13e-18 |
|
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: 80.17 E-value: 3.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 14 RVSGMQFSYDvQDPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAGKH-------MVGGKNVVQvLDRSAFhdtelvc 86
Cdd:cd03214 1 EVENLSVGYG-GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLkpssgeiLLDGKDLAS-LSPKEL------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 87 SGDLSYLggswsktagsagdipLQgdfSAEHMifgveGIDPFrREKLIDLLdinlqwrmhkvSDGQRRRVQICMGLLHPF 166
Cdd:cd03214 72 ARKIAYV---------------PQ---ALELL-----GLAHL-ADRPFNEL-----------SGGERQRVLLARALAQEP 116
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15240093 167 KVLLLDEVTVDLDVVARMDLLEFFKEECEQRGATIVYATH 206
Cdd:cd03214 117 PILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLH 156
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-212 |
6.19e-18 |
|
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: 83.28 E-value: 6.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 2 AEKNASAVDGAIRVSGMQFSYDVQD-PIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILA-------GKHMVGGKNVVQv 73
Cdd:COG4987 323 AEPAPAPGGPSLELEDVSFRYPGAGrPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLrfldpqsGSITLGGVDLRD- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 74 LDRSAFHDTELVCSGDlSYLggsWSKT--------AGSAGDiplqgdfsaEHMIFGVE--GIDPFRREkLIDLLDINLQW 143
Cdd:COG4987 402 LDEDDLRRRIAVVPQR-PHL---FDTTlrenlrlaRPDATD---------EELWAALErvGLGDWLAA-LPDGLDTWLGE 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15240093 144 RMHKVSDGQRRRVQICMGLLHPFKVLLLDEVTVDLDVVARMDLLEFFKEECEQRgaTIVYATHIFDGLE 212
Cdd:COG4987 468 GGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLAGLE 534
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
44-226 |
7.84e-18 |
|
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: 80.10 E-value: 7.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 44 LVGANGSGKTTLLKILA-------GKHMVGGKNVVQ----VLDRSAFHDT------ELVCSGDLSYLGGswsktagsagd 106
Cdd:cd03266 36 LLGPNGAGKTTTLRMLAgllepdaGFATVDGFDVVKepaeARRRLGFVSDstglydRLTARENLEYFAG----------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 107 iplqgdfsaehmIFGVEGiDPF--RREKLIDLLDIN--LQWRMHKVSDGQRRRVQICMGLLHPFKVLLLDEVTVDLDVVA 182
Cdd:cd03266 105 ------------LYGLKG-DELtaRLEELADRLGMEelLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15240093 183 RMDLLEFFKEECEQrGATIVYATHIFDGLETWASHLAYINGGEL 226
Cdd:cd03266 172 TRALREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
31-236 |
3.26e-17 |
|
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: 78.18 E-value: 3.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 31 DFNLDLPAGSRCLLVGANGSGKTTLLKILA-------GKHMVGGKNVVQvldrsafhDTELVcsgdlsylggswSKTAGS 103
Cdd:cd03265 18 GVSFRVRRGEIFGLLGPNGAGKTTTIKMLTtllkptsGRATVAGHDVVR--------EPREV------------RRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 104 AG-DIPLQGDFSA-EHM-----IFGVEGIDpfRREKLIDLLD-INLQWRMHKV----SDGQRRRVQICMGLLHPFKVLLL 171
Cdd:cd03265 78 VFqDLSVDDELTGwENLyiharLYGVPGAE--RRERIDELLDfVGLLEAADRLvktySGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15240093 172 DEVTVDLDVVARMDLLEFFKEECEQRGATIVYATHIFDGLETWASHLAYINGGELKLSAKLDEIK 236
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
13-229 |
6.47e-17 |
|
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: 77.23 E-value: 6.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 13 IRVSGMQFSYDVQDpIFFDFNLDLPAGSRCLLvGANGSGKTTLLKILAG-KHMVGGKNVVQVLD----RSAFHDTelvcs 87
Cdd:cd03264 1 LQLENLTKRYGKKR-ALDGVSLTLGPGMYGLL-GPNGAGKTTLMRILATlTPPSSGTIRIDGQDvlkqPQKLRRR----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 88 gdLSYLggswsktagsAGDIPLQGDFSAE----HMIFgVEGIDPFRREKLID--LLDINLQWRMHK----VSDGQRRRVQ 157
Cdd:cd03264 74 --IGYL----------PQEFGVYPNFTVRefldYIAW-LKGIPSKEVKARVDevLELVNLGDRAKKkigsLSGGMRRRVG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15240093 158 ICMGLLHPFKVLLLDEVTVDLDVVARMDLLEFFKEECEQRgaTIVYATHIFDGLETWASHLAYINGGELKLS 229
Cdd:cd03264 141 IAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
7-206 |
7.11e-17 |
|
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: 80.02 E-value: 7.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 7 SAVDGAIRVSGMQFSYDVQDPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAGkHMVGGKNVVQVLDRSAFHDTELVC 86
Cdd:TIGR02857 316 AAPASSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLG-FVDPTEGSIAVNGVPLADADADSW 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 87 SGDLSYLGGSWSKTAGS-AGDIPL-QGDFSAEHMIFGVE--GIDPFRREkLIDLLDINLQWRMHKVSDGQRRRVQICMGL 162
Cdd:TIGR02857 395 RDQIAWVPQHPFLFAGTiAENIRLaRPDASDAEIREALEraGLDEFVAA-LPQGLDTPIGEGGAGLSGGQAQRLALARAF 473
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15240093 163 LHPFKVLLLDEVTVDLDVVARMDLLEFFKEECeqRGATIVYATH 206
Cdd:TIGR02857 474 LRDAPLLLLDEPTAHLDAETEAEVLEALRALA--QGRTVLLVTH 515
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
12-206 |
1.19e-16 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 77.01 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 12 AIRVSGMQFSYDVQD---PIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILA-------GKHMVGGKNVVQvLDRSA--- 78
Cdd:COG1136 4 LLELRNLTKSYGTGEgevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGgldrptsGEVLIDGQDISS-LSERElar 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 79 ---------FHDTELvcsgdLSYLggswsktagSAGD---IPLqgdfsaehMIFGVEGIDpfRREKLIDLLD-INLQWRM 145
Cdd:COG1136 83 lrrrhigfvFQFFNL-----LPEL---------TALEnvaLPL--------LLAGVSRKE--RRERARELLErVGLGDRL 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15240093 146 HK----VSDGQRRRVQICMGLLHPFKVLLLDEVTVDLDVVARMDLLEFFKEECEQRGATIVYATH 206
Cdd:COG1136 139 DHrpsqLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTH 203
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
31-176 |
1.63e-16 |
|
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: 74.61 E-value: 1.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 31 DFNLDLPAGSRCLLVGANGSGKTTLLKILAGKHM-VGGKnvVQVLDRSAFHDTELVCSGDLSYLGgswsktagsaGDIPL 109
Cdd:pfam00005 3 NVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSpTEGT--ILLDGQDLTDDERKSLRKEIGYVF----------QDPQL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 110 QGDFSA-EHMIFGVEGIDPFRREK------------LIDLLDINLQWRMHKVSDGQRRRVQICMGLLHPFKVLLLDEVTV 176
Cdd:pfam00005 71 FPRLTVrENLRLGLLLKGLSKREKdaraeealeklgLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
31-206 |
1.83e-16 |
|
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: 76.39 E-value: 1.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 31 DFNLDLPAGSRCLLVGANGSGKTTLLKILAG-KHMVGGKnvvqVLdrsaFHDTelvcsgDLSYLGGSWSKTAGSA-GDIP 108
Cdd:cd03257 23 DVSFSIKKGETLGLVGESGSGKSTLARAILGlLKPTSGS----II----FDGK------DLLKLSRRLRKIRRKEiQMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 109 lQGDFSA--------EH-----MIFGVEGIDPFRREKLIDLLD-INLQWRM-----HKVSDGQRRRVQICMGL-LHPfKV 168
Cdd:cd03257 89 -QDPMSSlnprmtigEQiaeplRIHGKLSKKEARKEAVLLLLVgVGLPEEVlnrypHELSGGQRQRVAIARALaLNP-KL 166
|
170 180 190
....*....|....*....|....*....|....*...
gi 15240093 169 LLLDEVTVDLDVVARMDLLEFFKEECEQRGATIVYATH 206
Cdd:cd03257 167 LIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITH 204
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
31-206 |
2.15e-16 |
|
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: 76.02 E-value: 2.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 31 DFNLDLPAGSRCLLVGANGSGKTTLLKILAGkhmvggknvvqvLDRsafhdtelVCSGDLSYLGGSWSKTAGSAGDIPL- 109
Cdd:cd03259 18 DLSLTVEPGEFLALLGPSGCGKTTLLRLIAG------------LER--------PDSGEILIDGRDVTGVPPERRNIGMv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 110 -QgDFS-------AEHMIFGVEGIDPFRREK------LIDLLDIN--LQWRMHKVSDGQRRRVQICMGLLHPFKVLLLDE 173
Cdd:cd03259 78 fQ-DYAlfphltvAENIAFGLKLRGVPKAEIrarvreLLELVGLEglLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190
....*....|....*....|....*....|...
gi 15240093 174 VTVDLDVVARMDLLEFFKEECEQRGATIVYATH 206
Cdd:cd03259 157 PLSALDAKLREELREELKELQRELGITTIYVTH 189
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
27-206 |
1.19e-15 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 73.42 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 27 PIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAG--KHMVG------GKNVVQVLDRSAFHDTELVCSGDLSYLGgSWS 98
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGvlRPTSGtvrragGARVAYVPQRSEVPDSLPLTVRDLVAMG-RWA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 99 KtAGSAGDIPLQGDFSAEHMIFGVeGIDPFRREKLIDLldinlqwrmhkvSDGQRRRVQICMGLLHPFKVLLLDEVTVDL 178
Cdd:NF040873 85 R-RGLWRRLTRDDRAAVDDALERV-GLADLAGRQLGEL------------SGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180
....*....|....*....|....*...
gi 15240093 179 DVVARMDLLEFFKEECEqRGATIVYATH 206
Cdd:NF040873 151 DAESRERIIALLAEEHA-RGATVVVVTH 177
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
13-225 |
2.40e-15 |
|
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: 72.22 E-value: 2.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 13 IRVSGMQFSYDvQDPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAGkhmvggknvvqvLDRSAfhdtelvcSGDLSY 92
Cdd:cd03229 1 LELKNVSKRYG-QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAG------------LEEPD--------SGSILI 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 93 LGGSWskTAGSAGDIPLQGDFSaehMIFgvegidpfRREKLIDLLDInLQWRMHKVSDGQRRRVQICMGLLHPFKVLLLD 172
Cdd:cd03229 60 DGEDL--TDLEDELPPLRRRIG---MVF--------QDFALFPHLTV-LENIALGLSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15240093 173 EVTVDLDVVARMDLLEFFKEECEQRGATIVYATHIFDGLETWASHLAYINGGE 225
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
14-224 |
2.71e-15 |
|
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: 72.95 E-value: 2.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 14 RVSGMQFSYDVQdPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILA-------GKHMVGGKNVVQVLDRSAF------H 80
Cdd:cd03235 1 EVEDLTVSYGGH-PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILgllkptsGSIRVFGKPLEKERKRIGYvpqrrsI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 81 DT-------ELVCSGDLSYLGgsWSKTAGSAgdiplqgDFS-AEHMIFGVeGIDPFrREKLIDLLdinlqwrmhkvSDGQ 152
Cdd:cd03235 80 DRdfpisvrDVVLMGLYGHKG--LFRRLSKA-------DKAkVDEALERV-GLSEL-ADRQIGEL-----------SGGQ 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15240093 153 RRRVQICMGLLHPFKVLLLDEVTVDLDVVARMDLLEFFKEECeQRGATIVYATHIFDGLETWASHLAYINGG 224
Cdd:cd03235 138 QQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELR-REGMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
13-206 |
3.21e-15 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 72.78 E-value: 3.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 13 IRVSGMQFSYDVQDPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILA-------GKHMVGGKNVVQvLDRSA------- 78
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYgeerptsGQVLVNGQDLSR-LKRREipylrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 79 ----FHDTELvcsgdLSYLggswsktagSAGD---IPLQgdfsaehmifgVEGIDP-FRREKLIDLLD-INLQWRMHK-- 147
Cdd:COG2884 81 igvvFQDFRL-----LPDR---------TVYEnvaLPLR-----------VTGKSRkEIRRRVREVLDlVGLSDKAKAlp 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15240093 148 --VSDGQRRRVQICMGLLHPFKVLLLDEVTVDLDVVARMDLLEFFKEECeQRGATIVYATH 206
Cdd:COG2884 136 heLSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEIN-RRGTTVLIATH 195
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
13-206 |
6.53e-15 |
|
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: 74.17 E-value: 6.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 13 IRVSGMQFSYDVQDPIFF----DFNLDLPAGSRCLLVGANGSGKTTLLKILAGkhmvggknvvqvLDRSAfhdtelvcSG 88
Cdd:COG1123 261 LEVRNLSKRYPVRGKGGVravdDVSLTLRRGETLGLVGESGSGKSTLARLLLG------------LLRPT--------SG 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 89 DLSYLGGSWSKTAGSA-------------------------GDI---PL--QGDFSAEHmifgvegidpfRREKLIDLLD 138
Cdd:COG1123 321 SILFDGKDLTKLSRRSlrelrrrvqmvfqdpysslnprmtvGDIiaePLrlHGLLSRAE-----------RRERVAELLE 389
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15240093 139 -INLQWRM-----HKVSDGQRRRVQICMGL-LHPfKVLLLDEVTVDLDVVARMDLLEFFKEECEQRGATIVYATH 206
Cdd:COG1123 390 rVGLPPDLadrypHELSGGQRQRVAIARALaLEP-KLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISH 463
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
31-226 |
6.66e-15 |
|
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: 71.48 E-value: 6.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 31 DFNLDLPAGSRCLLVGANGSGKTTLLKILAGkhmvggknvvqvLDRSAfhdtelvcSGDLSYLGGSWSKTA------GSA 104
Cdd:cd03268 18 DISLHVKKGEIYGFLGPNGAGKTTTMKIILG------------LIKPD--------SGEITFDGKSYQKNIealrriGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 105 GDIP-LQGDFSAEHMiFGVEGIDPFRREKLID-LLDI-NLQWRMHK----VSDGQRRRVQICMGLLHPFKVLLLDEVTVD 177
Cdd:cd03268 78 IEAPgFYPNLTAREN-LRLLARLLGIRKKRIDeVLDVvGLKDSAKKkvkgFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15240093 178 LDVVARMDLLEFFKEECEQrGATIVYATHIFDGLETWASHLAYINGGEL 226
Cdd:cd03268 157 LDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
13-206 |
8.15e-15 |
|
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: 70.49 E-value: 8.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 13 IRVSGMQFSYDVQD-PIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAGkhmvggknvvqvldrsaFHDTElvcsgdls 91
Cdd:cd03228 1 IEFKNVSFSYPGRPkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLR-----------------LYDPT-------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 92 ylggswsktagsAGDIPLQGdfsaehmifgvegidpfrreklIDLLDINLQWRMHKV-------------------SDGQ 152
Cdd:cd03228 56 ------------SGEILIDG----------------------VDLRDLDLESLRKNIayvpqdpflfsgtirenilSGGQ 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15240093 153 RRRVQICMGLLHPFKVLLLDEVTVDLDVVARMDLLEFFKEECEQRgaTIVYATH 206
Cdd:cd03228 102 RQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAKGK--TVIVIAH 153
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
13-225 |
8.45e-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: 69.78 E-value: 8.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 13 IRVSGMQFSYDVQdPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAGKhmvggknvvqvldrsafhdtelvcsgdlsy 92
Cdd:cd03221 1 IELENLSKTYGGK-LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGE------------------------------ 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 93 lggswsktagsagDIPLQGDFsaehmifgvegidpfrreKLIDLLDINLqwrMHKVSDGQRRRVQICMGLLHPFKVLLLD 172
Cdd:cd03221 50 -------------LEPDEGIV------------------TWGSTVKIGY---FEQLSGGEKMRLALAKLLLENPNLLLLD 95
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15240093 173 EVTVDLDVVARMDLLEFFKeecEQRGaTIVYATHIFDGLETWASHLAYINGGE 225
Cdd:cd03221 96 EPTNHLDLESIEALEEALK---EYPG-TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
6-206 |
1.06e-14 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 73.55 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 6 ASAVDGA-IRVSGMQFSYDVQDPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILA-------GKHMVGGKNvVQVLDRS 77
Cdd:TIGR02868 327 AVGLGKPtLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAglldplqGEVTLDGVP-VSSLDQD 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 78 AFHDTELVCSGDLSYLGGSWSKTAGSAgdiplQGDFSAEHMIFGVEGI---DPFRRekLIDLLDINLQWRMHKVSDGQRR 154
Cdd:TIGR02868 406 EVRRRVSVCAQDAHLFDTTVRENLRLA-----RPDATDEELWAALERVglaDWLRA--LPDGLDTVLGEGGARLSGGERQ 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15240093 155 RVQICMGLLHPFKVLLLDEVTVDLDVVARMDLLE-FFKEEceqRGATIVYATH 206
Cdd:TIGR02868 479 RLALARALLADAPILLLDEPTEHLDAETADELLEdLLAAL---SGRTVVLITH 528
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
9-206 |
7.02e-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: 71.40 E-value: 7.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 9 VDGAIRVSGMQFSYDVQD-PIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAGKH-------MVGGKNVVQvLDRSAFH 80
Cdd:COG2274 470 LKGDIELENVSFRYPGDSpPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYeptsgriLIDGIDLRQ-IDPASLR 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 81 DtelvcsgDLSYLggswsktagsagdipLQGD--FS---AEHMIFGVEGIDpfrREKLIDLLDI---------------- 139
Cdd:COG2274 549 R-------QIGVV---------------LQDVflFSgtiRENITLGDPDAT---DEEIIEAARLaglhdfiealpmgydt 603
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15240093 140 -------NLqwrmhkvSDGQRRRVQICMGLLHPFKVLLLDEVTVDLDVVARMDLLEFFKEECeqRGATIVYATH 206
Cdd:COG2274 604 vvgeggsNL-------SGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLL--KGRTVIIIAH 668
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
13-188 |
7.93e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 70.86 E-value: 7.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 13 IRVSGMQFSYDvQDPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAGK------HMVGGKNVV-----QvlDRSAFHD 81
Cdd:COG0488 316 LELEGLSKSYG-DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGElepdsgTVKLGETVKigyfdQ--HQEELDP 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 82 TELVcsgdLSYLggswskTAGSAGDIPLQ-----GDFsaehmifgveGIDPFRREKLIDLLdinlqwrmhkvSDGQRRRV 156
Cdd:COG0488 393 DKTV----LDEL------RDGAPGGTEQEvrgylGRF----------LFSGDDAFKPVGVL-----------SGGEKARL 441
|
170 180 190
....*....|....*....|....*....|..
gi 15240093 157 QICMGLLHPFKVLLLDEVTVDLDVVARmDLLE 188
Cdd:COG0488 442 ALAKLLLSPPNVLLLDEPTNHLDIETL-EALE 472
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
13-212 |
1.56e-13 |
|
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: 67.34 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 13 IRVSGMQFSYDVQD-PIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAGkhmvggknvvqvlDRSAFHDTELVCSGDLS 91
Cdd:cd03247 1 LSINNVSFSYPEQEqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTG-------------DLKPQQGEITLDGVPVS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 92 YLGGSWSKTagsagdiplqgdfsaehmiFGVEGIDPFrrekLID--LLDiNLQWRMhkvSDGQRRRVQICMGLLHPFKVL 169
Cdd:cd03247 68 DLEKALSSL-------------------ISVLNQRPY----LFDttLRN-NLGRRF---SGGERQRLALARILLQDAPIV 120
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15240093 170 LLDEVTVDLDVVARMDLLEFFKEECEQRgaTIVYATHIFDGLE 212
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDK--TLIWITHHLTGIE 161
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
27-235 |
1.73e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 69.00 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 27 PIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAGKHmVGGKNVVQVLDRSAFHDTElvcSGDLSylggSWSKTAGSAGD 106
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLH-VPTQGSVRVDDTLITSTSK---NKDIK----QIRKKVGLVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 107 IPLQGDFsAEHMI---------FGV--EGIDPFRREKLI------DLLDINlqwrMHKVSDGQRRRVQICMGLLHPFKVL 169
Cdd:PRK13649 93 FPESQLF-EETVLkdvafgpqnFGVsqEEAEALAREKLAlvgiseSLFEKN----PFELSGGQMRRVAIAGILAMEPKIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15240093 170 LLDEVTVDLDVVARMDLLEFFKeECEQRGATIVYATHIFDGLETWASHLAYINGGELKLSAKLDEI 235
Cdd:PRK13649 168 VLDEPTAGLDPKGRKELMTLFK-KLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
13-248 |
2.62e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 68.12 E-value: 2.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 13 IRVSGMQFSYDvQDPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILA-------GKHMVGGKNVVQVLDRS-----AF- 79
Cdd:PRK11231 3 LRTENLTVGYG-TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFArlltpqsGTVFLGDKPISMLSSRQlarrlALl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 80 ---HDT-------ELVCSGDLSYLggswsktagsagdiPLQGDFSAE-HMIfgVE------GIDPFRREKLIDLldinlq 142
Cdd:PRK11231 82 pqhHLTpegitvrELVAYGRSPWL--------------SLWGRLSAEdNAR--VNqameqtRINHLADRRLTDL------ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 143 wrmhkvSDGQRRRVQICMGLLHPFKVLLLDEVTVDLDV---VARMDLLeffkEECEQRGATIVYATHIFDGLETWASHLA 219
Cdd:PRK11231 140 ------SGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDInhqVELMRLM----RELNTQGKTVVTVLHDLNQASRYCDHLV 209
|
250 260
....*....|....*....|....*....
gi 15240093 220 YINGGELKLSAKLDEIkdlkTSPNLLSVV 248
Cdd:PRK11231 210 VLANGHVMAQGTPEEV----MTPGLLRTV 234
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
34-226 |
4.70e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 67.51 E-value: 4.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 34 LDLPAGSRCLLVGANGSGKTTLLKILaGKH-------MVGGKNVVQVLDRSAFhdtelvcSGDLSYLGGSWSKTAG---- 102
Cdd:PRK10575 32 LTFPAGKVTGLIGHNGSGKSTLLKML-GRHqppsegeILLDAQPLESWSSKAF-------ARKVAYLPQQLPAAEGmtvr 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 103 ---SAGDIPLQGDFSAehmiFGVEgiDPFRREKLIDLLDIN-LQWRM-HKVSDGQRRRVQICMGLLHPFKVLLLDEVTVD 177
Cdd:PRK10575 104 elvAIGRYPWHGALGR----FGAA--DREKVEEAISLVGLKpLAHRLvDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15240093 178 LDVVARMDLLEFFKEECEQRGATIVYATHIFDGLETWASHLAYINGGEL 226
Cdd:PRK10575 178 LDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEM 226
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
7-206 |
6.79e-13 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 67.04 E-value: 6.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 7 SAVDGAIRVSGMQFSYDVQD---PIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAGkhmvggknvvqvLDRSAfhdte 83
Cdd:COG1116 2 SAAAPALELRGVSKRFPTGGggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAG------------LEKPT----- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 84 lvcSGDLSYLGGSWSKTAGSAGDIPlQgDFS-------AEHMIFGVE--GIDP-FRREKLIDLLD-INLQWRMHK----V 148
Cdd:COG1116 65 ---SGEVLVDGKPVTGPGPDRGVVF-Q-EPAllpwltvLDNVALGLElrGVPKaERRERARELLElVGLAGFEDAyphqL 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15240093 149 SDGQRRRVQICMGL-LHPfKVLLLDEVTVDLDVVARMDLLEFFKEECEQRGATIVYATH 206
Cdd:COG1116 140 SGGMRQRVAIARALaNDP-EVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTH 197
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
13-226 |
1.36e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 66.30 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 13 IRVSGMQFSYDVQDPI----FFDFNLDLPAGSRCLLVGANGSGKTTLLKILAG--KHMVGGKNVVQVLDRSAFHDTELvc 86
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFasraLFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGllQPTEGKVTVGDIVVSSTSKQKEI-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 87 sgdlsylgGSWSKTAGSAGDIPLQGDFSA---EHMIFGVE--GIDPFRREKL----IDLLDINLQ-WRMH--KVSDGQRR 154
Cdd:PRK13643 80 --------KPVRKKVGVVFQFPESQLFEEtvlKDVAFGPQnfGIPKEKAEKIaaekLEMVGLADEfWEKSpfELSGGQMR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15240093 155 RVQICMGLLHPFKVLLLDEVTVDLDVVARMDLLEFFkEECEQRGATIVYATHIFDGLETWASHLAYINGGEL 226
Cdd:PRK13643 152 RVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLF-ESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHI 222
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
12-206 |
1.52e-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: 67.09 E-value: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 12 AIRVSGMQFSYDVQDPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAGKH-------MVGGKNVVQvLDRSAFHDtel 84
Cdd:COG4988 336 SIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLppysgsiLINGVDLSD-LDPASWRR--- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 85 vcsgDLSYLG-------GSWsktagsAGDIPL-QGDFSAEHMIFGVE--GIDPFRREkLIDLLDINLQWRMHKVSDGQRR 154
Cdd:COG4988 412 ----QIAWVPqnpylfaGTI------RENLRLgRPDASDEELEAALEaaGLDEFVAA-LPDGLDTPLGEGGRGLSGGQAQ 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15240093 155 RVQICMGLLHPFKVLLLDEVTVDLDVVARMDLLEFFKEECEQRgaTIVYATH 206
Cdd:COG4988 481 RLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITH 530
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
13-235 |
2.81e-12 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 65.01 E-value: 2.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 13 IRVSGMQFSYDVQDPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKIL-------AGKHMVGGKNVVQVldrsafhdtelv 85
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMInrlieptSGEIFIDGEDIREQ------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 86 csgDLSYLGGSWSKTAGSAGDIPlqgdfsaeHM--------IFGVEGIDPFRRE-------KLIDLLDINLQWRM-HKVS 149
Cdd:cd03295 69 ---DPVELRRKIGYVIQQIGLFP--------HMtveenialVPKLLKWPKEKIReradellALVGLDPAEFADRYpHELS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 150 DGQRRRVQICMGLLHPFKVLLLDEVTVDLDVVARMDLLEFFKEECEQRGATIVYATHIFDGLETWASHLAYINGGELKLS 229
Cdd:cd03295 138 GGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQV 217
|
....*.
gi 15240093 230 AKLDEI 235
Cdd:cd03295 218 GTPDEI 223
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
26-207 |
3.58e-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: 63.92 E-value: 3.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 26 DPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAG-KHMVGGknvvqvldrsafhdTELVCSGDLSYLGGSWSKTAGSA 104
Cdd:TIGR01189 13 RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGlLRPDSG--------------EVRWNGTPLAEQRDEPHENILYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 105 GDIP-LQGDFSAE------HMIFGVEGIDPFRREKLIDLLDINlQWRMHKVSDGQRRRVQICMGLLHPFKVLLLDEVTVD 177
Cdd:TIGR01189 79 GHLPgLKPELSALenlhfwAAIHGGAQRTIEDALAAVGLTGFE-DLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
170 180 190
....*....|....*....|....*....|
gi 15240093 178 LDVVARMDLLEFFKEECeQRGATIVYATHI 207
Cdd:TIGR01189 158 LDKAGVALLAGLLRAHL-ARGGIVLLTTHQ 186
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
31-237 |
3.92e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 65.13 E-value: 3.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 31 DFNLDLPAGSRCLLVGANGSGKTTLLKILAGkhmvggknvvqVLDrsafHDtelvcSGDLSYLGGswsktagsagdiPLQ 110
Cdd:COG4152 19 DVSFTVPKGEIFGLLGPNGAGKTTTIRIILG-----------ILA----PD-----SGEVLWDGE------------PLD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 111 GDFSA------------------EHMIF-----GVEGIDPFRR-EKLIDLLDINlQWRMHKV---SDGQRRRVQICMGLL 163
Cdd:COG4152 67 PEDRRrigylpeerglypkmkvgEQLVYlarlkGLSKAEAKRRaDEWLERLGLG-DRANKKVeelSKGNQQKVQLIAALL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15240093 164 HPFKVLLLDEVTVDLDVVARMDLLEFFKEECEQrGATIVYATHIFDGLETWASHLAYINGGELKLSAKLDEIKD 237
Cdd:COG4152 146 HDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRR 218
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
23-209 |
4.80e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.82 E-value: 4.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 23 DVQDPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAGKH---MVGGKNVVQVLDrsafhdtelvCSGDLSYLggswsk 99
Cdd:COG2401 40 VVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgtPVAGCVDVPDNQ----------FGREASLI------ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 100 tagsaGDIPLQGDFSAEHMIFGVEGI-DP--FRReklidlldinlqwRMHKVSDGQRRRVQICMGLLHPFKVLLLDEVTV 176
Cdd:COG2401 104 -----DAIGRKGDFKDAVELLNAVGLsDAvlWLR-------------RFKELSTGQKFRFRLALLLAERPKLLVIDEFCS 165
|
170 180 190
....*....|....*....|....*....|....*...
gi 15240093 177 DLD-----VVARMdllefFKEECEQRGATIVYATHIFD 209
Cdd:COG2401 166 HLDrqtakRVARN-----LQKLARRAGITLVVATHHYD 198
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
14-227 |
5.17e-12 |
|
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: 63.43 E-value: 5.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 14 RVSGMQFSYDVQDPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAGkhmvggknvvqvLDRSafhdtelvCSGDLSyL 93
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAG------------LIKE--------SSGSIL-L 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 94 GGSWSKTA---GSAG------DIPLQGDFSAEHMIFGVEGID--PFRREKLIDLLDIN--LQWRMHKVSDGQRRRVQICM 160
Cdd:cd03226 60 NGKPIKAKerrKSIGyvmqdvDYQLFTDSVREELLLGLKELDagNEQAETVLKDLDLYalKERHPLSLSGGQKQRLAIAA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15240093 161 GLLHPFKVLLLDEVTVDLDvVARMDLL-EFFKEECEQrGATIVYATHIFDGLETWASHLAYINGGELK 227
Cdd:cd03226 140 ALLSGKDLLIFDEPTSGLD-YKNMERVgELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
13-224 |
5.19e-12 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 63.67 E-value: 5.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 13 IRVSGMQFSYDVQDpifFDFNLDLPAGSRCLLVGANGSGKTTLLKILAG-------KHMVGGKNV--VQVLDR---SAFH 80
Cdd:cd03298 1 VRLDKIRFSYGEQP---MHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGfetpqsgRVLINGVDVtaAPPADRpvsMLFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 81 DTELvcsgdLSYLGGSWSKTAGSAGDIPLQG-DFSAEHMIFGVEGIDPFRREKLIDLldinlqwrmhkvSDGQRRRVQIC 159
Cdd:cd03298 78 ENNL-----FAHLTVEQNVGLGLSPGLKLTAeDRQAIEVALARVGLAGLEKRLPGEL------------SGGERQRVALA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15240093 160 MGLLHPFKVLLLDEVTVDLDVVARMDLLEFFKEECEQRGATIVYATHIFDGLETWASHLAYINGG 224
Cdd:cd03298 141 RVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNG 205
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
13-206 |
8.71e-12 |
|
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: 63.26 E-value: 8.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 13 IRVSGMQFSYDVQD---PIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAGkhmvggknvvqvLDRSAfhdtelvcSGD 89
Cdd:cd03293 1 LEVRNVSKTYGGGGgavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAG------------LERPT--------SGE 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 90 LSYLGGSWSKTAGSAGDIPlQGD-----FSAEHMI-FGVE--GIDPF-RREKLIDLLD-INLQWRMHK----VSDGQRRR 155
Cdd:cd03293 61 VLVDGEPVTGPGPDRGYVF-QQDallpwLTVLDNVaLGLElqGVPKAeARERAEELLElVGLSGFENAyphqLSGGMRQR 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15240093 156 VQICMGLLHPFKVLLLDEVTVDLDVVARMDLLEFFKEECEQRGATIVYATH 206
Cdd:cd03293 140 VALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTH 190
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
31-235 |
1.29e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 63.47 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 31 DFNLDLPAGSRCLLVGANGSGKTTLLKILAgkhmvggkNVVQVLDRSAFHDTELV---CSGDLSYLGGSWSKTAGSAGDI 107
Cdd:PRK10253 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLS--------RLMTPAHGHVWLDGEHIqhyASKEVARRIGLLAQNATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 108 PLQgdfsaEHMIFGVEGIDP-FRREKLIDLLDINLQWRMHKVSD-----------GQRRRVQICMGLLHPFKVLLLDEVT 175
Cdd:PRK10253 97 TVQ-----ELVARGRYPHQPlFTRWRKEDEEAVTKAMQATGITHladqsvdtlsgGQRQRAWIAMVLAQETAIMLLDEPT 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 176 VDLDVVARMDLLEFFKEECEQRGATIVYATHIFDGLETWASHLAYINGGELKLSAKLDEI 235
Cdd:PRK10253 172 TWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
12-235 |
1.96e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 62.70 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 12 AIRVSGMQFSYDVQD-PIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAGkhmvggknVVQVLDRSAFHDTELVCSGDL 90
Cdd:PRK13632 7 MIKVENVSFSYPNSEnNALKNVSFEINEGEYVAILGHNGSGKSTISKILTG--------LLKPQSGEIKIDGITISKENL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 91 SYLggswSKTAGsagdIPLQG---DF---SAEHMI-FGVEG--IDPFRREKLIDllDINLQWRM--------HKVSDGQR 153
Cdd:PRK13632 79 KEI----RKKIG----IIFQNpdnQFigaTVEDDIaFGLENkkVPPKKMKDIID--DLAKKVGMedyldkepQNLSGGQK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 154 RRVQICMGL-LHPfKVLLLDEVTVDLDVVARMDLLEFFKEECEQRGATIVYATHIFDGLeTWASHLAYINGGELKLSAKL 232
Cdd:PRK13632 149 QRVAIASVLaLNP-EIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKP 226
|
...
gi 15240093 233 DEI 235
Cdd:PRK13632 227 KEI 229
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
15-209 |
2.36e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 63.55 E-value: 2.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 15 VSGMQFSYDVQdPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAGK--------HMVGGKNVVQV-------LDRSAF 79
Cdd:COG0488 1 LENLSKSFGGR-PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGElepdsgevSIPKGLRIGYLpqeppldDDLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 80 hdtELVCSGD------------LSYLGGSWSKTAGSAGDipLQGDFSAEHmifGVEgIDPfRREKLIDLLDIN---LQWR 144
Cdd:COG0488 80 ---DTVLDGDaelraleaeleeLEAKLAEPDEDLERLAE--LQEEFEALG---GWE-AEA-RAEEILSGLGFPeedLDRP 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15240093 145 MHKVSDGQRRRVQICMGLLHPFKVLLLDEVTVDLDVVARMDLLEFFKEEceqRGATIV-----Y-----ATHIFD 209
Cdd:COG0488 150 VSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNY---PGTVLVvshdrYfldrvATRILE 221
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
13-244 |
2.76e-11 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 61.69 E-value: 2.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 13 IRVSGMQFSYDVQDpifFDFNLDLPAGSRCLLVGANGSGKTTLLKILAGkhmvggknvvqvldrsaFHDTElvcSGDLSY 92
Cdd:COG3840 2 LRLDDLTYRYGDFP---LRFDLTIAAGERVAILGPSGAGKSTLLNLIAG-----------------FLPPD---SGRILW 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 93 LGGSWSKTAgsagdiPLQGDFSaehMIF---------GVE-----GIDP------FRREKLIDLLD-INL----QWRMHK 147
Cdd:COG3840 59 NGQDLTALP------PAERPVS---MLFqennlfphlTVAqniglGLRPglkltaEQRAQVEQALErVGLagllDRLPGQ 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 148 VSDGQRRRVQICMGLLHPFKVLLLDEVTVDLDVVARMDLLEFFKEECEQRGATIVYATHIFDGLETWASHLAYINGGELK 227
Cdd:COG3840 130 LSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIA 209
|
250
....*....|....*..
gi 15240093 228 LSAKLDEIKDLKTSPNL 244
Cdd:COG3840 210 ADGPTAALLDGEPPPAL 226
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
11-181 |
3.22e-11 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 63.61 E-value: 3.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 11 GAIRVSGMQFSYDVQDPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKIL-------AGKHMVGGKNVVQvLDRSAFHdte 83
Cdd:TIGR01193 472 GDIVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLvgffqarSGEILLNGFSLKD-IDRHTLR--- 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 84 lvcsGDLSYLGGSWSKTAGSAGDIPLQG--DFSAEHMIFGVEGIDPFRR--EKLIDLLDINLQWRMHKVSDGQRRRVQIC 159
Cdd:TIGR01193 548 ----QFINYLPQEPYIFSGSILENLLLGakENVSQDEIWAACEIAEIKDdiENMPLGYQTELSEEGSSISGGQKQRIALA 623
|
170 180
....*....|....*....|..
gi 15240093 160 MGLLHPFKVLLLDEVTVDLDVV 181
Cdd:TIGR01193 624 RALLTDSKVLILDESTSNLDTI 645
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
26-212 |
5.08e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 60.66 E-value: 5.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 26 DPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAGKHMVGGKNVvqVLDRSAFHDTElvCSGDLSYLGGS--------- 96
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTI--KLDGGDIDDPD--VAEACHYLGHRnamkpaltv 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 97 ------WSKTAGsagdiplQGDFSAEHMIFGVEgidpfrrekLIDLLDInlqwRMHKVSDGQRRRVQICMGLLHPFKVLL 170
Cdd:PRK13539 91 aenlefWAAFLG-------GEELDIAAALEAVG---------LAPLAHL----PFGYLSAGQKRRVALARLLVSNRPIWI 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15240093 171 LDEVTVDLDVVARMDLLEFFKEECEQrGATIVYATHIFDGLE 212
Cdd:PRK13539 151 LDEPTAALDAAAVALFAELIRAHLAQ-GGIVIAATHIPLGLP 191
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
11-206 |
1.16e-10 |
|
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: 59.91 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 11 GAIRVSGMQFSYDVQD-PIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAGKH-------MVGGKNVVQvLDRSafhdt 82
Cdd:cd03245 1 GRIEFRNVSFSYPNQEiPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYkptsgsvLLDGTDIRQ-LDPA----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 83 elVCSGDLSYLGGSWSKTAGSAGD-IPLQGDFSAEHMIFGV---EGIDPFRReKLIDLLDINLQWRMHKVSDGQRRRVQI 158
Cdd:cd03245 75 --DLRRNIGYVPQDVTLFYGTLRDnITLGAPLADDERILRAaelAGVTDFVN-KHPNGLDLQIGERGRGLSGGQRQAVAL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15240093 159 CMGLLHPFKVLLLDEVTVDLDVVARMDLLEFFKEECEQRgaTIVYATH 206
Cdd:cd03245 152 ARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDK--TLIIITH 197
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
29-226 |
2.01e-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: 59.23 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 29 FFDFNLDLPA-GSRCLLVGANGSGKTTLLKILAGKHMVGGKNVVqvLDRSAFHDTELvcSGDLS----YLGGSWSKTAgs 103
Cdd:cd03297 12 DFTLKIDFDLnEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIV--LNGTVLFDSRK--KINLPpqqrKIGLVFQQYA-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 104 agdipLQGDFS-AEHMIFGVEGIDP----FRREKLIDLLDIN--LQWRMHKVSDGQRRRVQICMGLLHPFKVLLLDEVTV 176
Cdd:cd03297 86 -----LFPHLNvRENLAFGLKRKRNredrISVDELLDLLGLDhlLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15240093 177 DLDVVARMDLLEFFKEECEQRGATIVYATHIFDGLETWASHLAYINGGEL 226
Cdd:cd03297 161 ALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
13-249 |
4.11e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 59.23 E-value: 4.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 13 IRVSGMQFSYDVQDPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAG-KHMVGGKNVVQVLDrsafhdtelvcSGDLS 91
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGlLRPQKGKVLVSGID-----------TGDFS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 92 YLGGSwSKTAGSAGDIP---LQGDFSAEHMIFGVEG--IDPFRREKLID--LLDINLQWRMHK----VSDGQRRRVQICM 160
Cdd:PRK13644 71 KLQGI-RKLVGIVFQNPetqFVGRTVEEDLAFGPENlcLPPIEIRKRVDraLAEIGLEKYRHRspktLSGGQGQCVALAG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 161 GLLHPFKVLLLDEVTVDLDVVARMDLLEFFKeECEQRGATIVYATHIFDGLETwASHLAYINGGELKLSAKLDEI----- 235
Cdd:PRK13644 150 ILTMEPECLIFDEVTSMLDPDSGIAVLERIK-KLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVlsdvs 227
|
250
....*....|....*.
gi 15240093 236 -KDLK-TSPNLLSVVE 249
Cdd:PRK13644 228 lQTLGlTPPSLIELAE 243
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
11-226 |
4.44e-10 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 59.32 E-value: 4.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 11 GAIRVSGMQFSYDvQDPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILA-------GKHMVGGKNV--VQVLDRsafhd 81
Cdd:COG3839 2 ASLELENVSKSYG-GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAgledptsGEILIGGRDVtdLPPKDR----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 82 telvcsgDLSYLGGSW----SKTAgsagdiplqgdfsAEHMIFG--VEGIDPFRREKLI----------DLLDinlqwrm 145
Cdd:COG3839 76 -------NIAMVFQSYalypHMTV-------------YENIAFPlkLRKVPKAEIDRRVreaaellgleDLLD------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 146 HKVSD---GQRRRVQICMGLLHPFKVLLLDEVTVDLDVVARMDLLEFFKEECEQRGATIVYATHifDGLE--TWASHLAY 220
Cdd:COG3839 129 RKPKQlsgGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTH--DQVEamTLADRIAV 206
|
....*.
gi 15240093 221 INGGEL 226
Cdd:COG3839 207 MNDGRI 212
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
3-61 |
5.02e-10 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 59.79 E-value: 5.02e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 15240093 3 EKNASAVDGAIRVSGMQFSYDVQDPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAG 61
Cdd:COG1132 330 AVPLPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLR 388
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
13-206 |
1.02e-09 |
|
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: 57.63 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 13 IRVSGMQFSYDVQDPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKIL-------AGKHMVGGKNVVQV-LD--RSA---- 78
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLfrfydvsSGSILIDGQDIREVtLDslRRAigvv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 79 ------FHDTEL--VCSGDLsylggswsktagSAGDiplqgdfsaEHMIFGVE--GIDPfRREKLIDLLDINLQWRMHKV 148
Cdd:cd03253 81 pqdtvlFNDTIGynIRYGRP------------DATD---------EEVIEAAKaaQIHD-KIMRFPDGYDTIVGERGLKL 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15240093 149 SDGQRRRVQICMGLLHPFKVLLLDEVTVDLDVVARMDLLEFFKEECEQRgaTIVYATH 206
Cdd:cd03253 139 SGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGR--TTIVIAH 194
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
27-206 |
1.16e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 56.74 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 27 PIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILA-------GKHMVGGKNVVQVldRSAFHDtelvcsgDLSYLGgswsK 99
Cdd:PRK13538 15 ILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAglarpdaGEVLWQGEPIRRQ--RDEYHQ-------DLLYLG----H 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 100 TAGsagdipLQGDFSA-EHMIFGVEGIDPFRREKLIDLLD-INLQWRM----HKVSDGQRRRVQICMGLLHPFKVLLLDE 173
Cdd:PRK13538 82 QPG------IKTELTAlENLRFYQRLHGPGDDEALWEALAqVGLAGFEdvpvRQLSAGQQRRVALARLWLTRAPLWILDE 155
|
170 180 190
....*....|....*....|....*....|...
gi 15240093 174 VTVDLDVVARMDLLEFFKEECEqRGATIVYATH 206
Cdd:PRK13538 156 PFTAIDKQGVARLEALLAQHAE-QGGMVILTTH 187
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
13-206 |
1.99e-09 |
|
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: 56.81 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 13 IRVSGMQFSYDVQDPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAG---------------KHMVGGKNVVQVLDRS 77
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGlveptsgsvlidgtdINKLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 78 A--FHDTEL---------VCSGDLSYLGGSWSktagsagdipLQGDFSAEHMIFGVEGIDpfrrekLIDLLDINLQwRMH 146
Cdd:cd03256 81 GmiFQQFNLierlsvlenVLSGRLGRRSTWRS----------LFGLFPKEEKQRALAALE------RVGLLDKAYQ-RAD 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 147 KVSDGQRRRVQICMGLLHPFKVLLLDEVTVDLDVVARMDLLEFFKEECEQRGATIVYATH 206
Cdd:cd03256 144 QLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLH 203
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
31-226 |
2.07e-09 |
|
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: 56.11 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 31 DFNLDLPAGSRCLLVGANGSGKTTLLKILA-------GKHMVGGKNV--VQVLDRsafhdtelvcsgDLSYLGGSWS--- 98
Cdd:cd03301 18 DLNLDIADGEFVVLLGPSGCGKTTTLRMIAgleeptsGRIYIGGRDVtdLPPKDR------------DIAMVFQNYAlyp 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 99 -KTAgsagdiplqgdfsAEHMIFGV-------EGIDPfRREKLIDLLDIN--LQWRMHKVSDGQRRRVQICMGLLHPFKV 168
Cdd:cd03301 86 hMTV-------------YDNIAFGLklrkvpkDEIDE-RVREVAELLQIEhlLDRKPKQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15240093 169 LLLDEVTVDLDVVARMDLLEFFKEECEQRGATIVYATHIFDGLETWASHLAYINGGEL 226
Cdd:cd03301 152 FLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
33-209 |
2.74e-09 |
|
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: 55.13 E-value: 2.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 33 NLDLPAGSRCLLVGANGSGKTTLLKILAGkhmvggknvVQVLDrsafhdtelvcsgdlsylggswsktagsAGDIPLQGD 112
Cdd:cd03216 20 SLSVRRGEVHALLGENGAGKSTLMKILSG---------LYKPD----------------------------SGEILVDGK 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 113 fsaehmifGVEGIDPFRREKL-IdlldinlqwRM-HKVSDGQRRRVQICMGLLHPFKVLLLDEVTVDLDVVARMDLLEFF 190
Cdd:cd03216 63 --------EVSFASPRDARRAgI---------AMvYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVI 125
|
170
....*....|....*....
gi 15240093 191 KEECEQrGATIVYATHIFD 209
Cdd:cd03216 126 RRLRAQ-GVAVIFISHRLD 143
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
31-207 |
2.82e-09 |
|
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: 55.58 E-value: 2.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 31 DFNLDlpAGSRCLLVGANGSGKTTLLKILAGkhmvggknvvqvLDRSAFHDTeLVCSGDLSYLGGSWSKTAGSAGDIP-L 109
Cdd:cd03231 20 SFTLA--AGEALQVTGPNGSGKTTLLRILAG------------LSPPLAGRV-LLNGGPLDFQRDSIARGLLYLGHAPgI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 110 QGDFSAE------HMIFGVEGI-DPFRREKLIDLLDINLqwrmHKVSDGQRRRVQICMGLLHPFKVLLLDEVTVDLDVVA 182
Cdd:cd03231 85 KTTLSVLenlrfwHADHSDEQVeEALARVGLNGFEDRPV----AQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG 160
|
170 180
....*....|....*....|....*
gi 15240093 183 RMDLLEFFKEECeQRGATIVYATHI 207
Cdd:cd03231 161 VARFAEAMAGHC-ARGGMVVLTTHQ 184
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
13-235 |
4.29e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 56.18 E-value: 4.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 13 IRVSGMQFSYDVQDPI----FFDFNLDLPAGSRCLLVGANGSGKTTLLKILAGKHMvGGKNVVQVLDRSAFHDTElvcSG 88
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFerraLYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQ-PTSGTVTIGERVITAGKK---NK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 89 DLSYLggswSKTAGSAGDIP--------LQGDFSAEHMIFGVEGIDPFRREK-LIDLLDIN---LQWRMHKVSDGQRRRV 156
Cdd:PRK13634 79 KLKPL----RKKVGIVFQFPehqlfeetVEKDICFGPMNFGVSEEDAKQKAReMIELVGLPeelLARSPFELSGGQMRRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15240093 157 QICMGLLHPFKVLLLDEVTVDLDVVARMDLLEFFKEECEQRGATIVYATHIFDGLETWASHLAYINGGELKLSAKLDEI 235
Cdd:PRK13634 155 AIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
13-206 |
4.67e-09 |
|
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: 55.32 E-value: 4.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 13 IRVSGMQFSYDvQDPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILA-------GKHMVGGKNVVQVL--DR---SAFH 80
Cdd:cd03300 1 IELENVSKFYG-GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAgfetptsGEILLDGKDITNLPphKRpvnTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 81 DTELvcsgdlsylggswsktagsagdiplqgdFS----AEHMIFGVE--GIDP-FRREKLIDLLDI----NLQWRM-HKV 148
Cdd:cd03300 80 NYAL----------------------------FPhltvFENIAFGLRlkKLPKaEIKERVAEALDLvqleGYANRKpSQL 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15240093 149 SDGQRRRVQICMGL-LHPfKVLLLDEVTVDLDVVARMDLLEFFKEECEQRGATIVYATH 206
Cdd:cd03300 132 SGGQQQRVAIARALvNEP-KVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTH 189
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
30-235 |
5.20e-09 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 56.26 E-value: 5.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 30 FDFNLDLPAGSRCLLVGANGSGKTTLLKILAGkhmvggknvvqvLDRSAfhdtelvcSGDLSyLGGS-WSKTAgsagdip 108
Cdd:COG4148 16 LDVDFTLPGRGVTALFGPSGSGKTTLLRAIAG------------LERPD--------SGRIR-LGGEvLQDSA------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 109 lQGDFSAEH-----MIF---------GVEG------------IDPFRREKLIDLLDIN--LQWRMHKVSDGQRRRVQICM 160
Cdd:COG4148 68 -RGIFLPPHrrrigYVFqearlfphlSVRGnllygrkrapraERRISFDEVVELLGIGhlLDRRPATLSGGERQRVAIGR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15240093 161 GLL-HPfKVLLLDEVTVDLDVVARMDLLEFFKEECEQRGATIVYATHIFDGLETWASHLAYINGGELKLSAKLDEI 235
Cdd:COG4148 147 ALLsSP-RLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEV 221
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
31-206 |
1.42e-08 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 53.95 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 31 DFNLDLPAGSRCLLVGANGSGKTTLLKIL-------AGKHMVGGKNV-------VQVLDRS---AFHDTELvcsgdLSYL 93
Cdd:cd03292 19 GINISISAGEFVFLVGPSGAGKSTLLKLIykeelptSGTIRVNGQDVsdlrgraIPYLRRKigvVFQDFRL-----LPDR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 94 GgswsktagsagdiplqgdfSAEHMIFGVEGIDPFRRE---KLIDLLD-INLQWRMH----KVSDGQRRRVQICMGLLHP 165
Cdd:cd03292 94 N-------------------VYENVAFALEVTGVPPREirkRVPAALElVGLSHKHRalpaELSGGEQQRVAIARAIVNS 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15240093 166 FKVLLLDEVTVDLDVVARMDLLEFFKEeCEQRGATIVYATH 206
Cdd:cd03292 155 PTILIADEPTGNLDPDTTWEIMNLLKK-INKAGTTVVVATH 194
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
25-244 |
1.63e-08 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 53.94 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 25 QDPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILagkhmvggkNVVQVLDrsafhdtelvcSGDLSYLGGSWSKTAGSA 104
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCI---------NKLEEIT-----------SGDLIVDGLKVNDPKVDE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 105 GDIPLQGDF------------SAEHMIFG---VEGIDPFRREKL-IDLLD-INLQWRMH----KVSDGQRRRVQICMGLL 163
Cdd:PRK09493 73 RLIRQEAGMvfqqfylfphltALENVMFGplrVRGASKEEAEKQaRELLAkVGLAERAHhypsELSGGQQQRVAIARALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 164 HPFKVLLLDEVTVDLDVVARMDLLEFFKEECEQrGATIVYATHIFDGLETWASHLAYINGGELKLSAKLDEIKDLKTSPN 243
Cdd:PRK09493 153 VKPKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQR 231
|
.
gi 15240093 244 L 244
Cdd:PRK09493 232 L 232
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
31-225 |
1.86e-08 |
|
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: 53.44 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 31 DFNLDLPAGSRCLLVGANGSGKTTLLKIL-------AGKHMVGGKNVvQVLDRSAFhdtelvcsGDLSYLGGSWSKTAgs 103
Cdd:cd03269 18 DISFSVEKGEIFGLLGPNGAGKTTTIRMIlgiilpdSGEVLFDGKPL-DIAARNRI--------GYLPEERGLYPKMK-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 104 agdiplqgdfSAEHMIF-----GVEGIDPFRR-EKLIDLLDINLQW--RMHKVSDGQRRRVQICMGLLHPFKVLLLDEVT 175
Cdd:cd03269 87 ----------VIDQLVYlaqlkGLKKEEARRRiDEWLERLELSEYAnkRVEELSKGNQQKVQFIAAVIHDPELLILDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15240093 176 VDLDVVARmDLLEFFKEECEQRGATIVYATHIFDGLETWASHLAYINGGE 225
Cdd:cd03269 157 SGLDPVNV-ELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
12-237 |
2.25e-08 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 53.44 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 12 AIRVSGMQFSYDVQdPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKIL-------AGKHMVGGKNVVQvLDRSAFHDTEL 84
Cdd:COG1127 5 MIEVRNLTKSFGDR-VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIigllrpdSGEILVDGQDITG-LSEKELYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 85 vcsgDLSYLggswsktagsagdipLQGD--FSA------------EHMIFGVEGIDPFRREKL--IDLLDINlqwrmHK- 147
Cdd:COG1127 83 ----RIGML---------------FQGGalFDSltvfenvafplrEHTDLSEAEIRELVLEKLelVGLPGAA-----DKm 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 148 ---VSDGQRRRVqicmGL-----LHPfKVLLLDEVTVDLDVVARMDLLEFFKEECEQRGATIVYATHIFDGLETWASHLA 219
Cdd:COG1127 139 pseLSGGMRKRV----ALaralaLDP-EILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVA 213
|
250
....*....|....*...
gi 15240093 220 YINGGELKLSAKLDEIKD 237
Cdd:COG1127 214 VLADGKIIAEGTPEELLA 231
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
31-226 |
3.09e-08 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 52.92 E-value: 3.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 31 DFNLDLPAGSRCLLVGANGSGKTTLLKILAGkhmvggknvvqvldrsafhdTELVCSGDLSYLGGSWSKTAGSAGdipLQ 110
Cdd:cd03220 40 DVSFEVPRGERIGLIGRNGAGKSTLLRLLAG--------------------IYPPDSGTVTVRGRVSSLLGLGGG---FN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 111 GDFSAE------HMIFGVEgiDPFRREKLIDLLD-------INLQWRMHkvSDGQRRRVQICMGLLHPFKVLLLDEV--T 175
Cdd:cd03220 97 PELTGReniylnGRLLGLS--RKEIDEKIDEIIEfselgdfIDLPVKTY--SSGMKARLAFAIATALEPDILLIDEVlaV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15240093 176 VDldvvarmdllEFFKEECEQR-------GATIVYATHIFDGLETWASHLAYINGGEL 226
Cdd:cd03220 173 GD----------AAFQEKCQRRlrellkqGKTVILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
31-209 |
3.11e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 53.70 E-value: 3.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 31 DFNLDLPAGSRCLLVGANGSGKTTL-------LKILAGKHMVGGKNVvqvlDRSAFHDTELvcsgdlsylggswSKTAGS 103
Cdd:PRK13636 24 GININIKKGEVTAILGGNGAGKSTLfqnlngiLKPSSGRILFDGKPI----DYSRKGLMKL-------------RESVGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 104 AGDIPLQGDFSA---EHMIFGV--------------------EGIDPFRREKlidlldinlqwrMHKVSDGQRRRVQICM 160
Cdd:PRK13636 87 VFQDPDNQLFSAsvyQDVSFGAvnlklpedevrkrvdnalkrTGIEHLKDKP------------THCLSFGQKKRVAIAG 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15240093 161 GLLHPFKVLLLDEVTVDLDVVARMDLLEFFKEECEQRGATIVYATHIFD 209
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDID 203
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
31-206 |
3.23e-08 |
|
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: 53.11 E-value: 3.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 31 DFNLDLPAGSRCLLVGANGSGKTTLLKILAG-KHMVGGKNVVQVLDRSAFHDTElvcsgdlsylggswsKTAGsagdIPL 109
Cdd:cd03296 20 DVSLDIPSGELVALLGPSGSGKTTLLRLIAGlERPDSGTILFGGEDATDVPVQE---------------RNVG----FVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 110 QGDFSAEHMI------FGVEgIDPFR--------REKLIDLLD-INLQW---RM-HKVSDGQRRRVQICMGLLHPFKVLL 170
Cdd:cd03296 81 QHYALFRHMTvfdnvaFGLR-VKPRSerppeaeiRAKVHELLKlVQLDWladRYpAQLSGGQRQRVALARALAVEPKVLL 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 15240093 171 LDEVTVDLDVVARMDLLEFFKEECEQRGATIVYATH 206
Cdd:cd03296 160 LDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTH 195
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
13-180 |
3.30e-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: 54.17 E-value: 3.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 13 IRVSGMQFSYDvqDPIFF-DFNLDLPAGSRCLLVGANGSGKTTLLKILAGKhmvggknvvQVLDRSAFHDTELVcsgDLS 91
Cdd:TIGR03719 323 IEAENLTKAFG--DKLLIdDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQ---------EQPDSGTIEIGETV---KLA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 92 YLGGS----------WSKTAGSAgDIPLQGDFS----AEHMIFGVEGIDpfrREKLIDLLdinlqwrmhkvSDGQRRRVQ 157
Cdd:TIGR03719 389 YVDQSrdaldpnktvWEEISGGL-DIIKLGKREipsrAYVGRFNFKGSD---QQKKVGQL-----------SGGERNRVH 453
|
170 180
....*....|....*....|...
gi 15240093 158 ICMGLLHPFKVLLLDEVTVDLDV 180
Cdd:TIGR03719 454 LAKTLKSGGNVLLLDEPTNDLDV 476
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
9-224 |
3.47e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 53.20 E-value: 3.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 9 VDGAIRVSGMQFSYDVQDPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAGKHMVGgKNVVQVLDRSAFHDTE----- 83
Cdd:PRK13647 1 MDNIIEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQ-RGRVKVMGREVNAENEkwvrs 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 84 ---LVCSG--DLSYLGGSWSKTAgsagdiplqgdFSAEHMIFGVEGIDpfrrEKLIDLLDINLQWRM-----HKVSDGQR 153
Cdd:PRK13647 80 kvgLVFQDpdDQVFSSTVWDDVA-----------FGPVNMGLDKDEVE----RRVEEALKAVRMWDFrdkppYHLSYGQK 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15240093 154 RRVQICMGLLHPFKVLLLDEVTVDLDVVARMDLLEFFkEECEQRGATIVYATHIFDGLETWASHLAYINGG 224
Cdd:PRK13647 145 KRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEIL-DRLHNQGKTVIVATHDVDLAAEWADQVIVLKEG 214
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-226 |
3.57e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 53.48 E-value: 3.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 13 IRVSGMQFSY-DVQDPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKIL-------AGKHMVGG-----KNVVQVLDRSA- 78
Cdd:PRK13635 6 IRVEHISFRYpDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLnglllpeAGTITVGGmvlseETVWDVRRQVGm 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 79 -FH--DTELVcsgdlsylggswsktagsagdiplqGDFSAEHMIFGVE--GIDpfrREKLIDLLDINL-QWRM------- 145
Cdd:PRK13635 86 vFQnpDNQFV-------------------------GATVQDDVAFGLEniGVP---REEMVERVDQALrQVGMedflnre 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 146 -HKVSDGQRRRVQICMGL-LHPfKVLLLDEVTVDLDVVARMDLLEFFKEECEQRGATIVYATHIFDGLETwASHLAYING 223
Cdd:PRK13635 138 pHRLSGGQKQRVAIAGVLaLQP-DIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNK 215
|
...
gi 15240093 224 GEL 226
Cdd:PRK13635 216 GEI 218
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
31-238 |
3.75e-08 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 52.78 E-value: 3.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 31 DFNLDLPAGSRCLLVGANGSGKTTLLKILA-------GKHMVGGKnVVQVLDRSA-FHdtelvcsGDLS-----YLGGSw 97
Cdd:COG1134 44 DVSFEVERGESVGIIGRNGAGKSTLLKLIAgileptsGRVEVNGR-VSALLELGAgFH-------PELTgreniYLNGR- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 98 sktagsagdipLQG--------------DFSaehmifgveGIDPFrreklIDLldinlqwrmhKV---SDGQRRR----V 156
Cdd:COG1134 115 -----------LLGlsrkeidekfdeivEFA---------ELGDF-----IDQ----------PVktySSGMRARlafaV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 157 QICMgllhPFKVLLLDEVTvdldvvARMDllEFFKEECEQR-------GATIVYATHIFDGLETWASHLAYINGGELKLS 229
Cdd:COG1134 160 ATAV----DPDILLVDEVL------AVGD--AAFQKKCLARirelresGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMD 227
|
....*....
gi 15240093 230 AKLDEIKDL 238
Cdd:COG1134 228 GDPEEVIAA 236
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
11-180 |
5.32e-08 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 52.23 E-value: 5.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 11 GAIRVSGMQFSYDVQDPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKIL-------AGKHMVGGKNVVQVlDRSAFHDTE 83
Cdd:cd03254 1 GEIEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLmrfydpqKGQILIDGIDIRDI-SRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 84 LVCSGDLSYLGGSWSKtagsagDIPLQGDFSAEHMIFGVE---GIDPFRReKLIDLLDINLQWRMHKVSDGQRRRVQICM 160
Cdd:cd03254 80 GVVLQDTFLFSGTIME------NIRLGRPNATDEEVIEAAkeaGAHDFIM-KLPNGYDTVLGENGGNLSQGERQLLAIAR 152
|
170 180
....*....|....*....|
gi 15240093 161 GLLHPFKVLLLDEVTVDLDV 180
Cdd:cd03254 153 AMLRDPKILILDEATSNIDT 172
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
13-184 |
5.33e-08 |
|
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: 52.23 E-value: 5.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 13 IRVSGMQFSYD-VQDPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAGKHMVGGKNVvqVLDRSAFHDTELvcsGDLS 91
Cdd:cd03251 1 VEFKNVTFRYPgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRI--LIDGHDVRDYTL---ASLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 92 ylggswSKTAGSAGDIPLQGDFSAEHMIFGVEGIDPFRRE-------------KLIDLLDINLQWRMHKVSDGQRRRVQI 158
Cdd:cd03251 76 ------RQIGLVSQDVFLFNDTVAENIAYGRPGATREEVEeaaraanahefimELPEGYDTVIGERGVKLSGGQRQRIAI 149
|
170 180
....*....|....*....|....*.
gi 15240093 159 CMGLLHPFKVLLLDEVTVDLDVVARM 184
Cdd:cd03251 150 ARALLKDPPILILDEATSALDTESER 175
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
129-206 |
5.45e-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: 53.13 E-value: 5.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 129 RREKLIDLLD---INLQWRM-----HKVSDGQRRRVQICMGL-LHPfKVLLLDEVTVDLDVVARMDLLEFFKEECEQRGA 199
Cdd:COG0444 124 ARERAIELLErvgLPDPERRldrypHELSGGMRQRVMIARALaLEP-KLLIADEPTTALDVTIQAQILNLLKDLQRELGL 202
|
....*..
gi 15240093 200 TIVYATH 206
Cdd:COG0444 203 AILFITH 209
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
31-226 |
5.51e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 52.83 E-value: 5.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 31 DFNLDLPAGSRCLLVGANGSGKTTLLKIlagkhMVGgknVVQVLDRSAFHDTELVCSGDLSYLggswSKTAGsagdIPLQ 110
Cdd:PRK13648 27 DVSFNIPKGQWTSIVGHNGSGKSTIAKL-----MIG---IEKVKSGEIFYNNQAITDDNFEKL----RKHIG----IVFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 111 -------GDFSAEHMIFGVEG----IDPFRREKLIDLLDINLQWRM----HKVSDGQRRRVQICMGL-LHPfKVLLLDEV 174
Cdd:PRK13648 91 npdnqfvGSIVKYDVAFGLENhavpYDEMHRRVSEALKQVDMLERAdyepNALSGGQKQRVAIAGVLaLNP-SVIILDEA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15240093 175 TVDLDVVARMDLLEFFKEECEQRGATIVYATHifDGLETW-ASHLAYINGGEL 226
Cdd:PRK13648 170 TSMLDPDARQNLLDLVRKVKSEHNITIISITH--DLSEAMeADHVIVMNKGTV 220
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
31-206 |
7.07e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 52.78 E-value: 7.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 31 DFNLDLPAGSRCLLVGANGSGKTTLLKILAG-KHMVGGknvvqvldRSAFHDTelvcsgDLSYLggswsktagSAGDIPL 109
Cdd:PRK10851 20 DISLDIPSGQMVALLGPSGSGKTTLLRIIAGlEHQTSG--------HIRFHGT------DVSRL---------HARDRKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 110 QGDFSA----EHMI------FGVEgIDPfRRE---------KLIDLLDI----NLQWRM-HKVSDGQRRRVQICMGLLHP 165
Cdd:PRK10851 77 GFVFQHyalfRHMTvfdniaFGLT-VLP-RRErpnaaaikaKVTQLLEMvqlaHLADRYpAQLSGGQKQRVALARALAVE 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15240093 166 FKVLLLDEVTVDLDVVARMDLLEFFKEECEQRGATIVYATH 206
Cdd:PRK10851 155 PQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTH 195
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
13-237 |
7.51e-08 |
|
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: 52.12 E-value: 7.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 13 IRVSGMQFSYDVQdPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAGkhmvggknvvqvLDRSAfhdtelvcSGDLSY 92
Cdd:cd03261 1 IELRGLTKSFGGR-TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVG------------LLRPD--------SGEVLI 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 93 LGGSWSKtAGSAGDIPL--------QGD--FSA------------EHMIFGVEGIDPFRREKL--------IDLLDINLq 142
Cdd:cd03261 60 DGEDISG-LSEAELYRLrrrmgmlfQSGalFDSltvfenvafplrEHTRLSEEEIREIVLEKLeavglrgaEDLYPAEL- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 143 wrmhkvSDGQRRRVQICMGL-LHPfKVLLLDEVTVDLDVVARMDLLEFFKEECEQRGATIVYATHIFDGLETWASHLAYI 221
Cdd:cd03261 138 ------SGGMKKRVALARALaLDP-ELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVL 210
|
250
....*....|....*.
gi 15240093 222 NGGELKLSAKLDEIKD 237
Cdd:cd03261 211 YDGKIVAEGTPEELRA 226
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
13-206 |
8.47e-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: 51.80 E-value: 8.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 13 IRVSGMQFSYDvQDPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKIL------------AGKHMVGGKNVVqvldrsafh 80
Cdd:cd03260 1 IELRDLNVYYG-DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndlipgapdEGEVLLDGKDIY--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 81 dtelvcsgDLSYLGGSWSKTAGSAGDIPLQGDFS-AEHMIFGVegidPFRREKLIDLLDINLQWRMHKV----------- 148
Cdd:cd03260 71 --------DLDVDVLELRRRVGMVFQKPNPFPGSiYDNVAYGL----RLHGIKLKEELDERVEEALRKAalwdevkdrlh 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15240093 149 ----SDGQRRRVQICMGLLHPFKVLLLDEVTVDLDVVARMDLLEFFKEECEQRgaTIVYATH 206
Cdd:cd03260 139 alglSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTH 198
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
13-206 |
1.07e-07 |
|
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: 50.68 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 13 IRVSGMQFSY-DVQDPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAGKHMVGGKNVvqVLDRSAFHDTelvcsgDLS 91
Cdd:cd03246 1 LEVENVSFRYpGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRV--RLDGADISQW------DPN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 92 YLGgswsKTAGS-AGDIPLQGDFSAEHmIFgvegidpfrreklidlldinlqwrmhkvSDGQRRRVQICMGLLHPFKVLL 170
Cdd:cd03246 73 ELG----DHVGYlPQDDELFSGSIAEN-IL----------------------------SGGQRQRLGLARALYGNPRILV 119
|
170 180 190
....*....|....*....|....*....|....*....
gi 15240093 171 LDEVTVDLDV---VARMDLLEFFKEeceqRGATIVYATH 206
Cdd:cd03246 120 LDEPNSHLDVegeRALNQAIAALKA----AGATRIVIAH 154
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
9-235 |
1.19e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 51.72 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 9 VDGAIRVSGMQFSY-DVQDPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAGKHM---------------VGGKNVVQ 72
Cdd:PRK13640 2 KDNIVEFKHVSFTYpDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLpddnpnskitvdgitLTAKTVWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 73 VLDRSA--FHDTelvcsgDLSYLGGSwsktagsagdiplQGDFSAehmiFGVEGIDPFRREKLIDLLDINLQWRM----- 145
Cdd:PRK13640 82 IREKVGivFQNP------DNQFVGAT-------------VGDDVA----FGLENRAVPRPEMIKIVRDVLADVGMldyid 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 146 ---HKVSDGQRRRVQICMGLLHPFKVLLLDEVTVDLDVVARMDLLEFFKEECEQRGATIVYATHIFDGLETwASHLAYIN 222
Cdd:PRK13640 139 sepANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLD 217
|
250
....*....|...
gi 15240093 223 GGELKLSAKLDEI 235
Cdd:PRK13640 218 DGKLLAQGSPVEI 230
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
146-248 |
1.26e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 51.73 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 146 HKVSDGQRRRVQICMGLLHPFKVLLLDEVTVDLDVVARMDLLEFFKEECEQRGATIVYATHIFDGLETWASHLAYINGGE 225
Cdd:PRK13652 136 HHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGR 215
|
90 100
....*....|....*....|...
gi 15240093 226 LKLSAKLDEIkdlKTSPNLLSVV 248
Cdd:PRK13652 216 IVAYGTVEEI---FLQPDLLARV 235
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
18-202 |
1.55e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 50.72 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 18 MQFSYDVQD-PIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAGKH-------MVGGKNVVQvlDRSAFHDtELVCSGD 89
Cdd:PRK13540 5 IELDFDYHDqPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLnpekgeiLFERQSIKK--DLCTYQK-QLCFVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 90 LSYLGGSWSKTAGSAGDIplqgdfsaeHMIFGVEGIDP----FRREKLIDlldinlqWRMHKVSDGQRRRVQICMGLLHP 165
Cdd:PRK13540 82 RSGINPYLTLRENCLYDI---------HFSPGAVGITElcrlFSLEHLID-------YPCGLLSSGQKRQVALLRLWMSK 145
|
170 180 190
....*....|....*....|....*....|....*..
gi 15240093 166 FKVLLLDEVTVDLDVVARMDLLEFFKEECEQRGATIV 202
Cdd:PRK13540 146 AKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLL 182
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
31-206 |
1.77e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 52.03 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 31 DFNLDLPAGSRCLLVGANGSGKTTLLKIL-------AGKHMVGGKNVVQvLDRSA------------FHDTELvcsgdLS 91
Cdd:PRK10535 26 GISLDIYAGEMVAIVGASGSGKSTLMNILgcldkptSGTYRVAGQDVAT-LDADAlaqlrrehfgfiFQRYHL-----LS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 92 YLggswskTAGSAGDIPLqgdfsaehMIFGVEGIDpfRREKLIDLLD-INLQWRMH----KVSDGQRRRVQICMGLLHPF 166
Cdd:PRK10535 100 HL------TAAQNVEVPA--------VYAGLERKQ--RLLRAQELLQrLGLEDRVEyqpsQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15240093 167 KVLLLDEVTVDLDVVARMDLLEFFKEECEQrGATIVYATH 206
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTH 202
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
31-226 |
1.88e-07 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 51.57 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 31 DFNLDLPAGSRCLLVGANGSGKTTLLKILAGkhmvggknvvqvldrsafhdTELVCSGDLsYLGGSwsktagSAGDIP-- 108
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAG--------------------LEDITSGDL-FIGEK------RMNDVPpa 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 109 ------------LQGDFS-AEHMIFGVE--GIDPFRREKLID------LLDINLQWRMHKVSDGQRRRVQICMGLLHPFK 167
Cdd:PRK11000 74 ergvgmvfqsyaLYPHLSvAENMSFGLKlaGAKKEEINQRVNqvaevlQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15240093 168 VLLLDEVTVDLDVVARMDL-LEFFKEEcEQRGATIVYATHifDGLE--TWASHLAYINGGEL 226
Cdd:PRK11000 154 VFLLDEPLSNLDAALRVQMrIEISRLH-KRLGRTMIYVTH--DQVEamTLADKIVVLDAGRV 212
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
12-61 |
2.10e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 51.82 E-value: 2.10e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 15240093 12 AIRVSGMQFSYDvQDPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAG 61
Cdd:PRK15064 319 ALEVENLTKGFD-NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVG 367
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
129-249 |
2.63e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 50.86 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 129 RREKLIDL--LDIN-LQWRMHKVSDGQRRRVQICMGLLHPFKVLLLDEVTVDLDVVARMDLLEFFKEECEQrGATIVYAT 205
Cdd:PRK13651 144 RAAKYIELvgLDESyLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVT 222
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 15240093 206 HIFDGLETWASHLAYINGGELKLSAKLDEI-KDLK-------TSPNLLSVVE 249
Cdd:PRK13651 223 HDLDNVLEWTKRTIFFKDGKIIKDGDTYDIlSDNKfliennmEPPKLLNFVN 274
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
31-179 |
2.89e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 50.47 E-value: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 31 DFNLDLPAGSRCLLVGANGSGKTTLLKILAGKHMV-------GGKNVVQVLD--RSA-----FHDtelvcsgdlsylggs 96
Cdd:COG1101 24 GLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPdsgsiliDGKDVTKLPEykRAKyigrvFQD--------------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 97 wsktagsagdiPLQGdfSAEHMifGVE-----------------GIDPFRREKLIDL---LDINLQWRMH-KV---SDGQ 152
Cdd:COG1101 89 -----------PMMG--TAPSM--TIEenlalayrrgkrrglrrGLTKKRRELFRELlatLGLGLENRLDtKVgllSGGQ 153
|
170 180
....*....|....*....|....*..
gi 15240093 153 RRRVQICMGLLHPFKVLLLDEVTVDLD 179
Cdd:COG1101 154 RQALSLLMATLTKPKLLLLDEHTAALD 180
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
12-206 |
2.99e-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: 50.87 E-value: 2.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 12 AIRVSGMQFSYDvQDPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAGkhmvggknvvqvldrsaFhdtELVCSGDLs 91
Cdd:COG3842 5 ALELENVSKRYG-DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAG-----------------F---ETPDSGRI- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 92 YLGGSwsktagsagDIplqGDFSAE---------------HM-----I-FG--VEGIDP-FRREKLIDLLDI----NLQW 143
Cdd:COG3842 63 LLDGR---------DV---TGLPPEkrnvgmvfqdyalfpHLtvaenVaFGlrMRGVPKaEIRARVAELLELvgleGLAD 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15240093 144 RM-HKVSDGQRRRVQICMGL-LHPfKVLLLDEVTVDLDVVARMDLLEFFKEECEQRGATIVYATH 206
Cdd:COG3842 131 RYpHQLSGGQQQRVALARALaPEP-RVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTH 194
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
31-209 |
3.06e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 50.47 E-value: 3.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 31 DFNLDLPAGSRCLLVGANGSGKTTLlkilaGKHM------VGGKNVVQVLDRSafhDTELVcsgdlsylggsWS--KTAG 102
Cdd:PRK13633 28 DVNLEVKKGEFLVILGRNGSGKSTI-----AKHMnallipSEGKVYVDGLDTS---DEENL-----------WDirNKAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 103 SAGDIP---LQGDFSAEHMIFGVE--GIDPFRREKLID--LLDINL-QWRMHK---VSDGQRRRVQICmGLL--HPfKVL 169
Cdd:PRK13633 89 MVFQNPdnqIVATIVEEDVAFGPEnlGIPPEEIRERVDesLKKVGMyEYRRHAphlLSGGQKQRVAIA-GILamRP-ECI 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15240093 170 LLDEVTVDLDVVARMDLLEFFKEECEQRGATIVYATHIFD 209
Cdd:PRK13633 167 IFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYME 206
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-212 |
4.32e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 50.59 E-value: 4.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 2 AEKNASAVDGAIRVSGMQFSY-DVQDPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILA-------GKHMVGGKNvVQV 73
Cdd:PRK11160 328 TTSTAAADQVSLTLNNVSFTYpDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTrawdpqqGEILLNGQP-IAD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 74 LDRSAFHDTELVCSGDLSYLGGSWSKT----AGSAGDiplqgdfsaEHMifgvegIDPFRREKLIDLLD----INLqW-- 143
Cdd:PRK11160 407 YSEAALRQAISVVSQRVHLFSATLRDNlllaAPNASD---------EAL------IEVLQQVGLEKLLEddkgLNA-Wlg 470
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15240093 144 ---RmhKVSDGQRRRVQICMGLLHPFKVLLLDEVTVDLDVVARMDLLEFFKEECEQRgaTIVYATHIFDGLE 212
Cdd:PRK11160 471 eggR--QLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNK--TVLMITHRLTGLE 538
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
27-206 |
4.37e-07 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 50.58 E-value: 4.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 27 PIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAG--KHmvgGKNVVQV--LDRSAFhdtelvcsgdLS---YLGGswsk 99
Cdd:COG4178 377 PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGlwPY---GSGRIARpaGARVLF----------LPqrpYLPL---- 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 100 taGSAGDI---PLQ-GDFSAEHMIfgvEGIDPFRREKLIDLLDINLQWRmHKVSDGQRRRVQICMGLLHPFKVLLLDEVT 175
Cdd:COG4178 440 --GTLREAllyPATaEAFSDAELR---EALEAVGLGHLAERLDEEADWD-QVLSLGEQQRLAFARLLLHKPDWLFLDEAT 513
|
170 180 190
....*....|....*....|....*....|.
gi 15240093 176 VDLDVVARMDLLEFFKEECEqrGATIVYATH 206
Cdd:COG4178 514 SALDEENEAALYQLLREELP--GTTVISVGH 542
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
31-202 |
5.94e-07 |
|
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: 49.36 E-value: 5.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 31 DFNLDLPAGSRCLLVGANGSGKTTLLKILAGKH-------MVGGKNVVQV---------LDRSaFHDTELVcsGDLS--- 91
Cdd:cd03219 18 DVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLrptsgsvLFDGEDITGLppheiarlgIGRT-FQIPRLF--PELTvle 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 92 --YLGGswskTAGSAGDIPLQGDFSAEHMIfgvegidpfrREKLIDLLD-INLQWRMHKV----SDGQRRRVQICMGL-L 163
Cdd:cd03219 95 nvMVAA----QARTGSGLLLARARREEREA----------RERAEELLErVGLADLADRPagelSYGQQRRLEIARALaT 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 15240093 164 HPfKVLLLDEVTVDLDVVARMDLLEFFKeECEQRGATIV 202
Cdd:cd03219 161 DP-KLLLLDEPAAGLNPEETEELAELIR-ELRERGITVL 197
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
13-209 |
6.03e-07 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 49.63 E-value: 6.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 13 IRVSGMQFSYDvQDPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAGKhMVGGKNV---VQVLDRSafhdteLVCSGD 89
Cdd:PRK09984 5 IRVEKLAKTFN-QHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL-ITGDKSAgshIELLGRT------VQREGR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 90 LSylgGSWSKTAGSAGDIPLQGDF-----SAEHMIFGVEGIDPFRR------------EKLIDLLDINL----QWRMHKV 148
Cdd:PRK09984 77 LA---RDIRKSRANTGYIFQQFNLvnrlsVLENVLIGALGSTPFWRtcfswftreqkqRALQALTRVGMvhfaHQRVSTL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15240093 149 SDGQRRRVQICMGLLHPFKVLLLDEVTVDLDVVARMDLLEFFKEECEQRGATIVYATHIFD 209
Cdd:PRK09984 154 SGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVD 214
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
31-206 |
6.81e-07 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 49.29 E-value: 6.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 31 DFNLDLPAGSRCLLVGANGSGKTTLLKILAG-------KHMVGGKNVVQVLD--RSAFHDTELVcsgdlsylggSWSKTA 101
Cdd:PRK11247 30 QLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGletpsagELLAGTAPLAEAREdtRLMFQDARLL----------PWKKVI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 102 GSAGdIPLQGDFsaehmifgvegidpfRREKLIDLLDINLQWRMHK----VSDGQRRRVQICMGLLHPFKVLLLDEVTVD 177
Cdd:PRK11247 100 DNVG-LGLKGQW---------------RDAALQALAAVGLADRANEwpaaLSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180
....*....|....*....|....*....
gi 15240093 178 LDVVARMDLLEFFKEECEQRGATIVYATH 206
Cdd:PRK11247 164 LDALTRIEMQDLIESLWQQHGFTVLLVTH 192
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
16-179 |
1.06e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 48.31 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 16 SGMQFSYDvQDPIF--FDFNLDlpAGSRCLLVGANGSGKTTLLKILAG-KHMVGGKnvVQVldrsafhDTELVCSGD--- 89
Cdd:PRK13543 15 HALAFSRN-EEPVFgpLDFHVD--AGEALLVQGDNGAGKTTLLRVLAGlLHVESGQ--IQI-------DGKTATRGDrsr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 90 ----LSYLGGswsktagsagdipLQGDFSAE---HMIFGVEGIDPFRRE----KLIDLLDINlQWRMHKVSDGQRRRVQI 158
Cdd:PRK13543 83 fmayLGHLPG-------------LKADLSTLenlHFLCGLHGRRAKQMPgsalAIVGLAGYE-DTLVRQLSAGQKKRLAL 148
|
170 180
....*....|....*....|.
gi 15240093 159 CMGLLHPFKVLLLDEVTVDLD 179
Cdd:PRK13543 149 ARLWLSPAPLWLLDEPYANLD 169
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
13-206 |
1.49e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.18 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 13 IRVSGMQFSY-DVqdPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAGKhmvggknvvQVLDrsafhDTELVCSGDLs 91
Cdd:PRK11147 4 ISIHGAWLSFsDA--PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGE---------VLLD-----DGRIIYEQDL- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 92 ylggswsKTAGSAGDIP--LQG---DFSAE------------HMIFGVEGIDPFRR-----EKLIDLLDINLQW----RM 145
Cdd:PRK11147 67 -------IVARLQQDPPrnVEGtvyDFVAEgieeqaeylkryHDISHLVETDPSEKnlnelAKLQEQLDHHNLWqlenRI 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15240093 146 HKV---------------SDGQRRRVQICMGLLHPFKVLLLDEVTVDLDVVArMDLLE-FFKeecEQRGAtIVYATH 206
Cdd:PRK11147 140 NEVlaqlgldpdaalsslSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET-IEWLEgFLK---TFQGS-IIFISH 211
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
13-206 |
2.44e-06 |
|
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: 46.76 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 13 IRVSGMQFSYDVQDPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAGkhmvggknvvqvldrsafhdtelvcsgdL-S 91
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG----------------------------LwP 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 92 YLGGSWSKTAGsagdiplqgdfsaEHMIFgvegiDPFR--------REKLIDLLDINLqwrmhkvSDGQRRRVQICMGLL 163
Cdd:cd03223 53 WGSGRIGMPEG-------------EDLLF-----LPQRpylplgtlREQLIYPWDDVL-------SGGEQQRLAFARLLL 107
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15240093 164 HPFKVLLLDEVTVDLDVvarmDLLEFFKEECEQRGATIVYATH 206
Cdd:cd03223 108 HKPKFVFLDEATSALDE----ESEDRLYQLLKELGITVISVGH 146
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
148-235 |
2.52e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 47.74 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 148 VSDGQRRRVQICMGLLHPFKVLLLDEVTVDLDVVARMDLLEFFKEECEQRGATIVYATHIFDGLETWASHLAYINGGELK 227
Cdd:PRK13637 145 LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCE 224
|
....*...
gi 15240093 228 LSAKLDEI 235
Cdd:PRK13637 225 LQGTPREV 232
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
32-206 |
2.91e-06 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 47.27 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 32 FNLDLPAGSRCLLVGANGSGKTTLLKILAGkhmvggknvvqvldrsaFHDTElvcSGDLSYLGGSWSKTAgsagdiPLQG 111
Cdd:PRK10771 18 FDLTVERGERVAILGPSGAGKSTLLNLIAG-----------------FLTPA---SGSLTLNGQDHTTTP------PSRR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 112 DFS---AEHMIFG---VE-----GIDP------FRREKLIDL-----LDINLQWRMHKVSDGQRRRVQICMGLLHPFKVL 169
Cdd:PRK10771 72 PVSmlfQENNLFShltVAqniglGLNPglklnaAQREKLHAIarqmgIEDLLARLPGQLSGGQRQRVALARCLVREQPIL 151
|
170 180 190
....*....|....*....|....*....|....*..
gi 15240093 170 LLDEVTVDLDVVARMDLLEFFKEECEQRGATIVYATH 206
Cdd:PRK10771 152 LLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSH 188
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
12-206 |
3.02e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.43 E-value: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 12 AIRVSGMQFSYD--VQDPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAGkhmvggknvvqvlDRSAFHDTELVCSGD 89
Cdd:PLN03232 614 AISIKNGYFSWDskTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG-------------ELSHAETSSVVIRGS 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 90 LSYLGG-SWSKTAGSAGDIPLQGDFSAEHmiFGvEGIDPFRREKLIDLLD----INLQWRMHKVSDGQRRRVQICMGLLH 164
Cdd:PLN03232 681 VAYVPQvSWIFNATVRENILFGSDFESER--YW-RAIDVTALQHDLDLLPgrdlTEIGERGVNISGGQKQRVSMARAVYS 757
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15240093 165 PFKVLLLDEVTVDLDV-VARMDLLEFFKEECeqRGATIVYATH 206
Cdd:PLN03232 758 NSDIYIFDDPLSALDAhVAHQVFDSCMKDEL--KGKTRVLVTN 798
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
44-206 |
3.48e-06 |
|
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: 46.39 E-value: 3.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 44 LVGANGSGKTTLLKILAGKHMVGGKnvvqvldrsafhdtelvcSGDLsYLGGswsktagsagdIPLQGDFSAEHMIFgVE 123
Cdd:cd03213 40 IMGPSGAGKSTLLNALAGRRTGLGV------------------SGEV-LING-----------RPLDKRSFRKIIGY-VP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 124 gidpfRREKLIDLLDI--NLQW--RMHKVSDGQRRRVQICMGLLHPFKVLLLDEVTVDLDVVARMDLLEFFKEECeQRGA 199
Cdd:cd03213 89 -----QDDILHPTLTVreTLMFaaKLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLA-DTGR 162
|
....*..
gi 15240093 200 TIVYATH 206
Cdd:cd03213 163 TIICSIH 169
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
27-209 |
4.10e-06 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 46.49 E-value: 4.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 27 PIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAGKhmvggknvvqvldrsafHDTELVCSGDLSYLGGSWSKTAGSAgd 106
Cdd:cd03233 21 PILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR-----------------TEGNVSVEGDIHYNGIPYKEFAEKY-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 107 iplQGD--FSAEHMIF----GVEgidpfrrekliDLLDINLQWRMH----KVSDGQRRRVQICMGLLHPFKVLLLDEVTV 176
Cdd:cd03233 82 ---PGEiiYVSEEDVHfptlTVR-----------ETLDFALRCKGNefvrGISGGERKRVSIAEALVSRASVLCWDNSTR 147
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15240093 177 DLDVVARMDLLEFFKEECEQRGATIVYA--------THIFD 209
Cdd:cd03233 148 GLDSSTALEILKCIRTMADVLKTTTFVSlyqasdeiYDLFD 188
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
33-206 |
4.77e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 46.41 E-value: 4.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 33 NLDLPAGSRCLLVGANGSGKTTLLKIL-------AGKHMVGGKNVVQVLDRSA----------FHDTELVCsgdlsylgg 95
Cdd:PRK10908 22 TFHMRPGEMAFLTGHSGAGKSTLLKLIcgierpsAGKIWFSGHDITRLKNREVpflrrqigmiFQDHHLLM--------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 96 swSKTAGSAGDIPLqgdfsaehMIFGVEGIDPFRREKL----IDLLDINLQWRMhKVSDGQRRRVQICMGLLHPFKVLLL 171
Cdd:PRK10908 93 --DRTVYDNVAIPL--------IIAGASGDDIRRRVSAaldkVGLLDKAKNFPI-QLSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190
....*....|....*....|....*....|....*
gi 15240093 172 DEVTVDLDVVARMDLLEFFkEECEQRGATIVYATH 206
Cdd:PRK10908 162 DEPTGNLDDALSEGILRLF-EEFNRVGVTVLMATH 195
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
13-61 |
6.17e-06 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 46.68 E-value: 6.17e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 15240093 13 IRVSGMQFSYDvQDPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAG 61
Cdd:COG1118 3 IEVRNISKRFG-SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAG 50
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
10-59 |
6.47e-06 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 47.12 E-value: 6.47e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 15240093 10 DGAIRVSGMQFSYDVQDPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKIL 59
Cdd:COG5265 355 GGEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLL 404
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
27-61 |
7.29e-06 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 45.89 E-value: 7.29e-06
10 20 30
....*....|....*....|....*....|....*
gi 15240093 27 PIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAG 61
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMG 48
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
13-61 |
1.19e-05 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 46.33 E-value: 1.19e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 15240093 13 IRVSGMQFSY-DVQDPIFFD---FNLDLPAGSRCLLVGANGSGKTTLLKILAG 61
Cdd:COG4615 328 LELRGVTYRYpGEDGDEGFTlgpIDLTIRRGELVFIVGGNGSGKSTLAKLLTG 380
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
11-61 |
1.28e-05 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 46.25 E-value: 1.28e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 15240093 11 GAIRVSGMQFSYDVQDPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAG 61
Cdd:PRK10790 339 GRIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMG 389
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
31-206 |
1.30e-05 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 45.45 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 31 DFNLDLPAGSRCLLVGANGSGKTTLLKILAGkhmvggknvvqvLDRSAfhdtelvcSGDLSYLGGSWSKTAGSA-----G 105
Cdd:PRK10419 30 NVSLSLKSGETVALLGRSGCGKSTLARLLVG------------LESPS--------QGNVSWRGEPLAKLNRAQrkafrR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 106 DIPL--QGDFSAEHMIFGVEGI--DPFR--------------RE--KLIDLLDINLQWRMHKVSDGQRRRVQICMGLLHP 165
Cdd:PRK10419 90 DIQMvfQDSISAVNPRKTVREIirEPLRhllsldkaerlaraSEmlRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15240093 166 FKVLLLDEVTVDLDVVARMDLLEFFKEECEQRGATIVYATH 206
Cdd:PRK10419 170 PKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITH 210
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
29-60 |
1.55e-05 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 45.37 E-value: 1.55e-05
10 20 30
....*....|....*....|....*....|...
gi 15240093 29 FFDFNLDLPAGSR-CLLVGANGSGKTTLLKILA 60
Cdd:COG3950 14 FEDLEIDFDNPPRlTVLVGENGSGKTTLLEAIA 46
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
12-205 |
1.91e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.88 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 12 AIRVSGMQFSYD--VQDPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAGkhmvggknvvqvlDRSAFHDTELVCSGD 89
Cdd:PLN03130 614 AISIKNGYFSWDskAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLG-------------ELPPRSDASVVIRGT 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 90 LSYLGG-SWSKTAGSAGDIplqgdfsaehmIFGVEgIDPFRREKLIDL--LDINLQW-----------RMHKVSDGQRRR 155
Cdd:PLN03130 681 VAYVPQvSWIFNATVRDNI-----------LFGSP-FDPERYERAIDVtaLQHDLDLlpggdlteigeRGVNISGGQKQR 748
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15240093 156 VQICMGLLHPFKVLLLDEVTVDLDV-VARMDLLEFFKEECeqRGATIVYAT 205
Cdd:PLN03130 749 VSMARAVYSNSDVYIFDDPLSALDAhVGRQVFDKCIKDEL--RGKTRVLVT 797
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
146-206 |
2.17e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 45.47 E-value: 2.17e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15240093 146 HKVSDGQRRRVQICMGLLHPFKVLLLDEVTVDLDVVARMDLLEFFKEECEQRGATIVYATH 206
Cdd:PRK15134 155 HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITH 215
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
13-206 |
2.40e-05 |
|
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: 44.24 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 13 IRVSGMQFSYDVQDPIFFDFNLDLPAGSRCLLVGANGSGKTT-LLKILAGKHMVGGK----NVVQvlDRSAFHDTELVCS 87
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSlLLAILGEMQTLEGKvhwsNKNE--SEPSFEATRSRNR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 88 GDLSYLG-GSWSKTAGSAGDIPLQGDFSAEHMIFGVEG------ID--PFRREKLIDLLDINLqwrmhkvSDGQRRRVQI 158
Cdd:cd03290 79 YSVAYAAqKPWLLNATVEENITFGSPFNKQRYKAVTDAcslqpdIDllPFGDQTEIGERGINL-------SGGQRQRICV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15240093 159 CMGLLHPFKVLLLDEVTVDLDV-----VARMDLLEFFKEecEQRgaTIVYATH 206
Cdd:cd03290 152 ARALYQNTNIVFLDDPFSALDIhlsdhLMQEGILKFLQD--DKR--TLVLVTH 200
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
12-61 |
2.47e-05 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 44.76 E-value: 2.47e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 15240093 12 AIRVSGMQFSYDvQDPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAG 61
Cdd:PRK13548 2 MLEARNLSVRLG-GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSG 50
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
33-209 |
2.85e-05 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 45.01 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 33 NLDLPAGSRCLLVGANGSGKTTLLKILAGKH-------MVGGKNVvqvldrsAFHDTelvcsgdlsylggswsKTAGSAG 105
Cdd:COG1129 24 SLELRPGEVHALLGENGAGKSTLMKILSGVYqpdsgeiLLDGEPV-------RFRSP----------------RDAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 106 ------DIPLQGDFS-AEHMIFGVE-----GIDP---FRR-EKLIDLLDINLQWRMhKVSD---GQRRRVQICMGLLHPF 166
Cdd:COG1129 81 iaiihqELNLVPNLSvAENIFLGREprrggLIDWramRRRaRELLARLGLDIDPDT-PVGDlsvAQQQLVEIARALSRDA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15240093 167 KVLLLDEVTVDLDV--VARM-DLLEFFKEeceqRGATIVYATHIFD 209
Cdd:COG1129 160 RVLILDEPTASLTEreVERLfRIIRRLKA----QGVAIIYISHRLD 201
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
31-226 |
3.07e-05 |
|
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: 44.18 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 31 DFNLDLPAGSRCLLVGANGSGKTTLLKILAGK----HMVGGKNVV--------QVLDRSAF---HDTelvcsgDLSYLG- 94
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGRveggGTTSGQILFngqprkpdQFQKCVAYvrqDDI------LLPGLTv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 95 -GSWSKTAGSAGDIPLQGDFSAEhmifgvegIDPFRREKLIDLLDINLQwRMHKVSDGQRRRVQICMGLLHPFKVLLLDE 173
Cdd:cd03234 99 rETLTYTAILRLPRKSSDAIRKK--------RVEDVLLRDLALTRIGGN-LVKGISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15240093 174 VTVDLDVVARMDLLEFFKEECeqRGATIVYAT---------HIFDgletwasHLAYINGGEL 226
Cdd:cd03234 170 PTSGLDSFTALNLVSTLSQLA--RRNRIVILTihqprsdlfRLFD-------RILLLSSGEI 222
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
12-223 |
3.46e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 44.49 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 12 AIRVSGMQFSYDVQDPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAG-KHMVGGK-NVVQVLDRSAFHDTeLVcsgd 89
Cdd:PRK15056 6 GIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGfVRLASGKiSILGQPTRQALQKN-LV---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 90 lSYLGGS----WSKTAgSAGDIPLQGDFSaeHMIFgvegidpFRREKLID-------LLDINLQWRMHK----VSDGQRR 154
Cdd:PRK15056 81 -AYVPQSeevdWSFPV-LVEDVVMMGRYG--HMGW-------LRRAKKRDrqivtaaLARVDMVEFRHRqigeLSGGQKK 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15240093 155 RVQICMGLLHPFKVLLLDE--VTVDLDVVARM-DLLEFFKEEceqrGATIVYATHIFDGLETWASHLAYING 223
Cdd:PRK15056 150 RVFLARAIAQQGQVILLDEpfTGVDVKTEARIiSLLRELRDE----GKTMLVSTHNLGSVTEFCDYTVMVKG 217
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
44-224 |
3.51e-05 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 44.41 E-value: 3.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 44 LVGANGSGKTTLLKILAGKHMVGgknvvqvldrsafhdtelvcSGDLSYLGGSWSKTAGSA----GDIP----LQGDFSA 115
Cdd:PRK13537 38 LLGPNGAGKTTTLRMLLGLTHPD--------------------AGSISLCGEPVPSRARHArqrvGVVPqfdnLDPDFTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 116 EH--MIFG-------------VEGIDPFRReklidlLDINLQWRMHKVSDGQRRRVQICMGLLHPFKVLLLDEVTVDLDV 180
Cdd:PRK13537 98 REnlLVFGryfglsaaaaralVPPLLEFAK------LENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDP 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15240093 181 VARMDLLEFFKeECEQRGATIVYATHIFDGLETWASHLAYINGG 224
Cdd:PRK13537 172 QARHLMWERLR-SLLARGKTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
16-209 |
3.60e-05 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 44.23 E-value: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 16 SGMQFSYdvQD-PIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAG-------------KHMVGGKNVVQVLDR---SA 78
Cdd:PRK13638 5 SDLWFRY--QDePVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGllrpqkgavlwqgKPLDYSKRGLLALRQqvaTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 79 FHDTElvcsGDLSYLggswsktagsagDIPLQGDFSAEHMifGVEGIDPFRR-EKLIDLLDIN--LQWRMHKVSDGQRRR 155
Cdd:PRK13638 83 FQDPE----QQIFYT------------DIDSDIAFSLRNL--GVPEAEITRRvDEALTLVDAQhfRHQPIQCLSHGQKKR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15240093 156 VQICMGLLHPFKVLLLDEVTVDLDVVARMDLLEFFKEECEQrGATIVYATHIFD 209
Cdd:PRK13638 145 VAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDID 197
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
13-179 |
3.65e-05 |
|
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: 44.07 E-value: 3.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 13 IRVSGMQFSY----DVqdPIFFDFNLDLPAGSRCLLVGANGSGKTTllkilagkhmvggknVVQVLDRsaFHDtelVCSG 88
Cdd:cd03249 1 IEFKNVSFRYpsrpDV--PILKGLSLTIPPGKTVALVGSSGCGKST---------------VVSLLER--FYD---PTSG 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 89 DLsYLGGSWSKT--------------------AGSAGDIPLQGDFSA--EHMI--FGVEGIDPFrREKLIDLLDINLQWR 144
Cdd:cd03249 59 EI-LLDGVDIRDlnlrwlrsqiglvsqepvlfDGTIAENIRYGKPDAtdEEVEeaAKKANIHDF-IMSLPDGYDTLVGER 136
|
170 180 190
....*....|....*....|....*....|....*
gi 15240093 145 MHKVSDGQRRRVQICMGLLHPFKVLLLDEVTVDLD 179
Cdd:cd03249 137 GSQLSGGQKQRIAIARALLRNPKILLLDEATSALD 171
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
31-206 |
3.80e-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: 44.68 E-value: 3.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 31 DFNLDLPAGSRCLLVGANGSGKTTL-LKILAgkhmvggknvvqvLDRSafhdtelvcSGDLSYLGGSWSKTAGSAgDIPL 109
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTLgLALLR-------------LIPS---------EGEIRFDGQDLDGLSRRA-LRPL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 110 QGDFsaeHMIFGvegiDPF----------------------------RREKLIDL-----LDINLQWRM-HKVSDGQRRR 155
Cdd:COG4172 361 RRRM---QVVFQ----DPFgslsprmtvgqiiaeglrvhgpglsaaeRRARVAEAleevgLDPAARHRYpHEFSGGQRQR 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15240093 156 VQICMGL-LHPfKVLLLDEVTVDLDVVARMDLLEFFKEECEQRGATIVYATH 206
Cdd:COG4172 434 IAIARALiLEP-KLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISH 484
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
4-179 |
4.07e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.02 E-value: 4.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 4 KNASAVDGAIRVSGMQFSYDVQD--PIFFDFNLDLPAGSRCLLVGANGSGKTTLLKIL------AGKHMVGGKNVvQVLD 75
Cdd:PTZ00265 1157 KNKNDIKGKIEIMDVNFRYISRPnvPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlKNDHHIVFKNE-HTND 1235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 76 RSAFHDTElvcsGDLSYLGG-------SWSKTAGSA---------GDIPLQG----DF------------SAEHMIFGVE 123
Cdd:PTZ00265 1236 MTNEQDYQ----GDEEQNVGmknvnefSLTKEGGSGedstvfknsGKILLDGvdicDYnlkdlrnlfsivSQEPMLFNMS 1311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 124 ------------------------GIDPFRrEKLIDLLDINLQWRMHKVSDGQRRRVQICMGLLHPFKVLLLDEVTVDLD 179
Cdd:PTZ00265 1312 iyenikfgkedatredvkrackfaAIDEFI-ESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLD 1390
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
144-206 |
4.68e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 43.94 E-value: 4.68e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 144 RM----HKVSDGQRRRVQICMGLLHPFKVLLLDEVTVDLDVVAR---MDLLEFFKEECeqrGATIVYATH 206
Cdd:PRK09473 154 RMkmypHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQaqiMTLLNELKREF---NTAIIMITH 220
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
32-206 |
5.98e-05 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 43.29 E-value: 5.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 32 FNLDLPAGSRCLLVGANGSGKTTLLKILAGkhMVGGKNVVQVLDR--SAFHDTEL-----------VCSGDL---SYLGG 95
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAG--LLPGQGEILLNGRplSDWSAAELarhraylsqqqSPPFAMpvfQYLAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 96 SWSKTAGSAGDIPLQGDFSaehmifgvegidpfRREKLIDLLDINLqwrmHKVSDGQRRRVQICMGLL--HPF-----KV 168
Cdd:COG4138 93 HQPAGASSEAVEQLLAQLA--------------EALGLEDKLSRPL----TQLSGGEWQRVRLAAVLLqvWPTinpegQL 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 15240093 169 LLLDEVTVDLDVVARMDLLEFFKEECEQrGATIVYATH 206
Cdd:COG4138 155 LLLDEPMNSLDVAQQAALDRLLRELCQQ-GITVVMSSH 191
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
33-214 |
6.46e-05 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 44.07 E-value: 6.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 33 NLDLPAGSRCLLVGANGSGKTTLLKILA------GKHMVGGKNVVQvLDRSAFHDTelvcsgdLSYLGGSWSKTAGSAGD 106
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLgflpyqGSLKINGIELRE-LDPESWRKH-------LSWVGQNPQLPHGTLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 107 IPLQGDFSAE----HMIFGVEGIDPFrREKLIDLLDINLQWRMHKVSDGQRRRVQICMGLLHPFKVLLLDEVTVDLDVVA 182
Cdd:PRK11174 442 NVLLGNPDASdeqlQQALENAWVSEF-LPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHS 520
|
170 180 190
....*....|....*....|....*....|..
gi 15240093 183 RMDLLEFFKEecEQRGATIVYATHIFDGLETW 214
Cdd:PRK11174 521 EQLVMQALNA--ASRRQTTLMVTHQLEDLAQW 550
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
31-61 |
6.82e-05 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 43.19 E-value: 6.82e-05
10 20 30
....*....|....*....|....*....|.
gi 15240093 31 DFNLDLPAGSRCLLVGANGSGKTTLLKILAG 61
Cdd:COG4181 30 GISLEVEAGESVAIVGASGSGKSTLLGLLAG 60
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
39-206 |
7.78e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 41.98 E-value: 7.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 39 GSRCLLVGANGSGKTTLLKILAGKHMVGGKNVVqvldrsafhdtelvcsgdlsYLGGswsktagsagdiplqgdfsaehm 118
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVI--------------------YIDG----------------------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 119 ifgvegiDPFRREKLIDLLDINLQWRMHKVSDGQRRRVQICMGLLHPFKVLLLDEVTVDLDVVARMDLLE-----FFKEE 193
Cdd:smart00382 39 -------EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrLLLLL 111
|
170
....*....|...
gi 15240093 194 CEQRGATIVYATH 206
Cdd:smart00382 112 KSEKNLTVILTTN 124
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
31-238 |
7.78e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 43.86 E-value: 7.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 31 DFNLDLPAGS-RCLLvGANGSGKTTLLKILAGKH-------MVGGKNVvqvldrsAFHDtelvcsgdlsylggswSKTAG 102
Cdd:COG3845 23 DVSLTVRPGEiHALL-GENGAGKSTLMKILYGLYqpdsgeiLIDGKPV-------RIRS----------------PRDAI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 103 SAG---------DIPlqgDFS-AEHMIFGVEGIDPFR------REKLIDL-----LDINLQWRMHKVSDGQRRRVQICMG 161
Cdd:COG3845 79 ALGigmvhqhfmLVP---NLTvAENIVLGLEPTKGGRldrkaaRARIRELserygLDVDPDAKVEDLSVGEQQRVEILKA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 162 LLHPFKVLLLDEVT-------VDldvvarmDLLEFFKEECEQrGATIVYATHifdgletwashlayinggelklsaKLDE 234
Cdd:COG3845 156 LYRGARILILDEPTavltpqeAD-------ELFEILRRLAAE-GKSIIFITH------------------------KLRE 203
|
....
gi 15240093 235 IKDL 238
Cdd:COG3845 204 VMAI 207
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
9-179 |
8.53e-05 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 43.85 E-value: 8.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 9 VDGAIRVSGMQFSYDVQD-PIFFDFNLDLPAGSRCLLVGANGSGKTTLLKIL-------AGKHMVGGKNV---------- 70
Cdd:PRK11176 338 AKGDIEFRNVTFTYPGKEvPALRNINFKIPAGKTVALVGRSGSGKSTIANLLtrfydidEGEILLDGHDLrdytlaslrn 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 71 -VQVLDRSA--FHDTelvCSGDLSYL-GGSWSKTagsagDIPlqgdfSAEHMIFGVEGIdpfrrEKLIDLLDINLQWRMH 146
Cdd:PRK11176 418 qVALVSQNVhlFNDT---IANNIAYArTEQYSRE-----QIE-----EAARMAYAMDFI-----NKMDNGLDTVIGENGV 479
|
170 180 190
....*....|....*....|....*....|...
gi 15240093 147 KVSDGQRRRVQICMGLLHPFKVLLLDEVTVDLD 179
Cdd:PRK11176 480 LLSGGQRQRIAIARALLRDSPILILDEATSALD 512
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
27-61 |
1.05e-04 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 42.66 E-value: 1.05e-04
10 20 30
....*....|....*....|....*....|....*
gi 15240093 27 PIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAG 61
Cdd:COG0410 17 HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISG 51
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
31-226 |
1.16e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 42.84 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 31 DFNLDLPAGSRCLLVGANGSGKTTLLKILAG--KHMVGgknVVQVLDRSAFHDTElvcSGDLSYLggswSKTAGSAGDIP 108
Cdd:PRK13646 25 DVNTEFEQGKYYAIVGQTGSGKSTLIQNINAllKPTTG---TVTVDDITITHKTK---DKYIRPV----RKRIGMVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 109 ---LQGDFSAEHMIFG-------VEGIDPFRREKLIDL---LDInLQWRMHKVSDGQRRRVQICMGLLHPFKVLLLDEVT 175
Cdd:PRK13646 95 esqLFEDTVEREIIFGpknfkmnLDEVKNYAHRLLMDLgfsRDV-MSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15240093 176 VDLDVVARMDLLEFFKEECEQRGATIVYATHIFDGLETWASHLAYINGGEL 226
Cdd:PRK13646 174 AGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
147-236 |
1.34e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 42.80 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 147 KVSDGQRRRVQICMGLLHPFKVLLLDEVTVDLDVVARMDLLEFFKEECEQrGATIVYATHIFDGLETWASHLAYINGGEL 226
Cdd:NF000106 144 KYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRV 222
|
90
....*....|
gi 15240093 227 KLSAKLDEIK 236
Cdd:NF000106 223 IADGKVDELK 232
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
13-61 |
1.87e-04 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 41.69 E-value: 1.87e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 15240093 13 IRVSGMQFSYD----VQDPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAG 61
Cdd:cd03250 1 ISVEDASFTWDsgeqETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLG 53
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
148-235 |
1.88e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 42.12 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 148 VSDGQRRRVQICMGLLHPFKVLLLDEVTVDLDVVARMDLLEFFKEEcEQRGATIVYATHIFDGLETWASHLAYINGGELK 227
Cdd:PRK13641 146 LSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDY-QKAGHTVILVTHNMDDVAEYADDVLVLEHGKLI 224
|
....*...
gi 15240093 228 LSAKLDEI 235
Cdd:PRK13641 225 KHASPKEI 232
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-224 |
2.04e-04 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 42.13 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 1 MAEKNASAVDGAIRVSGMQFSYDvQDPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAGkhmvggknvvqvldrsafh 80
Cdd:PRK13536 30 KASIPGSMSTVAIDLAGVSKSYG-DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILG------------------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 81 dteLVC--SGDLSYLGGSWSKTAGSA----GDIP----LQGDFSAEH--MIFG---------VEGIDP----FRReklid 135
Cdd:PRK13536 90 ---MTSpdAGKITVLGVPVPARARLArariGVVPqfdnLDLEFTVREnlLVFGryfgmstreIEAVIPslleFAR----- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 136 lLDINLQWRMHKVSDGQRRRVQICMGLLHPFKVLLLDEVTVDLDVVARMDLLEFFKeECEQRGATIVYATHIFDGLETWA 215
Cdd:PRK13536 162 -LESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLR-SLLARGKTILLTTHFMEEAERLC 239
|
....*....
gi 15240093 216 SHLAYINGG 224
Cdd:PRK13536 240 DRLCVLEAG 248
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
146-226 |
2.08e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 41.99 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 146 HKVSDGQRRRVQICmGLL--HPfKVLLLDEVTVDLDVVARMDLLEFFKEeCEQRGATIVYATHIFDGLETWASHLAYING 223
Cdd:PRK13639 136 HHLSGGQKKRVAIA-GILamKP-EIIVLDEPTSGLDPMGASQIMKLLYD-LNKEGITIIISTHDVDLVPVYADKVYVMSD 212
|
...
gi 15240093 224 GEL 226
Cdd:PRK13639 213 GKI 215
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
28-242 |
2.20e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 41.96 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 28 IFFDFNLDLPAGSRCLLVGANGSGKTTLLKILagkhmvggKNVVQVldrsafHDTELVCSGDLSYLGgswsKTAGSAGDI 107
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVL--------NRLIEI------YDSKIKVDGKVLYFG----KDIFQIDAI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 108 PLQGDFSaehMIFgvEGIDPF--------------------RRE--KLID--LLDINLQWRMH--------KVSDGQRRR 155
Cdd:PRK14246 87 KLRKEVG---MVF--QQPNPFphlsiydniayplkshgikeKREikKIVEecLRKVGLWKEVYdrlnspasQLSGGQQQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 156 VQICMGLLHPFKVLLLDEVTVDLDVVARMDLLEFFKEecEQRGATIVYATHIFDGLETWASHLAYINGGELKLSAKLDEI 235
Cdd:PRK14246 162 LTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITE--LKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI 239
|
....*..
gi 15240093 236 kdlKTSP 242
Cdd:PRK14246 240 ---FTSP 243
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
21-241 |
2.28e-04 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 42.13 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 21 SYDVQdPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAGKHMVGGKNVVqvLDrsafhdtelvcSGDLSYLGGSWSKT 100
Cdd:PRK11607 28 SFDGQ-HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIM--LD-----------GVDLSHVPPYQRPI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 101 AGSAGDIPLQGDFSAEHMI-FGVE------GIDPFRREKLIDLLDIN--LQWRMHKVSDGQRRRVQICMGLLHPFKVLLL 171
Cdd:PRK11607 94 NMMFQSYALFPHMTVEQNIaFGLKqdklpkAEIASRVNEMLGLVHMQefAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15240093 172 DEVTVDLDVVAR-------MDLLeffkeecEQRGATIVYATHIFDGLETWASHLAYINGGELKLSAKLDEIKDLKTS 241
Cdd:PRK11607 174 DEPMGALDKKLRdrmqlevVDIL-------ERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTT 243
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
31-206 |
2.35e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 42.46 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 31 DFNLDLPAGSRCLLVGANGSGKTTLLKILAGKHMvGGKNVVQVLDRSAFHDT--------------ELVCSGDLSYLGGS 96
Cdd:PRK09700 23 SVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHE-PTKGTITINNINYNKLDhklaaqlgigiiyqELSVIDELTVLENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 97 WsktagsAGDIPLQgdfsaehMIFGVEGID-PFRREKLIDLLD-----INLQWRMHKVSDGQRRRVQICMGLLHPFKVLL 170
Cdd:PRK09700 102 Y------IGRHLTK-------KVCGVNIIDwREMRVRAAMMLLrvglkVDLDEKVANLSISHKQMLEIAKTLMLDAKVII 168
|
170 180 190
....*....|....*....|....*....|....*.
gi 15240093 171 LDEVTVDLdVVARMDLLEFFKEECEQRGATIVYATH 206
Cdd:PRK09700 169 MDEPTSSL-TNKEVDYLFLIMNQLRKEGTAIVYISH 203
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
31-215 |
2.40e-04 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 42.01 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 31 DFNLDLPAGSRCLLVGANGSGKTTLLKILAG-------KHMVGGKNV----VQVLDrsafhdtelVCSGDLSYlggswsk 99
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGlekptegQIFIDGEDVthrsIQQRD---------ICMVFQSY------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 100 tA----GSAGD-----IPLQGDFSAEhmifgvegidpfRRE------KLIDLLDINLQWrMHKVSDGQRRRVQICMGLLH 164
Cdd:PRK11432 88 -AlfphMSLGEnvgygLKMLGVPKEE------------RKQrvkealELVDLAGFEDRY-VDQISGGQQQRVALARALIL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15240093 165 PFKVLLLDEVTVDLDVVARMDLLEFFKEECEQRGATIVYATHifDGLETWA 215
Cdd:PRK11432 154 KPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTH--DQSEAFA 202
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
33-60 |
2.89e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 41.84 E-value: 2.89e-04
10 20
....*....|....*....|....*...
gi 15240093 33 NLDLPAGSRCLLVGANGSGKTTLLKILA 60
Cdd:COG4637 15 DLELPLGPLTVLIGANGSGKSNLLDALR 42
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
44-206 |
2.93e-04 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 41.34 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 44 LVGANGSGKTTLLkilagkHMVGGknvvqvLDRSAfhdtelvcSGDLSYLGGSWSKTAGSA---------GDI----PLQ 110
Cdd:PRK11629 40 IVGSSGSGKSTLL------HLLGG------LDTPT--------SGDVIFNGQPMSKLSSAAkaelrnqklGFIyqfhHLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 111 GDFSAEH---MIFGVEGIDPFR-REKLIDLLD-INLQWRMH----KVSDGQRRRVQICMGLLHPFKVLLLDEVTVDLDVV 181
Cdd:PRK11629 100 PDFTALEnvaMPLLIGKKKPAEiNSRALEMLAaVGLEHRANhrpsELSGGERQRVAIARALVNNPRLVLADEPTGNLDAR 179
|
170 180
....*....|....*....|....*
gi 15240093 182 ARMDLLEFFKEECEQRGATIVYATH 206
Cdd:PRK11629 180 NADSIFQLLGELNRLQGTAFLVVTH 204
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
21-206 |
3.02e-04 |
|
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: 41.84 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 21 SYDVQDPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAGKhmvggknvvqvldrsafhDTElvcsgdlsYLGGSWSKT 100
Cdd:TIGR03719 13 VVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV------------------DKD--------FNGEARPQP 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 101 AGSAGDIPLQGDFSAEHMIFGV--EGIDPFRR-------------------EKLI-------------DLLDINLQ---- 142
Cdd:TIGR03719 67 GIKVGYLPQEPQLDPTKTVRENveEGVAEIKDaldrfneisakyaepdadfDKLAaeqaelqeiidaaDAWDLDSQleia 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15240093 143 ----------WRMHKVSDGQRRRVQICMGLLHPFKVLLLDEVTVDLDV--VArmdLLEFFKEECEqrgATIVYATH 206
Cdd:TIGR03719 147 mdalrcppwdADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAesVA---WLERHLQEYP---GTVVAVTH 216
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
13-62 |
3.02e-04 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 41.29 E-value: 3.02e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 15240093 13 IRVSGMQFSYDvQDPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAGK 62
Cdd:PRK11831 8 VDMRGVSFTRG-NRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQ 56
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
149-206 |
3.61e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 41.22 E-value: 3.61e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 149 SDGQRRRVQICMGLL--HPFkvLLLDEVTVDLDVVARMDLLEFFKEECEQRGATIVYATH 206
Cdd:PRK10418 142 SGGMLQRMMIALALLceAPF--IIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTH 199
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
31-180 |
3.91e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 41.64 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 31 DFNLDLPAGSRCLLVGANGSGKTTLLKILAGK------------------------HMVGGKNVVQVLdrsafhdtelvc 86
Cdd:PRK11819 342 DLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQeqpdsgtikigetvklayvdqsrdALDPNKTVWEEI------------ 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 87 SG--DLSYLGGSwsktagsagDIPLQGDFSAehmiFGVEGIDpfrREKLIDLLdinlqwrmhkvSDGQRRRVQICMGLLH 164
Cdd:PRK11819 410 SGglDIIKVGNR---------EIPSRAYVGR----FNFKGGD---QQKKVGVL-----------SGGERNRLHLAKTLKQ 462
|
170
....*....|....*.
gi 15240093 165 PFKVLLLDEVTVDLDV 180
Cdd:PRK11819 463 GGNVLLLDEPTNDLDV 478
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
13-209 |
4.44e-04 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 41.37 E-value: 4.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 13 IRVSGMQFSYDVQdPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKIL-------AGKHMVGGKNVVQvldRSAFHDTELV 85
Cdd:PRK09536 4 IDVSDLSVEFGDT-TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAIngtltptAGTVLVAGDDVEA---LSARAASRRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 86 csgdlsylggswsktAGSAGDIPLQGDFSAEHMI----------FGveGIDPFRR---EKLIDLLDIN--LQWRMHKVSD 150
Cdd:PRK09536 80 ---------------ASVPQDTSLSFEFDVRQVVemgrtphrsrFD--TWTETDRaavERAMERTGVAqfADRPVTSLSG 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15240093 151 GQRRRVQICMGLLHPFKVLLLDEVTVDLDVVARMDLLEFFKEECEQrGATIVYATHIFD 209
Cdd:PRK09536 143 GERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLD 200
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
31-206 |
5.84e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 41.05 E-value: 5.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 31 DFNLDLPAGSRCLLVGANGSGKTTLLKILAGKH-------MVGGKNVVQVLDRSAFHD------TELVCSGDLSYlggsw 97
Cdd:PRK11288 22 DISFDCRAGQVHALMGENGAGKSTLLKILSGNYqpdagsiLIDGQEMRFASTTAALAAgvaiiyQELHLVPEMTV----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 98 sktagsAGDIPLqGDFSAEHMIFGVEGIDPFRREKLIDL-LDINLQWRMHKVSDGQRRRVQICMGLLHPFKVLLLDEVTV 176
Cdd:PRK11288 97 ------AENLYL-GQLPHKGGIVNRRLLNYEAREQLEHLgVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTS 169
|
170 180 190
....*....|....*....|....*....|...
gi 15240093 177 DLDvvAR-MDLLefFK--EECEQRGATIVYATH 206
Cdd:PRK11288 170 SLS--AReIEQL--FRviRELRAEGRVILYVSH 198
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
18-61 |
7.35e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 40.65 E-value: 7.35e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 15240093 18 MQFSydvQDPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAG 61
Cdd:PRK15064 9 MQFG---AKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGG 49
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
39-67 |
7.54e-04 |
|
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: 39.53 E-value: 7.54e-04
10 20
....*....|....*....|....*....
gi 15240093 39 GSRCLLVGANGSGKTTLLKILAGKHMVGG 67
Cdd:cd03232 33 GTLTALMGESGAGKTTLLDVLAGRKTAGV 61
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
129-235 |
9.32e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 40.11 E-value: 9.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 129 RREKLIDLLDI--------NLQWRMHKVSDGQRRRVQICMGLLHPFKVLLLDEVTVDLDVVARMDLLEFFKEECEQRGAT 200
Cdd:PRK11022 127 RRQRAIDLLNQvgipdpasRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMA 206
|
90 100 110
....*....|....*....|....*....|....*
gi 15240093 201 IVYATHIFDGLETWASHLAYINGGELKLSAKLDEI 235
Cdd:PRK11022 207 LVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
148-244 |
9.46e-04 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 39.95 E-value: 9.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 148 VSDGQRRRVQICMGLLHPFKVLLLDEVTVDLDVVARMDLLEFFKEECEQrGATIVYATHIFDGLETWASHLAYINGGELK 227
Cdd:PRK10619 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIE 231
|
90
....*....|....*..
gi 15240093 228 LSAKLDEIKDLKTSPNL 244
Cdd:PRK10619 232 EEGAPEQLFGNPQSPRL 248
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
31-80 |
1.26e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 40.11 E-value: 1.26e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 15240093 31 DFNLDLPAGSRCLLVGANGSGKTTLLKILAG-KHMVGGKnvVQVLD---RSAFH 80
Cdd:NF033858 19 DVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGaRKIQQGR--VEVLGgdmADARH 70
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
13-206 |
1.62e-03 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 39.55 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 13 IRVSGMQFSYDVQdPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAGKHMVggknvvqvldrsafhdtelvcsgdlsy 92
Cdd:PRK09452 15 VELRGISKSFDGK-EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETP--------------------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 93 lggswsktagSAGDIPLQG----DFSAE---------------HMI------FGV-------EGIDPFRRE--KLIDLLD 138
Cdd:PRK09452 67 ----------DSGRIMLDGqditHVPAEnrhvntvfqsyalfpHMTvfenvaFGLrmqktpaAEITPRVMEalRMVQLEE 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15240093 139 INlQWRMHKVSDGQRRRVQICMGLLHPFKVLLLDEVTVDLDVVARMDLLEFFKEECEQRGATIVYATH 206
Cdd:PRK09452 137 FA-QRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTH 203
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
13-202 |
1.67e-03 |
|
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: 39.01 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 13 IRVSGMQFSYDVQDP-IFFDFNLDLPAGSRCLLVGANGSGKTTLLKILA-------GKHMVGGKNVVQVlDRSAFHDTEL 84
Cdd:cd03252 1 ITFEHVRFRYKPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQrfyvpenGRVLVDGHDLALA-DPAWLRRQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 85 VCSGDLSYLGGSWSKTAGSAGDIPlqgdfSAEHMIFGVE--GIDPFRREkLIDLLDINLQWRMHKVSDGQRRRVQICMGL 162
Cdd:cd03252 80 VVLQENVLFNRSIRDNIALADPGM-----SMERVIEAAKlaGAHDFISE-LPEGYDTIVGEQGAGLSGGQRQRIAIARAL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15240093 163 LHPFKVLLLDEVTVDLDVVARMDLLEFFKEECEQRGATIV 202
Cdd:cd03252 154 IHNPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIII 193
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
31-62 |
2.06e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 39.55 E-value: 2.06e-03
10 20 30
....*....|....*....|....*....|..
gi 15240093 31 DFNLDLPAGSRCLLVGANGSGKTTLLKILAGK 62
Cdd:PRK11147 337 DFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQ 368
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
120-235 |
2.26e-03 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 39.09 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 120 FGVEGIDPFRREKLIDLLDIN-LQWRM-HKVSDGQRRRVQICMGLLHPFKVLLLDEVTVDLDVVARMDLLEFFKEECEQR 197
Cdd:PRK11144 99 YGMAKSMVAQFDKIVALLGIEpLLDRYpGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREI 178
|
90 100 110
....*....|....*....|....*....|....*...
gi 15240093 198 GATIVYATHIFDGLETWASHLAYINGGELKLSAKLDEI 235
Cdd:PRK11144 179 NIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
31-61 |
2.26e-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: 38.28 E-value: 2.26e-03
10 20 30
....*....|....*....|....*....|.
gi 15240093 31 DFNLDLPAGSRCLLVGANGSGKTTLLKILAG 61
Cdd:cd03217 18 GVNLTIKKGEVHALMGPNGSGKSTLAKTIMG 48
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
147-209 |
2.47e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 38.56 E-value: 2.47e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15240093 147 KVSDGQRRRVQICMGLLHPFKVLLLDEVTVDLDVVARMDLLEFFKEECEQRGATIVYATHIFD 209
Cdd:PRK13650 140 RLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLD 202
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
34-61 |
2.53e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 39.00 E-value: 2.53e-03
10 20
....*....|....*....|....*...
gi 15240093 34 LDLPAGSRCLLVGANGSGKTTLLKILAG 61
Cdd:PRK10636 333 LNLVPGSRIGLLGRNGAGKSTLIKLLAG 360
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
31-235 |
2.74e-03 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 38.86 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 31 DFNLDLPAGSRCLLVGANGSGKTTLLKILAGK-HMVGGKNVVQVLDRSAFHDTEL--VCSGDLSYLGGSWSKTA------ 101
Cdd:PRK10070 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLiEPTRGQVLIDGVDIAKISDAELreVRRKKIAMVFQSFALMPhmtvld 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 102 GSAGDIPLQGDFSAEhmifgvegidpfRREKLIDLL-DINLQWRMH----KVSDGQRRRVQICMGLLHPFKVLLLDEVTV 176
Cdd:PRK10070 126 NTAFGMELAGINAEE------------RREKALDALrQVGLENYAHsypdELSGGMRQRVGLARALAINPDILLMDEAFS 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15240093 177 DLDVVARMDLLEFFKEECEQRGATIVYATHIFDGLETWASHLAYINGGELKLSAKLDEI 235
Cdd:PRK10070 194 ALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
146-206 |
2.78e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 39.07 E-value: 2.78e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15240093 146 HKVSDGQRRRVQICMGLLHPFKVLLLDEVTVDLDVVARMDLLEFFKEECEQRGATIVYATH 206
Cdd:PRK10261 167 HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITH 227
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
44-61 |
3.57e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 38.56 E-value: 3.57e-03
|
| VirB4 |
COG3451 |
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ... |
27-248 |
4.25e-03 |
|
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442674 [Multi-domain] Cd Length: 546 Bit Score: 38.39 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 27 PIFFDFNLDLPAGSrCLLVGANGSGKTTLLKILAGKHMVGGKNVVqVLD--RSAFHDTELvcsgdlsyLGGSWSktagsa 104
Cdd:COG3451 193 PVFFDFHDGLDNGN-TLILGPSGSGKSFLLKLLLLQLLRYGARIV-IFDpgGSYEILVRA--------LGGTYI------ 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 105 gdiplqgDFSAEHMIfgveGIDPFR-------REKLIDLLDINLQWRMHKVSDGQRRRVQICmgllhpfkvllLDEVTVD 177
Cdd:COG3451 257 -------DLSPGSPT----GLNPFDledteekRDFLLELLELLLGREGEPLTPEERAAIDRA-----------VRALYRR 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 178 LDVVARM---DLLEFFKEECEqrgativyATHIFDGLETWASHLAYI----NGGELKLSAKlD----EIKDLKTSPNLLS 246
Cdd:COG3451 315 ADPEERTtlsDLYELLKEQPE--------AKDLAARLEPYTKGGSYGwlfdGPTNLDLSDA-RfvvfDLTELLDNPELRP 385
|
..
gi 15240093 247 VV 248
Cdd:COG3451 386 PV 387
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
9-181 |
4.50e-03 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 38.40 E-value: 4.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 9 VDGAIRVSGMQFSYDVQDPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKIL-------AGKHMVGGKNV----VQVLDRS 77
Cdd:PRK13657 331 VKGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLqrvfdpqSGRILIDGTDIrtvtRASLRRN 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 78 ---AFHDTELVCS--GDLSYLGgswsKTAGSAGDIPLQGDFSAEHmifgvEGIDpfRREkliDLLDINLQWRMHKVSDGQ 152
Cdd:PRK13657 411 iavVFQDAGLFNRsiEDNIRVG----RPDATDEEMRAAAERAQAH-----DFIE--RKP---DGYDTVVGERGRQLSGGE 476
|
170 180
....*....|....*....|....*....
gi 15240093 153 RRRVQICMGLLHPFKVLLLDEVTVDLDVV 181
Cdd:PRK13657 477 RQRLAIARALLKDPPILILDEATSALDVE 505
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
27-61 |
4.81e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 37.70 E-value: 4.81e-03
10 20 30
....*....|....*....|....*....|....*
gi 15240093 27 PIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAG 61
Cdd:CHL00131 21 EILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG 55
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
13-61 |
5.22e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 38.30 E-value: 5.22e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 15240093 13 IRVSGMQFSYDVQDPIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAG 61
Cdd:PLN03073 509 ISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISG 557
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
43-60 |
5.80e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 37.75 E-value: 5.80e-03
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
146-206 |
6.01e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 37.64 E-value: 6.01e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15240093 146 HKVSDGQRRRVQICMGL-LHPfKVLLLDEVTVDLDVVARMDLLEFFKEECEQRGATIVYATH 206
Cdd:PRK11308 153 HMFSGGQRQRIAIARALmLDP-DVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISH 213
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
146-206 |
8.25e-03 |
|
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: 37.36 E-value: 8.25e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15240093 146 HKVSDGQRRRVQICMGLL-HPfKVLLLDEVTVDLDVVARMDLLEFFKEECEQRGATIVYATH 206
Cdd:COG4172 155 HQLSGGQRQRVMIAMALAnEP-DLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITH 215
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
27-206 |
8.80e-03 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 36.99 E-value: 8.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 27 PIFFDFNLDLPAGSRCLLVGANGSGKTTLLKILAGKHMVGGKNV----VQVLDRSA-----FHDTELVcsgdlsylggSW 97
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSItldgKPVEGPGAergvvFQNEGLL----------PW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240093 98 SKTAGSAGdiplqgdfsaehmiFGVE--GIDPFRRE-------KLIDLLDINlQWRMHKVSDGQRRRVQICMGLLHPFKV 168
Cdd:PRK11248 85 RNVQDNVA--------------FGLQlaGVEKMQRLeiahqmlKKVGLEGAE-KRYIWQLSGGQRQRVGIARALAANPQL 149
|
170 180 190
....*....|....*....|....*....|....*...
gi 15240093 169 LLLDEVTVDLDVVARMDLLEFFKEECEQRGATIVYATH 206
Cdd:PRK11248 150 LLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITH 187
|
|
| |
