|
Name |
Accession |
Description |
Interval |
E-value |
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-226 |
5.27e-116 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 331.62 E-value: 5.27e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 1 MN-IIEIEGLEKSFDIGDSKVKILKDINLQIQKGDFVCIMGASGSGKttllqllgglDIPSVGSIRVDGTEISTLKEKEL 79
Cdd:COG1136 1 MSpLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKstllnilgglDRPTSGEVLIDGQDISSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 80 ALFRRHKIGFIFQQFNLIPVFNAEENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFA 159
Cdd:COG1136 81 ARLRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446943912 160 NEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVAAHADKVVFLLDGEVIHEHA 226
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVSDER 227
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-221 |
2.18e-101 |
|
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: 294.40 E-value: 2.18e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFDIGDSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALFR 83
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 RHKIGFIFQQFNLIPVFNAEENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPA 163
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446943912 164 IILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVAAHADKVVFLLDGEV 221
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-228 |
3.67e-85 |
|
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: 253.51 E-value: 3.67e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 2 NIIEIEGLEKSFDIGDSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELAL 81
Cdd:COG4181 7 PIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 82 FRRHKIGFIFQQFNLIPVFNAEENVGLPLLLdnVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANE 161
Cdd:COG4181 87 LRARHVGFVFQSFQLLPTLTALENVMLPLEL--AGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446943912 162 PAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVAAHADKVVFLLDGEVIHEHAES 228
Cdd:COG4181 165 PAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTAAT 231
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
3-222 |
4.26e-72 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 224.19 E-value: 4.26e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 3 IIEIEGLEKSFDIGDSKVKILKDINLQIQKGDFVCIMGASGSGKttllqllggldiPSVGSIRVDGTEISTLKEKELALF 82
Cdd:COG1135 1 MIELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKstlircinllerPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 83 RRhKIGFIFQQFNLIPVFNAEENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEP 162
Cdd:COG1135 81 RR-KIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446943912 163 AIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVAAH-ADKVVFLLDGEVI 222
Cdd:COG1135 160 KVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRiCDRVAVLENGRIV 220
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-224 |
1.82e-71 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 218.99 E-value: 1.82e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 3 IIEIEGLEKSFDIGDSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALF 82
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 83 RRHkIGFIFQQFNLIPVFNAEENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEP 162
Cdd:cd03258 81 RRR-IGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446943912 163 AIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHD-PFVAAHADKVVFLLDGEVIHE 224
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEmEVVKRICDRVAVMEKGEVVEE 222
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-227 |
4.41e-70 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 214.92 E-value: 4.41e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 3 IIEIEGLEKSFDIGdskVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALF 82
Cdd:COG2884 1 MIRFENVSKRYPGG---REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 83 RRhKIGFIFQQFNLIPVFNAEENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEP 162
Cdd:COG2884 78 RR-RIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446943912 163 AIILADEPTGALDSENSKNIIAALRNACdELGQTAVIVTHDP-FVAAHADKVVFLLDGEVIHEHAE 227
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEIN-RRGTTVLIATHDLeLVDRMPKRVLELEDGRLVRDEAR 221
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-224 |
4.55e-69 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 212.93 E-value: 4.55e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 3 IIEIEGLEKSFdiGDSKVkiLKDINLQIQKGDFVCIMGASGSGKttllqllgglDIPSVGSIRVDGTEIsTLKEKELALF 82
Cdd:COG1126 1 MIEIENLHKSF--GDLEV--LKGISLDVEKGEVVVIIGPSGSGKstllrcinllEEPDSGTITVDGEDL-TDSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 83 RRhKIGFIFQQFNLIPVFNAEENVGL-PLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANE 161
Cdd:COG1126 76 RR-KVGMVFQQFNLFPHLTVLENVTLaPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAME 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446943912 162 PAIILADEPTGALDSENSKNIIAALRNACDElGQTAVIVTHD-PFVAAHADKVVFLLDGEVIHE 224
Cdd:COG1126 155 PKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEmGFAREVADRVVFMDGGRIVEE 217
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-216 |
7.93e-66 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 205.32 E-value: 7.93e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 1 MNIIEIEGLEKSFDIGDSKVKILKDINLQIQKGDFVCIMGASGSGKttllqllgglDIPSVGSIRVDGTEISTLkekela 80
Cdd:COG1116 5 APALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKstllrliaglEKPTSGEVLVDGKPVTGP------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 81 lfrRHKIGFIFQQFNLIPVFNAEENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFAN 160
Cdd:COG1116 79 ---GPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446943912 161 EPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVAAH-ADKVVFL 216
Cdd:COG1116 156 DPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFlADRVVVL 212
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
3-223 |
3.78e-64 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 211.51 E-value: 3.78e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 3 IIEIEGLEKSFDIGDSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALF 82
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 83 RRHKIGFIFQQFNLIPVFNAEENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEP 162
Cdd:PRK10535 84 RREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446943912 163 AIILADEPTGALDSENSKNIIAALRNACDElGQTAVIVTHDPFVAAHADKVVFLLDGEVIH 223
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVAAQAERVIEIRDGEIVR 223
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
3-219 |
2.13e-63 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 197.96 E-value: 2.13e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 3 IIEIEGLEKSFDIGDSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALF 82
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 83 RRHKIGFIFQQFNLIPVFNAEENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEP 162
Cdd:TIGR02211 81 RNKKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446943912 163 AIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVAAHADKVVFLLDG 219
Cdd:TIGR02211 161 SLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVLEMKDG 217
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
3-219 |
3.46e-62 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 194.55 E-value: 3.46e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 3 IIEIEGLEKSFDIGDSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALF 82
Cdd:NF038007 1 MLNMQNAEKCYITKTIKTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKIIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 83 RRHKIGFIFQQFNLIPVFNAEENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEP 162
Cdd:NF038007 81 RRELIGYIFQSFNLIPHLSIFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446943912 163 AIILADEPTGALDSENSKNIIAALRNaCDELGQTAVIVTHDPFVAAHADKVVFLLDG 219
Cdd:NF038007 161 ALLLADEPTGNLDSKNARAVLQQLKY-INQKGTTIIMVTHSDEASTYGNRIINMKDG 216
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
3-222 |
1.07e-61 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 194.51 E-value: 1.07e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 3 IIEIEGLEKSFDigdSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALF 82
Cdd:COG3638 2 MLELRNLSKRYP---GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 83 RRhKIGFIFQQFNLIPVFNAEENV---------GLPLLLDNVSQK-KATvtANRLLELVGLKGKEKHLPAQLSGGQQQRV 152
Cdd:COG3638 79 RR-RIGMIFQQFNLVPRLSVLTNVlagrlgrtsTWRSLLGLFPPEdRER--ALEALERVGLADKAYQRADQLSGGQQQRV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446943912 153 AIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVA-AHADKVVFLLDGEVI 222
Cdd:COG3638 156 AIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLArRYADRIIGLRDGRVV 226
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
3-220 |
1.43e-61 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 192.85 E-value: 1.43e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 3 IIEIEGLEKSFDIGdskVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALF 82
Cdd:TIGR02673 1 MIEFHNVSKAYPGG---VAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 83 RRHkIGFIFQQFNLIPVFNAEENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEP 162
Cdd:TIGR02673 78 RRR-IGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446943912 163 AIILADEPTGALDSENSKNIIAALRNACDeLGQTAVIVTHDP-FVAAHADKVVFLLDGE 220
Cdd:TIGR02673 157 PLLLADEPTGNLDPDLSERILDLLKRLNK-RGTTVIVATHDLsLVDRVAHRVIILDDGR 214
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-224 |
4.73e-61 |
|
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: 192.50 E-value: 4.73e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 2 NIIEIEGLEKSFDigdsKVKILKDINLQIQKGDFVCIMGASGSGKttllqllggldipSV-------------GSIRVDG 68
Cdd:COG1127 4 PMIEVRNLTKSFG----DRVVLDGVSLDVPRGEILAIIGGSGSGK-------------SVllkliigllrpdsGEILVDG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 69 TEISTLKEKELALFRRhKIGFIFQQ---FNLIPVFnaeENVGLPLL-LDNVSQKKATVTANRLLELVGLKGKEKHLPAQL 144
Cdd:COG1127 67 QDITGLSEKELYELRR-RIGMLFQGgalFDSLTVF---ENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSEL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 145 SGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHD-PFVAAHADKVVFLLDGEVIH 223
Cdd:COG1127 143 SGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDlDSAFAIADRVAVLADGKIIA 222
|
.
gi 446943912 224 E 224
Cdd:COG1127 223 E 223
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-222 |
1.99e-60 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 194.25 E-value: 1.99e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFDIGDSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALFR 83
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 RhKIGFIFQQFNLIPVFNAEENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPA 163
Cdd:PRK11153 82 R-QIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 164 IILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVAAH-ADKVVFLLDGEVI 222
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRiCDRVAVIDAGRLV 220
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-221 |
2.68e-60 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 189.66 E-value: 2.68e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFdiGDSKVkiLKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEIsTLKEKELALFR 83
Cdd:cd03262 1 IEIKNLHKSF--GDFHV--LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL-TDDKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 RhKIGFIFQQFNLIPVFNAEENVGL-PLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEP 162
Cdd:cd03262 76 Q-KVGMVFQQFNLFPHLTVLENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 163 AIILADEPTGALDSENSKNIIAALRNACDElGQTAVIVTHD-PFVAAHADKVVFLLDGEV 221
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEmGFAREVADRVIFMDDGRI 213
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-226 |
4.29e-60 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 189.64 E-value: 4.29e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 3 IIEIEGLEKSFDIGDSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALf 82
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKI- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 83 RRHKIGFIFQ--QFNLIPVFNAEENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHL---PAQLSGGQQQRVAIARA 157
Cdd:cd03257 80 RRKEIQMVFQdpMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLnryPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 158 FANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVAAH-ADKVVFLLDGEVIhEHA 226
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKiADRVAVMYAGKIV-EEG 228
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-216 |
5.19e-60 |
|
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: 189.22 E-value: 5.19e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFDIGDSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTlkekelalfR 83
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG---------P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 RHKIGFIFQQFNLIPVFNAEENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPA 163
Cdd:cd03293 72 GPDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446943912 164 IILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVAAH-ADKVVFL 216
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFlADRVVVL 205
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-222 |
6.94e-59 |
|
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: 187.00 E-value: 6.94e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFDigdSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALFR 83
Cdd:cd03256 1 IEVENLSKTYP---NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 RHkIGFIFQQFNLIPVFNAEENVGLPLL--------LDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIA 155
Cdd:cd03256 78 RQ-IGMIFQQFNLIERLSVLENVLSGRLgrrstwrsLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446943912 156 RAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDP-FVAAHADKVVFLLDGEVI 222
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVdLAREYADRIVGLKDGRIV 224
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-216 |
1.04e-57 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 182.82 E-value: 1.04e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 6 IEGLEKSFdiGDSKvkILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALFRRH 85
Cdd:TIGR03608 1 LKNISKKF--GDKV--ILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 86 KIGFIFQQFNLIPVFNAEENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAII 165
Cdd:TIGR03608 77 KLGYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446943912 166 LADEPTGALDSENSKNIIAALRNACDElGQTAVIVTHDPFVAAHADKVVFL 216
Cdd:TIGR03608 157 LADEPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDPEVAKQADRVIEL 206
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
3-219 |
1.06e-57 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 183.30 E-value: 1.06e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 3 IIEIEGLEKSFDIGDSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALF 82
Cdd:TIGR02982 1 VISIRNLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 83 RRHkIGFIFQQFNLIPVFNAEENVGLPL-LLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANE 161
Cdd:TIGR02982 81 RRR-IGYIFQAHNLLGFLTARQNVQMALeLQPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHH 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446943912 162 PAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVAAHADKVVFLLDG 219
Cdd:TIGR02982 160 PKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDNRILDVADRILQMEDG 217
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-222 |
6.92e-57 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 185.30 E-value: 6.92e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 1 MNIIEIEGLEKSFDigdsKVKILKDINLQIQKGDFVCIMGASGSGK----------TTllqllggldiPSVGSIRVDGTE 70
Cdd:COG3842 3 MPALELENVSKRYG----DVTALDDVSLSIEPGEFVALLGPSGCGKttllrmiagfET----------PDSGRILLDGRD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 71 IStlkekELALFRRHkIGFIFQQFNLIPVFNAEENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQ 150
Cdd:COG3842 69 VT-----GLPPEKRN-VGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446943912 151 RVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVA-AHADKVVFLLDGEVI 222
Cdd:COG3842 143 RVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEAlALADRIAVMNDGRIE 215
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-222 |
1.31e-56 |
|
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: 181.16 E-value: 1.31e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFDigdSKVkILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALFR 83
Cdd:cd03261 1 IELRGLTKSFG---GRT-VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 RhKIGFIFQQ---FNLIPVFnaeENVGLPL-----LLDNVSQKKATVTanrlLELVGLKGKEKHLPAQLSGGQQQRVAIA 155
Cdd:cd03261 77 R-RMGMLFQSgalFDSLTVF---ENVAFPLrehtrLSEEEIREIVLEK----LEAVGLRGAEDLYPAELSGGMKKRVALA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446943912 156 RAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHD-PFVAAHADKVVFLLDGEVI 222
Cdd:cd03261 149 RALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDlDTAFAIADRIAVLYDGKIV 216
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-222 |
2.51e-56 |
|
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: 179.64 E-value: 2.51e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFDigdsKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEkelalfR 83
Cdd:cd03259 1 LELKGLSKTYG----SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPP------E 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 RHKIGFIFQQFNLIPVFNAEENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPA 163
Cdd:cd03259 71 RRNIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 164 IILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVA-AHADKVVFLLDGEVI 222
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEAlALADRIAVMNEGRIV 210
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-224 |
3.00e-56 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 179.97 E-value: 3.00e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 2 NIIEIEGLEKSFDIGDSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELAL 81
Cdd:PRK10584 5 NIVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 82 FRRHKIGFIFQQFNLIPVFNAEENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANE 161
Cdd:PRK10584 85 LRAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGR 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446943912 162 PAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVAAHADKVVFLLDGEVIHE 224
Cdd:PRK10584 165 PDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-221 |
1.46e-55 |
|
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: 177.60 E-value: 1.46e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFDIGdskVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALFR 83
Cdd:cd03292 1 IEFINVTKTYPNG---TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 RHkIGFIFQQFNLIPVFNAEENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPA 163
Cdd:cd03292 78 RK-IGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446943912 164 IILADEPTGALDSENSkNIIAALRNACDELGQTAVIVTHDP-FVAAHADKVVFLLDGEV 221
Cdd:cd03292 157 ILIADEPTGNLDPDTT-WEIMNLLKKINKAGTTVVVATHAKeLVDTTRHRVIALERGKL 214
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-229 |
2.81e-55 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 177.88 E-value: 2.81e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 3 IIEIEGLEKSFDIGdskVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALF 82
Cdd:TIGR02315 1 MLEVENLSKVYPNG---KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 83 RRHkIGFIFQQFNLIPVFNAEENV---------GLPLLLDNVSqKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVA 153
Cdd:TIGR02315 78 RRR-IGMIFQHYNLIERLTVLENVlhgrlgykpTWRSLLGRFS-EEDKERALSALERVGLADKAYQRADQLSGGQQQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446943912 154 IARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVA-AHADKVVFLLDGEVIHEHAESK 229
Cdd:TIGR02315 156 IARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAkKYADRIVGLKAGEIVFDGAPSE 232
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-222 |
3.46e-53 |
|
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: 179.71 E-value: 3.46e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 3 IIEIEGLEKSFDI-GDSKVKILKDINLQIQKGDFVCIMGASGSGK----------TTllqllggldiPSVGSIRVDGTEI 71
Cdd:COG1123 260 LLEVRNLSKRYPVrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKstlarlllglLR----------PTSGSILFDGKDL 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 72 STLKEKELALFRRHkIGFIFQ----QFNliPVFNAEENVGLPL-LLDNVSQKKATVTANRLLELVGLkgKEKHL---PAQ 143
Cdd:COG1123 330 TKLSRRSLRELRRR-VQMVFQdpysSLN--PRMTVGDIIAEPLrLHGLLSRAERRERVAELLERVGL--PPDLAdryPHE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 144 LSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHD-PFVAAHADKVVFLLDGEVI 222
Cdd:COG1123 405 LSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDlAVVRYIADRVAVMYDGRIV 484
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-222 |
2.99e-50 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 172.01 E-value: 2.99e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 3 IIEIEGLEKSFDIGDskVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLdIPSV----GSIRVDGTEISTLKEKE 78
Cdd:COG1123 4 LLEVRDLSVRYPGGD--VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGL-LPHGgrisGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 79 lalfRRHKIGFIFQ----QFNLIPVfnaEENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAI 154
Cdd:COG1123 81 ----RGRRIGMVFQdpmtQLNPVTV---GDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446943912 155 ARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVAAH-ADKVVFLLDGEVI 222
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEiADRVVVMDDGRIV 222
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-214 |
3.04e-50 |
|
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: 167.15 E-value: 3.04e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 3 IIEIEGLEKSFDIGDSKVKILKDINLQIQKGDFVCIMGASGSGKttllqllggldipSV----------------GSIRV 66
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGK-------------STlarailgllpppgitsGEILF 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 67 DGTEISTLKEKELALFRRHKIGFIFQQ----FNliPVFNAEENVGLPLLL-DNVSQKKATVTANRLLELVGLKGKEKHL- 140
Cdd:COG0444 68 DGEDLLKLSEKELRKIRGREIQMIFQDpmtsLN--PVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPDPERRLd 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446943912 141 --PAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVAAH-ADKVV 214
Cdd:COG0444 146 ryPHELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEiADRVA 222
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
4-222 |
3.93e-50 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 165.51 E-value: 3.93e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSF-----------DIGDSKVKILK---------DINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGS 63
Cdd:cd03294 1 IKIKGLYKIFgknpqkafkllAKGKSKEEILKktgqtvgvnDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 64 IRVDGTEISTLKEKELALFRRHKIGFIFQQFNLIPVFNAEENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQ 143
Cdd:cd03294 81 VLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 144 LSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVAAH-ADKVVFLLDGEVI 222
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRlGDRIAIMKDGRLV 240
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
9-224 |
6.61e-50 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 163.83 E-value: 6.61e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 9 LEKSFDIGDSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALFRRHKIG 88
Cdd:PRK11629 11 LCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKLG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 89 FIFQQFNLIPVFNAEENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILAD 168
Cdd:PRK11629 91 FIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLAD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446943912 169 EPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVAAHADKVVFLLDGEVIHE 224
Cdd:PRK11629 171 EPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAE 226
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-229 |
8.42e-50 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 164.15 E-value: 8.42e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 1 MNIIEIEGLEKSFDiGDSkvkILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLK--EKE 78
Cdd:PRK11264 1 MSAIEVKNLVKKFH-GQT---VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARslSQQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 79 LALFR--RHKIGFIFQQFNLIPVFNAEENV--GlPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAI 154
Cdd:PRK11264 77 KGLIRqlRQHVGFVFQNFNLFPHRTVLENIieG-PVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446943912 155 ARAFANEPAIILADEPTGALDSENSKNIIAALRNACDElGQTAVIVTHD-PFVAAHADKVVFlLDGEVIHEHAESK 229
Cdd:PRK11264 156 ARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEmSFARDVADRAIF-MDQGRIVEQGPAK 229
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-220 |
1.68e-49 |
|
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: 161.87 E-value: 1.68e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 5 EIEGLekSFDIGDSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfrR 84
Cdd:cd03225 1 ELKNL--SFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKEL----R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 85 HKIGFIFQ----QFnlipvFNA--EENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAF 158
Cdd:cd03225 75 RKVGLVFQnpddQF-----FGPtvEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446943912 159 ANEPAIILADEPTGALDSENSKNIIAALRNACDElGQTAVIVTHDP-FVAAHADKVVFLLDGE 220
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLdLLLELADRVIVLEDGK 211
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-220 |
3.09e-49 |
|
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: 160.05 E-value: 3.09e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFdigdSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLkEKELALFR 83
Cdd:cd03229 1 LELKNVSKRY----GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDL-EDELPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 RhKIGFIFQQFNLIPVFNAEENVGLPllldnvsqkkatvtanrllelvglkgkekhlpaqLSGGQQQRVAIARAFANEPA 163
Cdd:cd03229 76 R-RIGMVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446943912 164 IILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVAAH-ADKVVFLLDGE 220
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
4-221 |
3.35e-49 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 162.66 E-value: 3.35e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFdiGDSKVkiLKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLK-------- 75
Cdd:COG4598 9 LEVRDLHKSF--GDLEV--LKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPdrdgelvp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 76 --EKELALFRRhKIGFIFQQFNLIPVFNAEENVGL-PLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRV 152
Cdd:COG4598 85 adRRQLQRIRT-RLGMVFQSFNLWSHMTVLENVIEaPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 153 AIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDElGQTAVIVTHDPFVAAH-ADKVVFLLDGEV 221
Cdd:COG4598 164 AIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDvSSHVVFLHQGRI 232
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-222 |
1.26e-48 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 161.12 E-value: 1.26e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFDIGDSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKElalfR 83
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKA----F 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 RHKIGFIFQQ----FNliPVFNAEENVGLPLLLDNVSQKKATVTanRLLELVGLKGKEKH-LPAQLSGGQQQRVAIARAF 158
Cdd:COG1124 78 RRRVQMVFQDpyasLH--PRHTVDRILAEPLRIHGLPDREERIA--ELLEQVGLPPSFLDrYPHQLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446943912 159 ANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVAAH-ADKVVFLLDGEVI 222
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIV 218
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-229 |
7.22e-48 |
|
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: 158.50 E-value: 7.22e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFDigdsKVKILKDINLQIQKGDFVCIMGASGSGK-----TTLLQLLGGLDIPSVGSIRVDGTEISTLKEKE 78
Cdd:cd03260 1 IELRDLNVYYG----DKHALKDISLDIPKGEITALIGPSGCGKstllrLLNRLNDLIPGAPDEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 79 LALFRRhkIGFIFQQFNLIPvFNAEENVGLPLLLDNVSQKKAT-VTANRLLELVGLKGKEK-HLPA-QLSGGQQQRVAIA 155
Cdd:cd03260 77 LELRRR--VGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELdERVEEALRKAALWDEVKdRLHAlGLSGGQQQRLCLA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446943912 156 RAFANEPAIILADEPTGALDSENSKNIIAALRNACDELgqTAVIVTHDPFVAAH-ADKVVFLLDGEVIhEHAESK 229
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARvADRTAFLLNGRLV-EFGPTE 225
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-222 |
6.10e-47 |
|
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: 156.31 E-value: 6.10e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFdiGDSKvKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfr 83
Cdd:cd03295 1 IEFENVTKRY--GGGK-KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVEL---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 RHKIGFIFQQFNLIPVFNAEENVGLPLLLDNVSQKKATVTANRLLELVGLKGKE--KHLPAQLSGGQQQRVAIARAFANE 161
Cdd:cd03295 74 RRKIGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEfaDRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446943912 162 PAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVAAH-ADKVVFLLDGEVI 222
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRlADRIAIMKNGEIV 215
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
3-224 |
7.84e-47 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 156.02 E-value: 7.84e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 3 IIEIEGLEKSFdiGDSKVkiLKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALf 82
Cdd:PRK09493 1 MIEFKNVSKHF--GPTQV--LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLI- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 83 rRHKIGFIFQQFNLIPVFNAEENVGL-PLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANE 161
Cdd:PRK09493 76 -RQEAGMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446943912 162 PAIILADEPTGALDSENSKNIIAALRNACDElGQTAVIVTHD-PFVAAHADKVVFLLDGEVIHE 224
Cdd:PRK09493 155 PKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEiGFAEKVASRLIFIDKGRIAED 217
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-221 |
8.97e-47 |
|
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: 155.86 E-value: 8.97e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFDigdsKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEIStlkekELALFR 83
Cdd:cd03300 1 IELENVSKFYG----GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT-----NLPPHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 RHkIGFIFQQFNLIPVFNAEENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPA 163
Cdd:cd03300 72 RP-VNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446943912 164 IILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVA-AHADKVVFLLDGEV 221
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEAlTMSDRIAVMNKGKI 209
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-224 |
2.20e-46 |
|
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: 154.41 E-value: 2.20e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLekSFDIGDSKvKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfr 83
Cdd:COG1122 1 IELENL--SFSYPGGT-PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLREL---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 RHKIGFIFQ----QFnlipvFNA--EENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARA 157
Cdd:COG1122 74 RRKVGLVFQnpddQL-----FAPtvEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446943912 158 FANEPAIILADEPTGALDSENSKNIIAALRNACDElGQTAVIVTHDP-FVAAHADKVVFLLDGEVIHE 224
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLdLVAELADRVIVLDDGRIVAD 215
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
4-222 |
4.22e-46 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 154.19 E-value: 4.22e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFdiGDSKVkiLKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKekelalFR 83
Cdd:TIGR00968 1 IEIANISKRF--GSFQA--LDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVH------AR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 RHKIGFIFQQFNLIPVFNAEENV--GLPLLLDNVSQKKATVtaNRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANE 161
Cdd:TIGR00968 71 DRKIGFVFQHYALFKHLTVRDNIafGLEIRKHPKAKIKARV--EELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446943912 162 PAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVAAH-ADKVVFLLDGEVI 222
Cdd:TIGR00968 149 PQVLLLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEvADRIVVMSNGKIE 210
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-222 |
2.74e-44 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 152.61 E-value: 2.74e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFDigdsKVKILKDINLQIQKGDFVCIMGASGSGKttllqllgglDIPSVGSIRVDGTEISTlkekELALFR 83
Cdd:COG1118 3 IEVRNISKRFG----SFTLLDDVSLEIASGELVALLGPSGSGKttllriiaglETPDSGRIVLNGRDLFT----NLPPRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 RHkIGFIFQQFNLIPVFNAEENV--GLPLLLDNVSQKKATVTanRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANE 161
Cdd:COG1118 75 RR-VGFVFQHYALFPHMTVAENIafGLRVRPPSKAEIRARVE--ELLELVQLEGLADRYPSQLSGGQRQRVALARALAVE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446943912 162 PAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVAAH-ADKVVFLLDGEVI 222
Cdd:COG1118 152 PEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALElADRVVVMNQGRIE 213
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
4-221 |
4.45e-44 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 152.11 E-value: 4.45e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFDigdsKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKelalfr 83
Cdd:TIGR03265 5 LSIDNIRKRFG----AFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQ------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 RHKIGFIFQQFNLIPVFNAEENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPA 163
Cdd:TIGR03265 75 KRDYGIVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446943912 164 IILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVA-AHADKVVFLLDGEV 221
Cdd:TIGR03265 155 LLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEAlSMADRIVVMNHGVI 213
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
4-222 |
6.80e-44 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 150.24 E-value: 6.80e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFdiGDSKVkILKDINLQIQKGDFVCIMGASGSGKttllqllggldiPSVGSIRVDGTEISTLKEKELalfR 83
Cdd:COG1125 2 IEFENVTKRY--PDGTV-AVDDLSLTIPAGEFTVLVGPSGCGKtttlrminrliePTSGRILIDGEDIRDLDPVEL---R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 RHkIGFIFQQFNLIPVFNAEENVGL-PLLLdNVSQKKATVTANRLLELVGLKGKE--KHLPAQLSGGQQQRVAIARAFAN 160
Cdd:COG1125 76 RR-IGYVIQQIGLFPHMTVAENIATvPRLL-GWDKERIRARVDELLELVGLDPEEyrDRYPHELSGGQQQRVGVARALAA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446943912 161 EPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVAAH-ADKVVFLLDGEVI 222
Cdd:COG1125 154 DPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKlGDRIAVMREGRIV 216
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-221 |
1.75e-43 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 146.50 E-value: 1.75e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLekSFDIGDSKvkILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfr 83
Cdd:COG4619 1 LELEGL--SFRVGGKP--ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEW---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 RHKIGFIFQQFNLIP--VfnaEENVGLPLLLDNvsQKKATVTANRLLELVGLKGKEKHLPA-QLSGGQQQRVAIARAFAN 160
Cdd:COG4619 73 RRQVAYVPQEPALWGgtV---RDNLPFPFQLRE--RKFDRERALELLERLGLPPDILDKPVeRLSGGERQRLALIRALLL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446943912 161 EPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVAAH-ADKVVFLLDGEV 221
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-222 |
6.32e-43 |
|
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: 145.94 E-value: 6.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFDigdsKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKekelalFR 83
Cdd:cd03296 3 IEVRNVSKRFG----DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP------VQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 RHKIGFIFQQFNLIPVFNAEENVGLPLLLDNVSQK--KATVTA--NRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFA 159
Cdd:cd03296 73 ERNVGFVFQHYALFRHMTVFDNVAFGLRVKPRSERppEAEIRAkvHELLKLVQLDWLADRYPAQLSGGQRQRVALARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446943912 160 NEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVAAH-ADKVVFLLDGEVI 222
Cdd:cd03296 153 VEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEvADRVVVMNKGRIE 216
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
4-222 |
3.19e-42 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 144.39 E-value: 3.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFdigdSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEIS---TLKEKELA 80
Cdd:COG4161 3 IQLKNINCFY----GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsqKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 81 LFRRhKIGFIFQQFNLIPVFNAEEN-VGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFA 159
Cdd:COG4161 79 LLRQ-KVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446943912 160 NEPAIILADEPTGALDSENSKNIIAALRnacdELGQTA---VIVTHDPFVAAH-ADKVVFLLDGEVI 222
Cdd:COG4161 158 MEPQVLLFDEPTAALDPEITAQVVEIIR----ELSQTGitqVIVTHEVEFARKvASQVVYMEKGRII 220
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-224 |
4.16e-42 |
|
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: 144.42 E-value: 4.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 3 IIEIEGLekSFDIGDskVKILKDINLQIQKGDFVCIMGASGSGK---------TTLlqllggldiPSVGSIRVDGTEIST 73
Cdd:COG1120 1 MLEAENL--SVGYGG--RPVLDDVSLSLPPGEVTALLGPNGSGKstllralagLLK---------PSSGEVLLDGRDLAS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 74 LKEKELAlfRRhkIGFIFQQFNLIPVFNAEENVGL---PLL--LDNVSQKKATVtANRLLELVGLKGKEKHLPAQLSGGQ 148
Cdd:COG1120 68 LSRRELA--RR--IAYVPQEPPAPFGLTVRELVALgryPHLglFGRPSAEDREA-VEEALERTGLEHLADRPVDELSGGE 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446943912 149 QQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDP-FVAAHADKVVFLLDGEVIHE 224
Cdd:COG1120 143 RQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLnLAARYADRLVLLKDGRIVAQ 219
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-221 |
5.40e-42 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 146.76 E-value: 5.40e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 1 MNIIEIEGLEKSFDigdsKVKILKDINLQIQKGDFVCIMGASGSGKttllqllgglDIPSVGSIRVDGTEISTLKEKEla 80
Cdd:COG3839 1 MASLELENVSKSYG----GVEALKDIDLDIEDGEFLVLLGPSGCGKstllrmiaglEDPTSGEILIGGRDVTDLPPKD-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 81 lfRRhkIGFIFQQFNLIPVFNAEENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFAN 160
Cdd:COG3839 75 --RN--IAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 161 EPAIILADEPTGALDsenskniiAALRNA--------CDELGQTAVIVTHDPFVA-AHADKVVFLLDGEV 221
Cdd:COG3839 151 EPKVFLLDEPLSNLD--------AKLRVEmraeikrlHRRLGTTTIYVTHDQVEAmTLADRIAVMNDGRI 212
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-222 |
1.33e-41 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 142.51 E-value: 1.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFDigdsKVKILKDINLQIQKGDFVCIMGASGSGK----------TTllqllggldiPSVGSIRVDGTEIST 73
Cdd:COG1131 1 IEVRGLTKRYG----DKTALDGVSLTVEPGEIFGLLGPNGAGKtttirmllglLR----------PTSGEVRVLGEDVAR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 74 LKEKelalfRRHKIGFIFQQFNLIPVFNAEENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVA 153
Cdd:COG1131 67 DPAE-----VRRRIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 154 IARAFANEPAIILADEPTGALDSENSKNIIAALRNACDElGQTAVIVTHDPFVAAH-ADKVVFLLDGEVI 222
Cdd:COG1131 142 LALALLHDPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERlCDRVAIIDKGRIV 210
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-227 |
2.20e-41 |
|
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: 148.68 E-value: 2.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 1 MNIIEIEGLEKSFDIGDSKVKILKDINLQIQKGDFVCIMGASGSGKttllqllggldipSV-----------------GS 63
Cdd:COG4172 4 MPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGK-------------SVtalsilrllpdpaahpsGS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 64 IRVDGTEISTLKEKELALFRRHKIGFIFQQ----FNliPVFNAEENVGLPLLL-DNVSQKKATVTANRLLELVGLKGKEK 138
Cdd:COG4172 71 ILFDGQDLLGLSERELRRIRGNRIAMIFQEpmtsLN--PLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDPER 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 139 HL---PAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHD-PFVAAHADKVV 214
Cdd:COG4172 149 RLdayPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDlGVVRRFADRVA 228
|
250
....*....|...
gi 446943912 215 FLLDGEVIhEHAE 227
Cdd:COG4172 229 VMRQGEIV-EQGP 240
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
4-221 |
2.59e-41 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 144.84 E-value: 2.59e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFDigdsKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKElalfr 83
Cdd:PRK10851 3 IEIANIKKSFG----RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 rHKIGFIFQQFNLIPVFNAEENV--GLPLL----LDNVSQKKATVTanRLLELVGLKGKEKHLPAQLSGGQQQRVAIARA 157
Cdd:PRK10851 74 -RKVGFVFQHYALFRHMTVFDNIafGLTVLprreRPNAAAIKAKVT--QLLEMVQLAHLADRYPAQLSGGQKQRVALARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446943912 158 FANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVAAH-ADKVVFLLDGEV 221
Cdd:PRK10851 151 LAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEvADRVVVMSQGNI 215
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-224 |
6.51e-41 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 141.80 E-value: 6.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLekSFDIGDSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGteISTLKEKELALFR 83
Cdd:TIGR04520 1 IEVENV--SFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENLWEIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 RhKIGFIFQ----QFNLIPVfnaEENV--GLPLLldNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARA 157
Cdd:TIGR04520 77 K-KVGMVFQnpdnQFVGATV---EDDVafGLENL--GVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446943912 158 FANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVAAHADKVVFLLDGEVIHE 224
Cdd:TIGR04520 151 LAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAE 217
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-220 |
1.09e-40 |
|
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: 137.90 E-value: 1.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLekSFDIGDSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfr 83
Cdd:cd03228 1 IEFKNV--SFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESL---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 RHKIGFIFQQFNLipvFNAeenvglpLLLDNVsqkkatvtanrllelvglkgkekhlpaqLSGGQQQRVAIARAFANEPA 163
Cdd:cd03228 75 RKNIAYVPQDPFL---FSG-------TIRENI----------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446943912 164 IILADEPTGALDSENSKNIIAALRNACDelGQTAVIVTHDPFVAAHADKVVFLLDGE 220
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-203 |
2.34e-40 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 140.00 E-value: 2.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 1 MNIIEIEGLEKSFDIGDSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKEla 80
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 81 lfrrhkiGFIFQQFNLIPVFNAEENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFAN 160
Cdd:COG4525 79 -------GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446943912 161 EPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHD 203
Cdd:COG4525 152 DPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS 194
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
4-228 |
2.42e-39 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 136.68 E-value: 2.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFdiGDSKVkiLKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEI---STLKEKELA 80
Cdd:PRK11124 3 IQLNGINCFY--GAHQA--LFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 81 LFRRhKIGFIFQQFNLIPVFNAEEN-VGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFA 159
Cdd:PRK11124 79 ELRR-NVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446943912 160 NEPAIILADEPTGALDSENSKNIIAALRnacdELGQTA---VIVTHDPFVAAH-ADKVVFLLDGEVIhEHAES 228
Cdd:PRK11124 158 MEPQVLLFDEPTAALDPEITAQIVSIIR----ELAETGitqVIVTHEVEVARKtASRVVYMENGHIV-EQGDA 225
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
21-223 |
3.01e-38 |
|
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: 133.19 E-value: 3.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 21 KILKDINLQIQ---KGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTeisTLKEKELALF---RRHKIGFIFQQF 94
Cdd:cd03297 8 KRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGT---VLFDSRKKINlppQQRKIGLVFQQY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 95 NLIPVFNAEENV--GLPLLldnvSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTG 172
Cdd:cd03297 85 ALFPHLNVRENLafGLKRK----RNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446943912 173 ALDSENSKNIIAALRNACDELGQTAVIVTHDPFVAAH-ADKVVFLLDGEVIH 223
Cdd:cd03297 161 ALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQY 212
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-221 |
3.58e-38 |
|
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: 132.76 E-value: 3.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFDigdsKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKElalfr 83
Cdd:cd03301 1 VELENVTKRFG----NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 rHKIGFIFQQFNLIPVFNAEENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPA 163
Cdd:cd03301 72 -RDIAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446943912 164 IILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVA-AHADKVVFLLDGEV 221
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAmTMADRIAVMNDGQI 209
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-227 |
3.62e-38 |
|
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: 141.51 E-value: 3.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLekSFDIGDSKVKILKDINLQIQKGDFVCIMGASGSGK-----------TtllqllggldiPSVGSIRVDGTEIS 72
Cdd:COG2274 474 IELENV--SFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKstllklllglyE-----------PTSGRILIDGIDLR 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 73 TLkekELALFRRHkIGFIFQQFNLipvFNAEenvglplLLDNVSQKKATVTANRL---LELVGLKGKEKHLP-------- 141
Cdd:COG2274 541 QI---DPASLRRQ-IGVVLQDVFL---FSGT-------IRENITLGDPDATDEEIieaARLAGLHDFIEALPmgydtvvg 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 142 ---AQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDelGQTAVIVTHDPFVAAHADKVVFLLD 218
Cdd:COG2274 607 eggSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRLADRIIVLDK 684
|
250
....*....|.
gi 446943912 219 GEVIHE--HAE 227
Cdd:COG2274 685 GRIVEDgtHEE 695
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-226 |
3.87e-38 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 133.68 E-value: 3.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 1 MNIIEIEGLekSFDIGDskVKILKDINLQIQKGDFVCIMGASGSGKttllqllggldiPSVGSIRVDGTEISTlkekela 80
Cdd:COG1121 4 MPAIELENL--TVSYGG--RPVLEDVSLTIPPGEFVAIVGPNGAGKstllkailgllpPTSGTVRLFGKPPRR------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 81 lfRRHKIGFIFQQFNLIPVF--NAEENVGLPL-----LLDNVSQKKATVtANRLLELVGLKGKEKHLPAQLSGGQQQRVA 153
Cdd:COG1121 73 --ARRRIGYVPQRAEVDWDFpiTVRDVVLMGRygrrgLFRRPSRADREA-VDEALERVGLEDLADRPIGELSGGQQQRVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446943912 154 IARAFANEPAIILADEPTGALDSENSKNIIAALRNACDElGQTAVIVTHDP-FVAAHADKVVfLLDGEVIHEHA 226
Cdd:COG1121 150 LARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLgAVREYFDRVL-LLNRGLVAHGP 221
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-224 |
1.95e-37 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 129.86 E-value: 1.95e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 5 EIEGLEKSFDigdsKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALfrr 84
Cdd:cd03214 1 EVENLSVGYG----GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELAR--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 85 hKIGFIFQqfnlipvfnaeenvglpllldnvsqkkatvtanrLLELVGLKG-KEKHLpAQLSGGQQQRVAIARAFANEPA 163
Cdd:cd03214 74 -KIAYVPQ----------------------------------ALELLGLAHlADRPF-NELSGGERQRVLLARALAQEPP 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446943912 164 IILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDP-FVAAHADKVVFLLDGEVIHE 224
Cdd:cd03214 118 ILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLnLAARYADRVILLKDGRIVAQ 179
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
21-222 |
6.18e-37 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 131.42 E-value: 6.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 21 KILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALFRRhKIGFIFQQfnliP-- 98
Cdd:TIGR04521 19 KALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLRK-KVGLVFQF----Peh 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 99 -VFnaEENV------GlPLLLdNVSQKKATVTANRLLELVGLKG--KEKHlPAQLSGGQQQRVAIARAFANEPAIILADE 169
Cdd:TIGR04521 94 qLF--EETVykdiafG-PKNL-GLSEEEAEERVKEALELVGLDEeyLERS-PFELSGGQMRRVAIAGVLAMEPEVLILDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446943912 170 PTGALDSENSKNIIAALRNACDELGQTAVIVTHD-PFVAAHADKVVFLLDGEVI 222
Cdd:TIGR04521 169 PTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSmEDVAEYADRVIVMHKGKIV 222
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
38-221 |
7.73e-37 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 132.62 E-value: 7.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 38 IMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEIStlkekELALFRRHkIGFIFQQFNLIPVFNAEENVGLPLLLDNVSQ 117
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVT-----NVPPHLRH-INMVFQSYALFPHMTVEENVAFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 118 KKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTA 197
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITF 154
|
170 180
....*....|....*....|....*
gi 446943912 198 VIVTHDPFVA-AHADKVVFLLDGEV 221
Cdd:TIGR01187 155 VFVTHDQEEAmTMSDRIAIMRKGKI 179
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
23-219 |
1.59e-36 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 129.12 E-value: 1.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 23 LKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELAlfrrhkigfIFQQFNLIPVFNA 102
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV---------VFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 103 EENVGLPLllDNV------SQKKATVTANrlLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGALDS 176
Cdd:TIGR01184 72 RENIALAV--DRVlpdlskSERRAIVEEH--IALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446943912 177 ENSKNIIAALRNACDELGQTAVIVTHDPFVAAH-ADKVVFLLDG 219
Cdd:TIGR01184 148 LTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLlSDRVVMLTNG 191
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-219 |
2.35e-36 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 128.71 E-value: 2.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 1 MN-IIEIEGLEKSFDI---GDSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVD----GTEIS 72
Cdd:COG4778 1 MTtLLEVENLSKTFTLhlqGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 73 TLKEKELALFRRHKIGFIFQQFNLIPVFNAEENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHL-PAQLSGGQQQR 151
Cdd:COG4778 81 QASPREILALRRRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERLWDLpPATFSGGEQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 152 VAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDElGqTAVI-VTHDP-FVAAHADKVVFLLDG 219
Cdd:COG4778 161 VNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-G-TAIIgIFHDEeVREAVADRVVDVTPF 228
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-224 |
2.36e-36 |
|
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: 129.21 E-value: 2.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFDigdsKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKelalfR 83
Cdd:COG4555 2 IEVENLSKKYG----KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-----A 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 RHKIGFIFQQFNLIPVFNAEENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPA 163
Cdd:COG4555 73 RRQIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446943912 164 IILADEPTGALDSENSKNIIAALRNACDElGQTAVIVTHDPFVAAH-ADKVVFLLDGEVIHE 224
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQ 213
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-227 |
6.45e-36 |
|
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: 134.12 E-value: 6.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLekSFDIGDSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfr 83
Cdd:COG4987 334 LELEDV--SFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDL---- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 RHKIGFIFQQfnlIPVFNA--EENvglpLLL--DNVSQKKATvtanRLLELVGLKGKEKHLP-----------AQLSGGQ 148
Cdd:COG4987 408 RRRIAVVPQR---PHLFDTtlREN----LRLarPDATDEELW----AALERVGLGDWLAALPdgldtwlgeggRRLSGGE 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 149 QQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDelGQTAVIVTHDPFVAAHADKVVFLLDGEVIHE--HA 226
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLERMDRILVLEDGRIVEQgtHE 554
|
.
gi 446943912 227 E 227
Cdd:COG4987 555 E 555
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-223 |
9.11e-36 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 127.45 E-value: 9.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKsfDIGDSKvkiLKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKelalfr 83
Cdd:cd03299 1 LKVENLSK--DWKEFK---LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 RHKIGFIFQQFNLIPVFNAEENV--GLPLLLDNVSQKKAtvtanRLLELVGLKGKEkHL----PAQLSGGQQQRVAIARA 157
Cdd:cd03299 70 KRDISYVPQNYALFPHMTVYKNIayGLKKRKVDKKEIER-----KVLEIAEMLGID-HLlnrkPETLSGGEQQRVAIARA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446943912 158 FANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDpF--VAAHADKVVFLLDGEVIH 223
Cdd:cd03299 144 LVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHD-FeeAWALADKVAIMLNGKLIQ 210
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
26-222 |
9.26e-36 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 127.18 E-value: 9.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 26 INLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLkekelALFRRhKIGFIFQQFNLIPVFNAEEN 105
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTAL-----PPAER-PVSMLFQENNLFPHLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 106 VGL---PLLLDNVSQKKATVTAnrlLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNI 182
Cdd:COG3840 92 IGLglrPGLKLTAEQRAQVEQA---LERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEM 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446943912 183 IAALRNACDELGQTAVIVTHDPFVAAH-ADKVVFLLDGEVI 222
Cdd:COG3840 169 LDLVDELCRERGLTVLMVTHDPEDAARiADRVLLVADGRIA 209
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-222 |
2.31e-35 |
|
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: 125.72 E-value: 2.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 5 EIEGLEKSFDigdsKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTlkekelalfRR 84
Cdd:cd03235 1 EVEDLTVSYG----GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK---------ER 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 85 HKIGFIFQQFNLIPVF--NAEENVGLPLLLDNVSQKKATVT----ANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAF 158
Cdd:cd03235 68 KRIGYVPQRRSIDRDFpiSVRDVVLMGLYGHKGLFRRLSKAdkakVDEALERVGLSELADRQIGELSGGQQQRVLLARAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446943912 159 ANEPAIILADEPTGALDSENSKNIIAALRNACDElGQTAVIVTHDPF-VAAHADKVVfLLDGEVI 222
Cdd:cd03235 148 VQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGlVLEYFDRVL-LLNRTVV 210
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
23-225 |
3.36e-35 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 125.37 E-value: 3.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 23 LKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALFRRhKIGFIFQQFNLIPVFNA 102
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRR-QIGMIFQDHHLLMDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 103 EENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNI 182
Cdd:PRK10908 97 YDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446943912 183 IaALRNACDELGQTAVIVTHD-PFVAAHADKVVFLLDGEVIHEH 225
Cdd:PRK10908 177 L-RLFEEFNRVGVTVLMATHDiGLISRRSYRMLTLSDGHLHGGV 219
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-227 |
4.31e-35 |
|
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: 131.80 E-value: 4.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLekSFDIGDSKVkILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfr 83
Cdd:COG4988 337 IELEDV--SFSYPGGRP-ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASW---- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 RHKIGFIFQQfnliPV-FNA--EENVGLpllldnvSQKKATVTA-NRLLELVGLKGKEKHLP-----------AQLSGGQ 148
Cdd:COG4988 410 RRQIAWVPQN----PYlFAGtiRENLRL-------GRPDASDEElEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQ 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 149 QQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDelGQTAVIVTHDPFVAAHADKVVFLLDGEVIHE--HA 226
Cdd:COG4988 479 AQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQADRILVLDDGRIVEQgtHE 556
|
.
gi 446943912 227 E 227
Cdd:COG4988 557 E 557
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
25-222 |
6.36e-35 |
|
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: 124.53 E-value: 6.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 25 DINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKElalfrrHKIGFIFQQFNLIPVFNAEE 104
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD------RPVSMLFQENNLFAHLTVEQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 105 NVGL---P-LLLDNVSQKKATVTANRllelVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSK 180
Cdd:cd03298 90 NVGLglsPgLKLTAEDRQAIEVALAR----VGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446943912 181 NIIAALRNACDELGQTAVIVTHDPFVAAH-ADKVVFLLDGEVI 222
Cdd:cd03298 166 EMLDLVLDLHAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIA 208
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
21-224 |
8.35e-35 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 125.47 E-value: 8.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 21 KILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEK--ELALFRRH-------KIGFIF 91
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgQLKVADKNqlrllrtRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 92 QQFNLIPVFNAEENV-GLPLLLDNVSQKKATVTANRLLELVGLKGKEK-HLPAQLSGGQQQRVAIARAFANEPAIILADE 169
Cdd:PRK10619 99 QHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAQgKYPVHLSGGQQQRVSIARALAMEPEVLLFDE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446943912 170 PTGALDSENSKNIIAALRNACDElGQTAVIVTHDPFVAAH-ADKVVFLLDGEVIHE 224
Cdd:PRK10619 179 PTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHvSSHVIFLHQGKIEEE 233
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
23-171 |
2.14e-34 |
|
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: 121.22 E-value: 2.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 23 LKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKelalFRRHKIGFIFQQFNLIPVFNA 102
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERK----SLRKEIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446943912 103 EENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHL----PAQLSGGQQQRVAIARAFANEPAIILADEPT 171
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-224 |
2.53e-34 |
|
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: 122.69 E-value: 2.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFDigdsKVKILKDINLQIQKGDFVcIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKelalFR 83
Cdd:cd03264 1 LQLENLTKRYG----KKRALDGVSLTLGPGMYG-LLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK----LR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 RHkIGFIFQQFNLIPVFNAEENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPA 163
Cdd:cd03264 72 RR-IGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446943912 164 IILADEPTGALDSENSkniiAALRNACDELGQTAVIV--TH---DpfVAAHADKVVFLLDGEVIHE 224
Cdd:cd03264 151 ILIVDEPTAGLDPEER----IRFRNLLSELGEDRIVIlsTHiveD--VESLCNQVAVLNKGKLVFE 210
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-221 |
2.70e-34 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 126.99 E-value: 2.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 1 MNIIEIEGLEKSFDigdSKvKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKela 80
Cdd:PRK09452 12 SPLVELRGISKSFD---GK-EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 81 lfRRHkIGFIFQQFNLIPVFNAEENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFAN 160
Cdd:PRK09452 85 --NRH-VNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446943912 161 EPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVA-AHADKVVFLLDGEV 221
Cdd:PRK09452 162 KPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEAlTMSDRIVVMRDGRI 223
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-220 |
6.52e-34 |
|
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: 120.04 E-value: 6.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 5 EIEGLEKSFDigdsKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfrR 84
Cdd:cd00267 1 EIENLSFRYG----GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL----R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 85 HKIGFIFQqfnlipvfnaeenvglpllldnvsqkkatvtanrllelvglkgkekhlpaqLSGGQQQRVAIARAFANEPAI 164
Cdd:cd00267 73 RRIGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446943912 165 ILADEPTGALDSENSKNIIAALRNACDElGQTAVIVTHDP-FVAAHADKVVFLLDGE 220
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPeLAELAADRVIVLKDGK 157
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-224 |
7.63e-34 |
|
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: 122.16 E-value: 7.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFDigdsKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELAlfr 83
Cdd:cd03219 1 LEVRGLTKRFG----GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 RHKIGFIFQQFNLIPVFNAEENV--------GLPLLLDNVSQKKATVT--ANRLLELVGLKGKEKHLPAQLSGGQQQRVA 153
Cdd:cd03219 74 RLGIGRTFQIPRLFPELTVLENVmvaaqartGSGLLLARARREEREARerAEELLERVGLADLADRPAGELSYGQQRRLE 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446943912 154 IARAFANEPAIILADEPTGALDSENSKNIIAALRNACDElGQTAVIVTHD-PFVAAHADKVVFLLDGEVIHE 224
Cdd:cd03219 154 IARALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDmDVVMSLADRVTVLDQGRVIAE 224
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-229 |
1.58e-33 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 122.07 E-value: 1.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 3 IIEIEGLekSFDIGDSKVkiLKDINLQIQKGDFVCIMGASGSGKttllql--lggldIPSV---GSIRVDGTEISTlKEK 77
Cdd:COG1117 11 KIEVRNL--NVYYGDKQA--LKDINLDIPENKVTALIGPSGCGKstllrclnrmndlIPGArveGEILLDGEDIYD-PDV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 78 ELALFRRhKIGFIFQQFNLIP--VFnaeENVGLPLLLDNVSQKK---ATVTanRLLELVGL----KGKEKHLPAQLSGGQ 148
Cdd:COG1117 86 DVVELRR-RVGMVFQKPNPFPksIY---DNVAYGLRLHGIKSKSeldEIVE--ESLRKAALwdevKDRLKKSALGLSGGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 149 QQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRnacdELGQ--TAVIVTHDPFVAAH-ADKVVFLLDGEVIhEH 225
Cdd:COG1117 160 QQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELIL----ELKKdyTIVIVTHNMQQAARvSDYTAFFYLGELV-EF 234
|
....
gi 446943912 226 AESK 229
Cdd:COG1117 235 GPTE 238
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-203 |
6.33e-33 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 123.41 E-value: 6.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 3 IIEIEGLEKSFDiGDSKVKilkDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEIStlkekELALF 82
Cdd:PRK11607 19 LLEIRNLTKSFD-GQHAVD---DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS-----HVPPY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 83 RRhKIGFIFQQFNLIPVFNAEENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEP 162
Cdd:PRK11607 90 QR-PINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRP 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446943912 163 AIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHD 203
Cdd:PRK11607 169 KLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHD 209
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-221 |
8.99e-33 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 117.70 E-value: 8.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLekSFDIGDSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKElalFR 83
Cdd:cd03246 1 LEVENV--SFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNE---LG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 RHkIGFIFQQFNLIPvfnaeenvGlpLLLDNVsqkkatvtanrllelvglkgkekhlpaqLSGGQQQRVAIARAFANEPA 163
Cdd:cd03246 76 DH-VGYLPQDDELFS--------G--SIAENI----------------------------LSGGQRQRLGLARALYGNPR 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446943912 164 IILADEPTGALDSENSKNIIAALRNAcDELGQTAVIVTHDPFVAAHADKVVFLLDGEV 221
Cdd:cd03246 117 ILVLDEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
3-222 |
1.03e-32 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 122.11 E-value: 1.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 3 IIEIEGLEKsfdigDSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLK-EKElal 81
Cdd:NF040840 1 MIRIENLSK-----DWKEFKLRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPpEKR--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 82 frrhKIGFIFQQFNLIPVFNAEENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANE 161
Cdd:NF040840 73 ----GIAYVYQNYMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446943912 162 PAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDpFVAA--HADKVVFLLDGEVI 222
Cdd:NF040840 149 PKLLLLDEPLSALDVQTRDELIREMKRWHREFGFTAIHVTHN-FEEAlsLADRVGIMLNGRLS 210
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-224 |
2.20e-32 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 118.99 E-value: 2.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 1 MNIIEIEGLEKSFDigdsKVKILKDINLQIQKGDFVCIMGASGSGK---------TTLlqllggldiPSVGSIRVDGTEI 71
Cdd:COG0411 2 DPLLEVRGLTKRFG----GLVAVDDVSLEVERGEIVGLIGPNGAGKttlfnlitgFYR---------PTSGRILFDGRDI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 72 STLKEKELAlfrRHKIGFIFQQFNLIPVFNAEENV---------------GLPLLLDNVSQKKATVTANRLLELVGLKGK 136
Cdd:COG0411 69 TGLPPHRIA---RLGIARTFQNPRLFPELTVLENVlvaaharlgrgllaaLLRLPRARREEREARERAEELLERVGLADR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 137 EKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHD-PFVAAHADKVVF 215
Cdd:COG0411 146 ADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDmDLVMGLADRIVV 225
|
....*....
gi 446943912 216 LLDGEVIHE 224
Cdd:COG0411 226 LDFGRVIAE 234
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
3-229 |
4.91e-32 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 117.78 E-value: 4.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 3 IIEIEGLEKSFdiGDSKVkiLKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLD--IPSV---GSIRVDGTEISTLKEK 77
Cdd:TIGR00972 1 AIEIENLNLFY--GEKEA--LKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNdlVPGVrieGKVLFDGQDIYDKKID 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 78 ELALfrRHKIGFIFQQFNLIPvFNAEENVGLPLLLDNV-SQKKATVTANRLLELVGL----KGKEKHLPAQLSGGQQQRV 152
Cdd:TIGR00972 77 VVEL--RRRVGMVFQKPNPFP-MSIYDNIAYGPRLHGIkDKKELDEIVEESLKKAALwdevKDRLHDSALGLSGGQQQRL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446943912 153 AIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELgqTAVIVTHDPFVAAH-ADKVVFLLDGEVIhEHAESK 229
Cdd:TIGR00972 154 CIARALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKKY--TIVIVTHNMQQAARiSDRTAFFYDGELV-EYGPTE 228
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
22-203 |
1.43e-31 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 117.11 E-value: 1.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 22 ILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKElalfrrhkiGFIFQQFNLIPVFN 101
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER---------GVVFQNEGLLPWRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 102 AEENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKN 181
Cdd:PRK11248 87 VQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQ 166
|
170 180
....*....|....*....|..
gi 446943912 182 IIAALRNACDELGQTAVIVTHD 203
Cdd:PRK11248 167 MQTLLLKLWQETGKQVLLITHD 188
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-213 |
3.44e-31 |
|
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: 114.50 E-value: 3.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFDigdsKVKILKDINLQIQKGDFVCIMGASGSGK----------TTllqllggldiPSVGSIRVDGTEIst 73
Cdd:COG4133 3 LEAENLSCRRG----ERLLFSGLSFTLAAGEALALTGPNGSGKttllrilaglLP----------PSAGEVLWNGEPI-- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 74 lkEKELALFRRHkIGFIFQQFNLIPVFNAEENVGLPLLLDNVSQKKATVTAnrLLELVGLKGKEKHLPAQLSGGQQQRVA 153
Cdd:COG4133 67 --RDAREDYRRR-LAYLGHADGLKPELTVRENLRFWAALYGLRADREAIDE--ALEAVGLAGLADLPVRQLSAGQKRRVA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 154 IARAFANEPAIILADEPTGALDSENSKNIIAALRNACDElGQTAVIVTHDPFVAAHADKV 213
Cdd:COG4133 142 LARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLAR-GGAVLLTTHQPLELAAARVL 200
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-221 |
4.84e-31 |
|
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: 113.26 E-value: 4.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFDigdsKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKelalfR 83
Cdd:cd03230 1 IEVRNLSKRYG----KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE-----V 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 RHKIGFIFQQFNLIPVFNAEENVglpllldnvsqkkatvtanrllelvglkgkekhlpaQLSGGQQQRVAIARAFANEPA 163
Cdd:cd03230 72 KRRIGYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446943912 164 IILADEPTGALDSENSKNIIAALRNACDElGQTAVIVTHD-PFVAAHADKVVFLLDGEV 221
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHIlEEAERLCDRVAILNNGRI 173
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-227 |
1.53e-30 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 119.11 E-value: 1.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLekSFDIGDSKvKILKDINLQIQKGDFVCIMGASGSGKttllqllggldiPSVGSIRVDGTEISTLKEKELalfr 83
Cdd:COG1132 340 IEFENV--SFSYPGDR-PVLKDISLTIPPGETVALVGPSGSGKstlvnlllrfydPTSGRILIDGVDIRDLTLESL---- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 RHKIGFIFQQFNLipvFNA--EENV--GLPllldNVSQ---KKATVTAN-----RLLE-----LVGLKGkekhlpAQLSG 146
Cdd:COG1132 413 RRQIGVVPQDTFL---FSGtiRENIryGRP----DATDeevEEAAKAAQahefiEALPdgydtVVGERG------VNLSG 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 147 GQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDelGQTAVIVTHDPFVAAHADKVVFLLDGEVIHE-- 224
Cdd:COG1132 480 GQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRNADRILVLDDGRIVEQgt 557
|
...
gi 446943912 225 HAE 227
Cdd:COG1132 558 HEE 560
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-222 |
1.84e-30 |
|
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: 118.63 E-value: 1.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 3 IIEIEGLEKSFDI-------GDSKVKILKDINLQIQKGDFVCIMGASGSGKttllqllggldIPSVGSIRVDGTEISTLK 75
Cdd:COG4172 275 LLEARDLKVWFPIkrglfrrTVGHVKAVDGVSLTLRRGETLGLVGESGSGKstlgl-allrlIPSEGEIRFDGQDLDGLS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 76 EKELALFRRHkIGFIFQ----QFNliPVFNAEENVGLPLLLDNVSQKKATVTA--NRLLELVGLKGKEKH-LPAQLSGGQ 148
Cdd:COG4172 354 RRALRPLRRR-MQVVFQdpfgSLS--PRMTVGQIIAEGLRVHGPGLSAAERRArvAEALEEVGLDPAARHrYPHEFSGGQ 430
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446943912 149 QQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHD-PFVAAHADKVVFLLDGEVI 222
Cdd:COG4172 431 RQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDlAVVRALAHRVMVMKDGKVV 505
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-224 |
2.24e-30 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 114.34 E-value: 2.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 2 NIIEIEGLekSFDIGDSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTeisTLKEKELAL 81
Cdd:PRK13635 4 EIIRVEHI--SFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM---VLSEETVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 82 FRRhKIGFIFQ----QFNLIPVFN----AEENVGLP--LLLDNVSQKkatvtanrlLELVGLKGKEKHLPAQLSGGQQQR 151
Cdd:PRK13635 79 VRR-QVGMVFQnpdnQFVGATVQDdvafGLENIGVPreEMVERVDQA---------LRQVGMEDFLNREPHRLSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446943912 152 VAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVAAHADKVVFLLDGEVIHE 224
Cdd:PRK13635 149 VAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEE 221
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
3-203 |
3.48e-30 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 114.83 E-value: 3.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 3 IIEIEGLEKSFDIG-------DSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLK 75
Cdd:COG4608 7 LLEVRDLKKHFPVRgglfgrtVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 76 EKELALFRRhKIGFIFQ--QFNLIPVFNAEENVGLPLLLDNVSQKKATVT-ANRLLELVGLKgkEKHL---PAQLSGGQQ 149
Cdd:COG4608 87 GRELRPLRR-RMQMVFQdpYASLNPRMTVGDIIAEPLRIHGLASKAERRErVAELLELVGLR--PEHAdryPHEFSGGQR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446943912 150 QRVAIARAFANEPAIILADEPTGALD-SENSK--NIIAALRnacDELGQTAVIVTHD 203
Cdd:COG4608 164 QRIGIARALALNPKLIVCDEPVSALDvSIQAQvlNLLEDLQ---DELGLTYLFISHD 217
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
4-222 |
6.57e-30 |
|
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: 111.53 E-value: 6.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFDigDSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfR 83
Cdd:cd03245 3 IEFRNVSFSYP--NQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADL---R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 RHkIGFIFQQFNLipvFNAEenvglplLLDNVSQKKATVTANRLLELVGLKGKEKHLP--------------AQLSGGQQ 149
Cdd:cd03245 78 RN-IGYVPQDVTL---FYGT-------LRDNITLGAPLADDERILRAAELAGVTDFVNkhpngldlqigergRGLSGGQR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446943912 150 QRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDelGQTAVIVTHDPFVAAHADKVVFLLDGEVI 222
Cdd:cd03245 147 QAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
27-221 |
6.70e-30 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 111.49 E-value: 6.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 27 NLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLkekelALFRRhKIGFIFQQFNLIPVFNAEENV 106
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGL-----APYQR-PVSMLFQENNLFAHLTVRQNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 107 GL---PLLLDNVSQKKATVTANRLlelVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNII 183
Cdd:TIGR01277 92 GLglhPGLKLNAEQQEKVVDAAQQ---VGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEML 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 446943912 184 AALRNACDELGQTAVIVTHDPF-VAAHADKVVFLLDGEV 221
Cdd:TIGR01277 169 ALVKQLCSERQRTLLMVTHHLSdARAIASQIAVVSQGKI 207
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-224 |
7.99e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 112.31 E-value: 7.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 1 MNIIEIEGLEKSFdigdSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGG-----LDIPSVGSIRVDGTEISTLK 75
Cdd:PRK14247 1 MNKIEIRDLKVSF----GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRlielyPEARVSGEVYLDGQDIFKMD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 76 EKELalfrRHKIGFIFQQFNLIPVFNAEENVGLPLLLDNVSQKKATVTA--NRLLELVGLKGKEKH---LPA-QLSGGQQ 149
Cdd:PRK14247 77 VIEL----RRRVQMVFQIPNPIPNLSIFENVALGLKLNRLVKSKKELQErvRWALEKAQLWDEVKDrldAPAgKLSGGQQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446943912 150 QRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELgqTAVIVTHDPFVAAH-ADKVVFLLDGEVIHE 224
Cdd:PRK14247 153 QRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARiSDYVAFLYKGQIVEW 226
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
20-227 |
1.65e-29 |
|
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: 111.09 E-value: 1.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 20 VKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfrRHKIGFIFQQFNLipv 99
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWL----RSQIGLVSQEPVL--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 100 FNA--EENV--GLPLLLDnVSQKKATVTAN----------RLLELVGLKGkekhlpAQLSGGQQQRVAIARAFANEPAII 165
Cdd:cd03249 89 FDGtiAENIryGKPDATD-EEVEEAAKKANihdfimslpdGYDTLVGERG------SQLSGGQKQRIAIARALLRNPKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446943912 166 LADEPTGALDSENSKNIIAALRNACdeLGQTAVIVTHDPFVAAHADKVVFLLDGEVIHE--HAE 227
Cdd:cd03249 162 LLDEATSALDAESEKLVQEALDRAM--KGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQgtHDE 223
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-221 |
1.77e-29 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 111.69 E-value: 1.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 6 IEGLEKSFdiGDSKVkiLKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKelalfrrh 85
Cdd:PRK11247 15 LNAVSKRY--GERTV--LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARED-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 86 kIGFIFQQFNLIPVFNAEENVGLPLlldnvsQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAII 165
Cdd:PRK11247 83 -TRLMFQDARLLPWKKVIDNVGLGL------KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446943912 166 LADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVA-AHADKVVFLLDGEV 221
Cdd:PRK11247 156 LLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAvAMADRVLLIEEGKI 212
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-224 |
2.65e-29 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 110.94 E-value: 2.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFdiGDSKVkiLKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELAlfr 83
Cdd:COG4604 2 IEIKNVSKRY--GGKVV--LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELA--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 rhKIGFIFQQFNLIPV-FNAEENVGL---PLlldnvSQKKATV-------TANRLLELVGLKgkEKHLPaQLSGGQQQRV 152
Cdd:COG4604 75 --KRLAILRQENHINSrLTVRELVAFgrfPY-----SKGRLTAedreiidEAIAYLDLEDLA--DRYLD-ELSGGQRQRA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446943912 153 AIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHD-PFVAAHADKVVFLLDGEVIHE 224
Cdd:COG4604 145 FIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDiNFASCYADHIVAMKDGRVVAQ 217
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
4-222 |
2.88e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 111.24 E-value: 2.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLekSFDIGDSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfr 83
Cdd:PRK13632 8 IKVENV--SFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEI---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 RHKIGFIFQ----QFNLIPVfnaEENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFA 159
Cdd:PRK13632 82 RKKIGIIFQnpdnQFIGATV---EDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446943912 160 NEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVAAHADKVVFLLDGEVI 222
Cdd:PRK13632 159 LNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLI 221
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-216 |
4.14e-29 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 114.69 E-value: 4.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFDIGDskvKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKelalFR 83
Cdd:TIGR02857 322 LEFSGVSVAYPGRR---PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADAD----SW 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 RHKIGFIFQQFNLIPVFNAEeNVGLpllldnvSQKKATVTA-NRLLELVGLKGKEKHLP-----------AQLSGGQQQR 151
Cdd:TIGR02857 395 RDQIAWVPQHPFLFAGTIAE-NIRL-------ARPDASDAEiREALERAGLDEFVAALPqgldtpigeggAGLSGGQAQR 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446943912 152 VAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDelGQTAVIVTHDPFVAAHADKVVFL 216
Cdd:TIGR02857 467 LALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALADRIVVL 529
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-221 |
5.97e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 110.59 E-value: 5.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 1 MNIIEIEGLEKSFDiGDSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELa 80
Cdd:PRK13650 2 SNIIEVKNLTFKYK-EDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDI- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 81 lfrRHKIGFIFQ----QFNLIPVfnaEENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIAR 156
Cdd:PRK13650 80 ---RHKIGMVFQnpdnQFVGATV---EDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446943912 157 AFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVAAHADKVVFLLDGEV 221
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-222 |
6.31e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 110.66 E-value: 6.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 2 NIIEIEGLekSFDIGDSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIP---SVGSIRVDGTeisTLKEKE 78
Cdd:PRK13640 4 NIVEFKHV--SFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGI---TLTAKT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 79 LALFRrHKIGFIFQ----QFNLIPVfnaEENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAI 154
Cdd:PRK13640 79 VWDIR-EKVGIVFQnpdnQFVGATV---GDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446943912 155 ARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVAAHADKVVFLLDGEVI 222
Cdd:PRK13640 155 AGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLL 222
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
22-216 |
7.05e-29 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 108.72 E-value: 7.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 22 ILKDINLQIQKGDFVCIMGASGSGKT---TLLQLLGGLDIPSVGSIRVDGTEISTLKekelALFRRhkIGFIFQQFNLIP 98
Cdd:COG4136 16 LLAPLSLTVAPGEILTLMGPSGSGKStllAAIAGTLSPAFSASGEVLLNGRRLTALP----AEQRR--IGILFQDDLLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 99 VFNAEENV--GLPlllDNV--SQKKATVtaNRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGAL 174
Cdd:COG4136 90 HLSVGENLafALP---PTIgrAQRRARV--EQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446943912 175 DSENSKNIIAALRNACDELGQTAVIVTHDPFVAAHADKVVFL 216
Cdd:COG4136 165 DAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAAGRVLDL 206
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
17-227 |
1.08e-28 |
|
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: 108.86 E-value: 1.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 17 DSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKekeLALFRRHkIGFIFQQfnl 96
Cdd:cd03253 11 DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVT---LDSLRRA-IGVVPQD--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 97 IPVFNA--EENV--GLPLLLD-----------------NVSQKKATVTANRllelvGLKgkekhlpaqLSGGQQQRVAIA 155
Cdd:cd03253 84 TVLFNDtiGYNIryGRPDATDeevieaakaaqihdkimRFPDGYDTIVGER-----GLK---------LSGGEKQRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446943912 156 RAFANEPAIILADEPTGALDSENSKNIIAALRNACDelGQTAVIVTHDPFVAAHADKVVFLLDGEVIHE--HAE 227
Cdd:cd03253 150 RAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVNADKIIVLKDGRIVERgtHEE 221
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
23-224 |
2.37e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 109.02 E-value: 2.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 23 LKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGteISTLKEKELALFRRhKIGFIFQQ-FNLIPVFN 101
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEENLWDIRN-KAGMVFQNpDNQIVATI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 102 AEENVGL-PLLLdNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSK 180
Cdd:PRK13633 103 VEEDVAFgPENL-GIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446943912 181 NIIAALRNACDELGQTAVIVTHDPFVAAHADKVVFLLDGEVIHE 224
Cdd:PRK13633 182 EVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVME 225
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
12-227 |
3.58e-28 |
|
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: 107.32 E-value: 3.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 12 SFDIGDSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfrRHKIGFIF 91
Cdd:cd03251 7 TFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASL----RRQIGLVS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 92 QQFNLipvFNA--EENV--GLPllldNVSQK---KATVTAN------RLLE----LVGLKGkekhlpAQLSGGQQQRVAI 154
Cdd:cd03251 83 QDVFL---FNDtvAENIayGRP----GATREeveEAARAANahefimELPEgydtVIGERG------VKLSGGQRQRIAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446943912 155 ARAFANEPAIILADEPTGALDSENSKNIIAALrnacDEL--GQTAVIVTHDPFVAAHADKVVFLLDGEVIHE--HAE 227
Cdd:cd03251 150 ARALLKDPPILILDEATSALDTESERLVQAAL----ERLmkNRTTFVIAHRLSTIENADRIVVLEDGKIVERgtHEE 222
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-222 |
4.61e-28 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 109.81 E-value: 4.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 2 NIIEIEGLEKSFdiGDSKVkiLKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEI--STLKEKEl 79
Cdd:PRK11432 5 NFVVLKNITKRF--GSNTV--IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVthRSIQQRD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 80 alfrrhkIGFIFQQFNLIPVFNAEENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFA 159
Cdd:PRK11432 80 -------ICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446943912 160 NEPAIILADEPTGALDSenskNIIAALRNACDELGQ----TAVIVTHDPFVA-AHADKVVFLLDGEVI 222
Cdd:PRK11432 153 LKPKVLLFDEPLSNLDA----NLRRSMREKIRELQQqfniTSLYVTHDQSEAfAVSDTVIVMNKGKIM 216
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
25-224 |
5.41e-28 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 107.07 E-value: 5.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 25 DINLQIQKGDFVCIMGASGSGK----TTLLQLLGGLDIPSVGSIRVDGTEISTLKekelalFRRHKIGFIFQQ----FNl 96
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKsltcLAILGLLPPGLTQTSGEILLDGRPLLPLS------IRGRHIATIMQNprtaFN- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 97 iPVFNAEENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHL---PAQLSGGQQQRVAIARAFANEPAIILADEPTGA 173
Cdd:TIGR02770 77 -PLFTMGNHAIETLRSLGKLSKQARALILEALEAVGLPDPEEVLkkyPFQLSGGMLQRVMIALALLLEPPFLIADEPTTD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446943912 174 LDSENSKNIIAALRNACDELGQTAVIVTHDPFVAAH-ADKVVFLLDGEVIHE 224
Cdd:TIGR02770 156 LDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARiADEVAVMDDGRIVER 207
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-222 |
1.49e-27 |
|
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: 105.03 E-value: 1.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 5 EIEGLekSFDIGDSKvKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEIstlKEKElalfRR 84
Cdd:cd03226 1 RIENI--SFSYKKGT-EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKE----RR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 85 HKIGFIFQ--QFNLIpvfnaEENVGLPLLLDNVSQKKATVTANRLLELVGLKG-KEKHlPAQLSGGQQQRVAIARAFANE 161
Cdd:cd03226 71 KSIGYVMQdvDYQLF-----TDSVREELLLGLKELDAGNEQAETVLKDLDLYAlKERH-PLSLSGGQKQRLAIAAALLSG 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446943912 162 PAIILADEPTGALDSENSKNIIAALRNACDElGQTAVIVTHDP-FVAAHADKVVFLLDGEVI 222
Cdd:cd03226 145 KDLLIFDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYeFLAKVCDRVLLLANGAIV 205
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-224 |
2.16e-27 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 106.39 E-value: 2.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 1 MNIIEIEGLekSFDIGDSKvkILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELA 80
Cdd:PRK11831 5 ANLVDMRGV--SFTRGNRC--IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 81 LFRRhKIGFIFQQFNLIPVFNAEENVGLPL---------LLdnvsqkKATVTANrlLELVGLKGKEKHLPAQLSGGQQQR 151
Cdd:PRK11831 81 TVRK-RMSMLFQSGALFTDMNVFDNVAYPLrehtqlpapLL------HSTVMMK--LEAVGLRGAAKLMPSELSGGMARR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446943912 152 VAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHD-PFVAAHADKVVFLLDGEVIHE 224
Cdd:PRK11831 152 AALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDvPEVLSIADHAYIVADKKIVAH 225
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
4-238 |
3.64e-27 |
|
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: 104.88 E-value: 3.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLekSFDIGDSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLkekELALFR 83
Cdd:cd03252 1 ITFEHV--RFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALA---DPAWLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 RhKIGFIFQQfNLIpvFNAEenvglplLLDNVSQKKATVTANRLLELVGLKGKEK---HLP-----------AQLSGGQQ 149
Cdd:cd03252 76 R-QVGVVLQE-NVL--FNRS-------IRDNIALADPGMSMERVIEAAKLAGAHDfisELPegydtivgeqgAGLSGGQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 150 QRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDelGQTAVIVTHDPFVAAHADKVVFLLDGEVI----HEH 225
Cdd:cd03252 145 QRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKNADRIIVMEKGRIVeqgsHDE 222
|
250
....*....|...
gi 446943912 226 AESKGWKFRNIPQ 238
Cdd:cd03252 223 LLAENGLYAYLYQ 235
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
4-221 |
4.02e-27 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 109.45 E-value: 4.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLekSFDIGDSKVKILKDINLQIQKGDFVCIMGASGSGK-----------TtllqllggldiPSVGSIRVDGTEIS 72
Cdd:COG4618 331 LSVENL--TVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKstlarllvgvwP-----------PTAGSVRLDGADLS 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 73 TLKEKELAlfrRHkIGFIFQQFNLipvFNA--EENVGLpllLDNVSQKKAtVTANRLL---ELVGlkgkekHLP------ 141
Cdd:COG4618 398 QWDREELG---RH-IGYLPQDVEL---FDGtiAENIAR---FGDADPEKV-VAAAKLAgvhEMIL------RLPdgydtr 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 142 -----AQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDElGQTAVIVTHDPFVAAHADKVVFL 216
Cdd:COG4618 461 igeggARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPSLLAAVDKLLVL 539
|
....*
gi 446943912 217 LDGEV 221
Cdd:COG4618 540 RDGRV 544
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
23-222 |
4.62e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 105.87 E-value: 4.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 23 LKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEIS-TLKEKELALFRRhKIGFIFqQFNLIPVFn 101
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITaGKKNKKLKPLRK-KVGIVF-QFPEHQLF- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 102 aEENVglplLLD--------NVSQKKATVTANRLLELVGLkgKEKHL---PAQLSGGQQQRVAIARAFANEPAIILADEP 170
Cdd:PRK13634 100 -EETV----EKDicfgpmnfGVSEEDAKQKAREMIELVGL--PEELLarsPFELSGGQMRRVAIAGVLAMEPEVLVLDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446943912 171 TGALDSENSKNIIAALRNACDELGQTAVIVTH---DpfVAAHADKVVFLLDGEVI 222
Cdd:PRK13634 173 TAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHsmeD--AARYADQIVVMHKGTVF 225
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-224 |
5.76e-27 |
|
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: 103.99 E-value: 5.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 3 IIEIEGLEKSFDIGDSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGteISTLKEKELAlf 82
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVKEPAEA-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 83 rRHKIGFIFQQFNLIPVFNAEENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEP 162
Cdd:cd03266 77 -RRRLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446943912 163 AIILADEPTGALDSENSKNIIAALRNACDElGQTAVIVTHD-PFVAAHADKVVFLLDGEVIHE 224
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQLRAL-GKCILFSTHImQEVERLCDRVVVLHRGRVVYE 217
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-222 |
7.22e-27 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 104.47 E-value: 7.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLekSFDIGdsKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALFR 83
Cdd:PRK13548 3 LEARNL--SVRLG--GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 rhkiGFIFQQFNLIPVFNAEENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFA---- 159
Cdd:PRK13548 79 ----AVLPQHSSLSFPFTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwe 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446943912 160 --NEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVAAH-ADKVVFLLDGEVI 222
Cdd:PRK13548 155 pdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARyADRIVLLHQGRLV 220
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-223 |
1.16e-26 |
|
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: 102.97 E-value: 1.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFdiGDSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKelalfR 83
Cdd:cd03263 1 LQIRNLTKTY--KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKA-----A 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 RHKIGFIFQQFNLIPVFNAEENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPA 163
Cdd:cd03263 74 RQSLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446943912 164 IILADEPTGALDSEnSKNIIAALRNACDElGQTAVIVTHDPFVAAH-ADKVVFLLDGEVIH 223
Cdd:cd03263 154 VLLLDEPTSGLDPA-SRRAIWDLILEVRK-GRSIILTTHSMDEAEAlCDRIAIMSDGKLRC 212
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
25-221 |
1.44e-26 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 105.96 E-value: 1.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 25 DINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTeisTLKEKELALF---RRHKIGFIFQQFNLIPVFN 101
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGR---TLFDSRKGIFlppEKRRIGYVFQEARLFPHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 102 AEENvgLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKN 181
Cdd:TIGR02142 92 VRGN--LRYGMKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446943912 182 IIAALRNACDELGQTAVIVTHDPFVAAH-ADKVVFLLDGEV 221
Cdd:TIGR02142 170 ILPYLERLHAEFGIPILYVSHSLQEVLRlADRVVVLEDGRV 210
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
4-224 |
1.69e-26 |
|
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: 103.07 E-value: 1.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFDigdSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfr 83
Cdd:cd03254 3 IEFENVNFSYD---EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSL---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 RHKIGFIFQQFNLipvFNAE--ENvglpLLLDNVSQKKATVtaNRLLELVGLKGKEKHLP-----------AQLSGGQQQ 150
Cdd:cd03254 76 RSMIGVVLQDTFL---FSGTimEN----IRLGRPNATDEEV--IEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446943912 151 RVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDelGQTAVIVTHDPFVAAHADKVVFLLDGEVIHE 224
Cdd:cd03254 147 LLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKNADKILVLDDGKIIEE 218
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-224 |
7.16e-26 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 105.65 E-value: 7.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFDigdsKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLD---------------IPSVGSIRV-- 66
Cdd:TIGR03269 1 IEVKNLTKKFD----GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyeptsgriiyhvalCEKCGYVERps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 67 -DGTEI----STLKEKEL-------ALFR--RHKIGFIFQQ-FNLIPVFNAEENVGLPLLLDNVSQKKATVTANRLLELV 131
Cdd:TIGR03269 77 kVGEPCpvcgGTLEPEEVdfwnlsdKLRRriRKRIAIMLQRtFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 132 GLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVAAH-A 210
Cdd:TIGR03269 157 QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDlS 236
|
250
....*....|....
gi 446943912 211 DKVVFLLDGEVIHE 224
Cdd:TIGR03269 237 DKAIWLENGEIKEE 250
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-224 |
7.79e-26 |
|
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: 100.97 E-value: 7.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLeksfDIGDSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELAlfr 83
Cdd:cd03224 1 LEVENL----NAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 RHKIGFIFQQFNLIPVFNAEENVGLPLLLDNVSQKKATVtaNRLLELV-GLKGKEKHLPAQLSGGQQQRVAIARAFANEP 162
Cdd:cd03224 74 RAGIGYVPEGRRIFPELTVEENLLLGAYARRRAKRKARL--ERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446943912 163 AIILADEPTGALDSENSKNIIAALRNACDElGQTAVIVTHD-PFVAAHADKVVFLLDGEVIHE 224
Cdd:cd03224 152 KLLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNaRFALEIADRAYVLERGRVVLE 213
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
3-224 |
2.41e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 100.92 E-value: 2.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 3 IIEIEGLEKSFDIGDSkvkILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALf 82
Cdd:PRK13639 1 ILETRDLKYSYPDGTE---ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEV- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 83 rRHKIGFIFQQF-NLIPVFNAEENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANE 161
Cdd:PRK13639 77 -RKTVGIVFQNPdDQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446943912 162 PAIILADEPTGALDSENSKNIIAALRNACDElGQTAVIVTHD-PFVAAHADKVVFLLDGEVIHE 224
Cdd:PRK13639 156 PEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDvDLVPVYADKVYVMSDGKIIKE 218
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-249 |
2.61e-25 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 100.47 E-value: 2.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 3 IIEIEGLEKSFDigdsKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGgldipsvGSIRVDGTEISTLK------E 76
Cdd:PRK09984 4 IIRVEKLAKTFN----QHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLS-------GLITGDKSAGSHIEllgrtvQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 77 KELALFR-----RHKIGFIFQQFNLIPVFNAEENV------GLPLLLDNVS-----QKKATVTAnrlLELVGLKGKEKHL 140
Cdd:PRK09984 73 REGRLARdirksRANTGYIFQQFNLVNRLSVLENVligalgSTPFWRTCFSwftreQKQRALQA---LTRVGMVHFAHQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 141 PAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHD-PFVAAHADKVVFLLDG 219
Cdd:PRK09984 150 VSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQvDYALRYCERIVALRQG 229
|
250 260 270
....*....|....*....|....*....|
gi 446943912 220 EVIHEHAESkgwKFRNipQQVIHIQEIMNR 249
Cdd:PRK09984 230 HVFYDGSSQ---QFDN--ERFDHLYRSINR 254
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
18-221 |
2.94e-25 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 103.97 E-value: 2.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 18 SKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEIstlKEKELALFRRHkIGFIFQQFNLI 97
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADL---KQWDRETFGKH-IGYLPQDVELF 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 98 PVFNAEenvglpllldNVSQKKATVTANRLLELVGLKGKEK---HLP-----------AQLSGGQQQRVAIARAFANEPA 163
Cdd:TIGR01842 405 PGTVAE----------NIARFGENADPEKIIEAAKLAGVHElilRLPdgydtvigpggATLSGGQRQRIALARALYGDPK 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446943912 164 IILADEPTGALDSENSkniiAALRNACDEL---GQTAVIVTHDPFVAAHADKVVFLLDGEV 221
Cdd:TIGR01842 475 LVVLDEPNSNLDEEGE----QALANAIKALkarGITVVVITHRPSLLGCVDKILVLQDGRI 531
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
23-222 |
3.34e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 100.59 E-value: 3.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 23 LKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEI-STLKEKELALFRRhKIGFIFqQFNLIPVFn 101
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItSTSKNKDIKQIRK-KVGLVF-QFPESQLF- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 102 aEENVglplLLD--------NVSQKKATVTANRLLELVGLKGK--EKHlPAQLSGGQQQRVAIARAFANEPAIILADEPT 171
Cdd:PRK13649 100 -EETV----LKDvafgpqnfGVSQEEAEALAREKLALVGISESlfEKN-PFELSGGQMRRVAIAGILAMEPKILVLDEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446943912 172 GALDSENSKNIIAALRNaCDELGQTAVIVTH---DpfVAAHADKVVFLLDGEVI 222
Cdd:PRK13649 174 AGLDPKGRKELMTLFKK-LHQSGMTIVLVTHlmdD--VANYADFVYVLEKGKLV 224
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
18-229 |
5.27e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 99.46 E-value: 5.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 18 SKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLD--IPSV---GSIRVDGTEISTLKEKELALfrRHKIGFIFQ 92
Cdd:PRK14239 16 NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNdlNPEVtitGSIVYNGHNIYSPRTDTVDL--RKEIGMVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 93 QFNLIPvFNAEENVGLPLLLDNVSQKKatvtanRLLELV--GLKG-------KEK-HLPA-QLSGGQQQRVAIARAFANE 161
Cdd:PRK14239 94 QPNPFP-MSIYENVVYGLRLKGIKDKQ------VLDEAVekSLKGasiwdevKDRlHDSAlGLSGGQQQRVCIARVLATS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446943912 162 PAIILADEPTGALDSENSKNIIAALRNACDELgqTAVIVTHDPFVAAH-ADKVVFLLDGEVIhEHAESK 229
Cdd:PRK14239 167 PKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRiSDRTGFFLDGDLI-EYNDTK 232
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-224 |
8.34e-25 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 99.38 E-value: 8.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 1 MNIIEIEGLEKSFDIGDSKVK-----ILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLK 75
Cdd:PRK10419 1 MTLLNVSGLSHHYAHGGLSGKhqhqtVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 76 EKELALFRRhKIGFIFQqfNLIPVFNAEENVGL----PLL-LDNVSQKKATVTANRLLELVGLK-GKEKHLPAQLSGGQQ 149
Cdd:PRK10419 81 RAQRKAFRR-DIQMVFQ--DSISAVNPRKTVREiirePLRhLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446943912 150 QRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHD-PFVAAHADKVVFLLDGEVIHE 224
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDlRLVERFCQRVMVMDNGQIVET 233
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
23-223 |
1.14e-24 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 101.26 E-value: 1.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 23 LKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALFRRHKIGFIFQQFNLIPVFNA 102
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 103 EENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNI 182
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446943912 183 IAALRNACDELGQTAVIVTHDPFVAAH-ADKVVFLLDGEVIH 223
Cdd:PRK10070 204 QDELVKLQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQ 245
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-222 |
1.26e-24 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 98.76 E-value: 1.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 1 MNIIEIEGLEKSFDIGDS-----KVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLK 75
Cdd:COG4167 2 SALLEVRNLSKTFKYRTGlfrrqQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 76 EKelalFRRHKIGFIFQQFNliPVFNAEENVG----LPLLLD---NVSQKKATVTANrlLELVGLKGKEKHL-PAQLSGG 147
Cdd:COG4167 82 YK----YRCKHIRMIFQDPN--TSLNPRLNIGqileEPLRLNtdlTAEEREERIFAT--LRLVGLLPEHANFyPHMLSSG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446943912 148 QQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVAAH-ADKVVFLLDGEVI 222
Cdd:COG4167 154 QKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHiSDKVLVMHQGEVV 229
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-228 |
1.84e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 98.65 E-value: 1.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 2 NIIEIEGLEKSFDIGdskVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELal 81
Cdd:PRK13647 3 NIIEVEDLHFRYKDG---TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWV-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 82 frRHKIGFIFQQfnliP---VFNA--EENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIAR 156
Cdd:PRK13647 78 --RSKVGLVFQD----PddqVFSStvWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446943912 157 AFANEPAIILADEPTGALDSENSKNIIAALrNACDELGQTAVIVTHD-PFVAAHADKVVFLLDGEVIHEHAES 228
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEIL-DRLHNQGKTVIVATHDvDLAAEWADQVIVLKEGRVLAEGDKS 223
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
25-222 |
2.34e-24 |
|
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: 99.79 E-value: 2.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 25 DINLQIQKGDF------------VC-IMGASGSGK----------TTllqllggldiPSVGSIRVDGTeisTLKEKELAL 81
Cdd:COG4148 4 EVDFRLRRGGFtldvdftlpgrgVTaLFGPSGSGKttllraiaglER----------PDSGRIRLGGE---VLQDSARGI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 82 F----RRHkIGFIFQQFNLIPVFNAEENvglpLL--LDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIA 155
Cdd:COG4148 71 FlpphRRR-IGYVFQEARLFPHLSVRGN----LLygRKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIG 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446943912 156 RAFANEPAIILADEPTGALDsENSKN-IIAALRNACDELGQTAVIVTHDPF-VAAHADKVVFLLDGEVI 222
Cdd:COG4148 146 RALLSSPRLLLMDEPLAALD-LARKAeILPYLERLRDELDIPILYVSHSLDeVARLADHVVLLEQGRVV 213
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
4-224 |
4.04e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 98.23 E-value: 4.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFDIG-DSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIR----------------- 65
Cdd:PRK13651 3 IKVKNIVKIFNKKlPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwifkdeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 66 -VDGTEISTLKEKELALFR--RHKIGFIFQqFNLIPVFNA--EENVGLPLLLDNVSQKKATVTANRLLELVGLKgkEKHL 140
Cdd:PRK13651 83 vLEKLVIQKTRFKKIKKIKeiRRRVGVVFQ-FAEYQLFEQtiEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLD--ESYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 141 ---PAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDElGQTAVIVTHD-PFVAAHADKVVFL 216
Cdd:PRK13651 160 qrsPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDlDNVLEWTKRTIFF 238
|
....*...
gi 446943912 217 LDGEVIHE 224
Cdd:PRK13651 239 KDGKIIKD 246
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-222 |
4.38e-24 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 100.95 E-value: 4.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLekSFDIGDSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKekeLALFR 83
Cdd:TIGR02203 331 VEFRNV--TFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT---LASLR 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 RHkIGFIFQQFNLipvFNAE--ENV--GLPLLLDNVSQKKATVTANrLLELVGLKGKEKHLP-----AQLSGGQQQRVAI 154
Cdd:TIGR02203 406 RQ-VALVSQDVVL---FNDTiaNNIayGRTEQADRAEIERALAAAY-AQDFVDKLPLGLDTPigengVLLSGGQRQRLAI 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 155 ARAFANEPAIILADEPTGALDSENSKNIIAALrnacDEL--GQTAVIVTHDPFVAAHADKVVFLLDGEVI 222
Cdd:TIGR02203 481 ARALLKDAPILILDEATSALDNESERLVQAAL----ERLmqGRTTLVIAHRLSTIEKADRIVVMDDGRIV 546
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
21-222 |
5.81e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 97.50 E-value: 5.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 21 KILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRV-DGTEISTLKEKELALFRRhKIGFIFQ------- 92
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgDIVVSSTSKQKEIKPVRK-KVGVVFQfpesqlf 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 93 -QFNLIPVFNAEENVGlpllldnVSQKKATVTANRLLELVGLKGK--EKHlPAQLSGGQQQRVAIARAFANEPAIILADE 169
Cdd:PRK13643 99 eETVLKDVAFGPQNFG-------IPKEKAEKIAAEKLEMVGLADEfwEKS-PFELSGGQMRRVAIAGILAMEPEVLVLDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446943912 170 PTGALDSEnSKNIIAALRNACDELGQTAVIVTH--DPfVAAHADKVVFLLDGEVI 222
Cdd:PRK13643 171 PTAGLDPK-ARIEMMQLFESIHQSGQTVVLVTHlmDD-VADYADYVYLLEKGHII 223
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-226 |
6.01e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 100.09 E-value: 6.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 3 IIEIEGLEKSFdigdSKVKILKDINLQIQKGDFVCIMGASGSGK-----------TtllqllggldiPSVGSIRVDGTEI 71
Cdd:COG1129 4 LLEMRGISKSF----GGVKALDGVSLELRPGEVHALLGENGAGKstlmkilsgvyQ-----------PDSGEILLDGEPV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 72 STLKEKElAlfRRHKIGFIFQQFNLIPVFNAEENVGLPLLLDN---VSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQ 148
Cdd:COG1129 69 RFRSPRD-A--QAAGIAIIHQELNLVPNLSVAENIFLGREPRRgglIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 149 QQRVAIARAFANEPAIILADEPTGALDSENSKN---IIAALRnacdELGQTAVIVTHD-PFVAAHADKVVFLLDGEVIHE 224
Cdd:COG1129 146 QQLVEIARALSRDARVLILDEPTASLTEREVERlfrIIRRLK----AQGVAIIYISHRlDEVFEIADRVTVLRDGRLVGT 221
|
..
gi 446943912 225 HA 226
Cdd:COG1129 222 GP 223
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
12-224 |
8.49e-24 |
|
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: 94.30 E-value: 8.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 12 SFDIGDSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKelalfRRHKIGFIF 91
Cdd:cd03247 7 SFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-----LSSLISVLN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 92 QQFNLipvFNAEenvglplLLDNVSqkkatvtanrllelvglkgkekhlpAQLSGGQQQRVAIARAFANEPAIILADEPT 171
Cdd:cd03247 82 QRPYL---FDTT-------LRNNLG-------------------------RRFSGGERQRLALARILLQDAPIVLLDEPT 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446943912 172 GALDSENSKNIIAALRNACDElgQTAVIVTHDPFVAAHADKVVFLLDGEVIHE 224
Cdd:cd03247 127 VGLDPITERQLLSLIFEVLKD--KTLIWITHHLTGIEHMDKILFLENGKIIMQ 177
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
27-224 |
9.77e-24 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 95.80 E-value: 9.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 27 NLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDG-----TEIStlkekelalfrRHKIGFIFQQFNLIPVFN 101
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGqdhttTPPS-----------RRPVSMLFQENNLFSHLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 102 AEENVGL---PLLLDNVSQKKatvTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSEN 178
Cdd:PRK10771 88 VAQNIGLglnPGLKLNAAQRE---KLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPAL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446943912 179 SKNIIAALRNACDELGQTAVIVTHDPFVAAH-ADKVVFLLDGEVIHE 224
Cdd:PRK10771 165 RQEMLTLVSQVCQERQLTLLMVSHSLEDAARiAPRSLVVADGRIAWD 211
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
3-222 |
1.08e-23 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 96.05 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 3 IIEIEGLEKSFDIGdskvKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDG-----TEISTLKEK 77
Cdd:TIGR02323 3 LLQVSGLSKSYGGG----KGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMrsgaeLELYQLSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 78 ELALFRRHKIGFIFQQF--NLIPVFNAEENVGLPLLLDNVSQ-KKATVTANRLLELVGL-KGKEKHLPAQLSGGQQQRVA 153
Cdd:TIGR02323 79 ERRRLMRTEWGFVHQNPrdGLRMRVSAGANIGERLMAIGARHyGNIRATAQDWLEEVEIdPTRIDDLPRAFSGGMQQRLQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 154 IARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVAA-HADKVVFLLDGEVI 222
Cdd:TIGR02323 159 IARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARlLAQRLLVMQQGRVV 228
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-222 |
1.10e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 96.27 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 22 ILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKE--KELALFRRHKIGFIFQQFNLIPV 99
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDifQIDAIKLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 100 FNAEENVGLPLLLDNVSQKKATVT-ANRLLELVGLkGKEKH----LPA-QLSGGQQQRVAIARAFANEPAIILADEPTGA 173
Cdd:PRK14246 105 LSIYDNIAYPLKSHGIKEKREIKKiVEECLRKVGL-WKEVYdrlnSPAsQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446943912 174 LDSENSKNIIAALRNACDELgqTAVIVTHDPFVAAH-ADKVVFLLDGEVI 222
Cdd:PRK14246 184 IDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARvADYVAFLYNGELV 231
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-224 |
1.60e-23 |
|
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: 93.26 E-value: 1.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFdigdSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKElAlfR 83
Cdd:cd03216 1 LELRGITKRF----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD-A--R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 RHKIGFIFqqfnlipvfnaeenvglpllldnvsqkkatvtanrllelvglkgkekhlpaQLSGGQQQRVAIARAFANEPA 163
Cdd:cd03216 74 RAGIAMVY---------------------------------------------------QLSVGERQMVEIARALARNAR 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446943912 164 IILADEPTGALDSENSKNIIAALRNACDElGQTAVIVTHD-PFVAAHADKVVFLLDGEVIHE 224
Cdd:cd03216 103 LLILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRlDEVFEIADRVTVLRDGRVVGT 163
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
23-251 |
1.97e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 96.05 E-value: 1.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 23 LKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEI-STLKEKELALFRRhKIGFIFQqFNLIPVFn 101
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItPETGNKNLKKLRK-KVSLVFQ-FPEAQLF- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 102 aeENVGL------PLLLdNVSQKKATVTANRLLELVGLKGK-EKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGAL 174
Cdd:PRK13641 100 --ENTVLkdvefgPKNF-GFSEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446943912 175 DSENSKNIIAALRNAcDELGQTAVIVTHD-PFVAAHADKVVFLLDGEVIhEHAEskgwkfrniPQQVIHIQEIMNRHF 251
Cdd:PRK13641 177 DPEGRKEMMQLFKDY-QKAGHTVILVTHNmDDVAEYADDVLVLEHGKLI-KHAS---------PKEIFSDKEWLKKHY 243
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-222 |
2.08e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 98.74 E-value: 2.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLekSFDIGDSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfr 83
Cdd:PRK11160 339 LTLNNV--SFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAL---- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 RHKIGFIFQQfnlIPVFNAEenvglplLLDNVSQKKATVTANRL---LELVGLkgkEKHLPA-------------QLSGG 147
Cdd:PRK11160 413 RQAISVVSQR---VHLFSAT-------LRDNLLLAAPNASDEALievLQQVGL---EKLLEDdkglnawlgeggrQLSGG 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446943912 148 QQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDelGQTAVIVTHDPFVAAHADKVVFLLDGEVI 222
Cdd:PRK11160 480 EQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQFDRICVMDNGQII 552
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
4-222 |
4.41e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 95.11 E-value: 4.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFDIGDS-KVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEIsTLKEKELALF 82
Cdd:PRK13637 3 IKIENLTHIYMEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDI-TDKKVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 83 RRhKIGFIFQ--QFNLIpvfnaEE-----------NVGLpllldnvSQKKATVTANRLLELVGLKG---KEKHlPAQLSG 146
Cdd:PRK13637 82 RK-KVGLVFQypEYQLF-----EEtiekdiafgpiNLGL-------SEEEIENRVKRAMNIVGLDYedyKDKS-PFELSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446943912 147 GQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTH---DpfVAAHADKVVFLLDGEVI 222
Cdd:PRK13637 148 GQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHsmeD--VAKLADRIIVMNKGKCE 224
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
4-222 |
7.20e-23 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 97.24 E-value: 7.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLekSFDIGDSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfr 83
Cdd:TIGR03375 464 IEFRNV--SFAYPGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADL---- 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 RHKIGFIFQQfnlIPVFNA--EENV--GLPLLLDNVSQKKATVTAnrLLELVGLKGKEKHLP-----AQLSGGQQQRVAI 154
Cdd:TIGR03375 538 RRNIGYVPQD---PRLFYGtlRDNIalGAPYADDEEILRAAELAG--VTEFVRRHPDGLDMQigergRSLSGGQRQAVAL 612
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446943912 155 ARAFANEPAIILADEPTGALDSENSKNIIAALRNACdeLGQTAVIVTHDPFVAAHADKVVFLLDGEVI 222
Cdd:TIGR03375 613 ARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWL--AGKTLVLVTHRTSLLDLVDRIIVMDNGRIV 678
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-222 |
8.80e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 97.23 E-value: 8.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 2 NIIEIEGLEKSFDIGDSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDG----------TEI 71
Cdd:PRK10261 11 DVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 72 STLKEKELALFRRHKIGFIFQQ--FNLIPVFNAEENVGLPLLL-DNVSQKKATVTANRLLELVGLKGKEKHL---PAQLS 145
Cdd:PRK10261 91 SEQSAAQMRHVRGADMAMIFQEpmTSLNPVFTVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIPEAQTILsryPHQLS 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446943912 146 GGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVAAH-ADKVVFLLDGEVI 222
Cdd:PRK10261 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEiADRVLVMYQGEAV 248
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
4-222 |
8.83e-23 |
|
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: 92.23 E-value: 8.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFDIGDSKVK--ILKDINLQIQKGDFVCIMGASGSGKTT-LLQLLGGLDIPSV-GSIRVDGTEIStlkekeL 79
Cdd:cd03213 4 LSFRNLTVTVKSSPSKSGkqLLKNVSGKAKPGELTAIMGPSGAGKSTlLNALAGRRTGLGVsGEVLINGRPLD------K 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 80 ALFRRHkIGFIFQQFNLIPVFNAEENVGlpllldnvsqkkatVTANrllelvgLKGkekhlpaqLSGGQQQRVAIARAFA 159
Cdd:cd03213 78 RSFRKI-IGYVPQDDILHPTLTVRETLM--------------FAAK-------LRG--------LSGGERKRVSIALELV 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446943912 160 NEPAIILADEPTGALDSENSKNIIAALRNACDElGQTAVIVTHDP--FVAAHADKVVFLLDGEVI 222
Cdd:cd03213 128 SNPSLLFLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHQPssEIFELFDKLLLLSQGRVI 191
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
22-224 |
1.36e-22 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 92.59 E-value: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 22 ILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELAlfrRHKIGFIFQQFNLIPVFN 101
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERA---RAGIAYVPQGREIFPRLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 102 AEENVglpllldnvsqkkatvtanrLLELVGLKGKEKHLPAQ------------------LSGGQQQRVAIARAFANEPA 163
Cdd:TIGR03410 92 VEENL--------------------LTGLAALPRRSRKIPDEiyelfpvlkemlgrrggdLSGGQQQQLAIARALVTRPK 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446943912 164 IILADEPTGALDSENSKNIIAALRNACDELGQTAVIV-THDPFVAAHADKVVFLLDGEVIHE 224
Cdd:TIGR03410 152 LLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVeQYLDFARELADRYYVMERGRVVAS 213
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-222 |
1.45e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 92.98 E-value: 1.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 22 ILKDINLQIQKGDFVCIMGASGSGKTTLLQL-----LGGLDIPSVGSIRVDGTEISTLKEKELALfrRHKIGFIFQQFNL 96
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrllELNEEARVEGEVRLFGRNIYSPDVDPIEV--RREVGMVFQYPNP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 97 IPVFNAEENVGLPLLLDNV--SQKKATVTANRLLELVGL----KGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEP 170
Cdd:PRK14267 97 FPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEP 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446943912 171 TGALDSENSKNIIAALRNACDELgqTAVIVTHDPFVAAH-ADKVVFLLDGEVI 222
Cdd:PRK14267 177 TANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARvSDYVAFLYLGKLI 227
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-203 |
2.91e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 92.46 E-value: 2.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 3 IIEIEGLEKSFDIG-DSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEkelal 81
Cdd:COG1101 1 MLELKNLSKTFNPGtVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPE----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 82 FRRHK-IGFIFQQ------FNL-IpvfnaEENvglpLLL-DNVSQK---KATVTANR------LLELVGLkGKEKHLPAQ 143
Cdd:COG1101 76 YKRAKyIGRVFQDpmmgtaPSMtI-----EEN----LALaYRRGKRrglRRGLTKKRrelfreLLATLGL-GLENRLDTK 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446943912 144 ---LSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHD 203
Cdd:COG1101 146 vglLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHN 208
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-224 |
3.56e-22 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 92.10 E-value: 3.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLekSFDIGdsKVKILKDINLQIQKGDFVCIMGASGSGK-----------TtllqllggldiPSVGSIRVDGTEIS 72
Cdd:COG4559 2 LEAENL--SVRLG--GRTLLDDVSLTLRPGELTAIIGPNGAGKstllklltgelT-----------PSSGEVRLNGRPLA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 73 TLKEKELALFR-----RHKIGFifqqfnliPvFNAEENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGG 147
Cdd:COG4559 67 AWSPWELARRRavlpqHSSLAF--------P-FTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 148 QQQRVAIARAFA-------NEPAIILADEPTGALDSENSKNIIAALRNACDElGQTAVIVTHDPFVAAH-ADKVVFLLDG 219
Cdd:COG4559 138 EQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQyADRILLLHQG 216
|
....*
gi 446943912 220 EVIHE 224
Cdd:COG4559 217 RLVAQ 221
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-222 |
6.18e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 94.39 E-value: 6.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 3 IIEIEGLEKSFDIGDSKVK-------ILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLdIPSVGSIRVDGTEISTLK 75
Cdd:PRK15134 275 LLDVEQLQVAFPIRKGILKrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRL-INSQGEIWFDGQPLHNLN 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 76 EKELALFRrHKIGFIFQQFN--LIPVFNAEENV--GL----PLLldNVSQKKATVTAnrLLELVGLKGKEKH-LPAQLSG 146
Cdd:PRK15134 354 RRQLLPVR-HRIQVVFQDPNssLNPRLNVLQIIeeGLrvhqPTL--SAAQREQQVIA--VMEEVGLDPETRHrYPAEFSG 428
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446943912 147 GQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRnACDELGQTAVI-VTHD-PFVAAHADKVVFLLDGEVI 222
Cdd:PRK15134 429 GQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLK-SLQQKHQLAYLfISHDlHVVRALCHQVIVLRQGEVV 505
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
11-221 |
6.33e-22 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 93.17 E-value: 6.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 11 KSFDigdsKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLG-GLDIPSvGSIRVDGTEISTLKEKElalfrrHKIGF 89
Cdd:PRK11000 11 KAYG----DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAgLEDITS-GDLFIGEKRMNDVPPAE------RGVGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 90 IFQQFNLIPVFNAEENVGLPLLLDNVSQKKATVTANRLLELVGLkgkeKHL----PAQLSGGQQQRVAIARAFANEPAII 165
Cdd:PRK11000 80 VFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQL----AHLldrkPKALSGGQRQRVAIGRTLVAEPSVF 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446943912 166 LADEPTGALDsenskniiAALR--------NACDELGQTAVIVTHDPFVA-AHADKVVFLLDGEV 221
Cdd:PRK11000 156 LLDEPLSNLD--------AALRvqmrieisRLHKRLGRTMIYVTHDQVEAmTLADKIVVLDAGRV 212
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
12-222 |
7.02e-22 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 94.26 E-value: 7.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 12 SFDIGDSKvKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfrRHKIGFIF 91
Cdd:PRK13657 341 SFSYDNSR-QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASL----RRNIAVVF 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 92 QQFNLipvFN--AEEN--VGLPlllD--NVSQKKATVTA----------NRLLELVGLKGKekhlpaQLSGGQQQRVAIA 155
Cdd:PRK13657 416 QDAGL---FNrsIEDNirVGRP---DatDEEMRAAAERAqahdfierkpDGYDTVVGERGR------QLSGGERQRLAIA 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446943912 156 RAFANEPAIILADEPTGALDSENSKNIIAALrnacDEL--GQTAVIVTHDPFVAAHADKVVFLLDGEVI 222
Cdd:PRK13657 484 RALLKDPPILILDEATSALDVETEAKVKAAL----DELmkGRTTFIIAHRLSTVRNADRILVFDNGRVV 548
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-226 |
8.89e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 94.00 E-value: 8.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 1 MNIIEIEGLEKSFDIGDSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLdIPS------VGSIRVDGTEISTL 74
Cdd:PRK15134 3 QPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRL-LPSppvvypSGDIRFHGESLLHA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 75 KEKELALFRRHKIGFIFQQ--FNLIPVFNAEENVGLPLLLD-NVSQKKATVTANRLLELVGLKGKEKHL---PAQLSGGQ 148
Cdd:PRK15134 82 SEQTLRGVRGNKIAMIFQEpmVSLNPLHTLEKQLYEVLSLHrGMRREAARGEILNCLDRVGIRQAAKRLtdyPHQLSGGE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446943912 149 QQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHD-PFVAAHADKVVFLLDGEVIHEHA 226
Cdd:PRK15134 162 RQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNlSIVRKLADRVAVMQNGRCVEQNR 240
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
23-216 |
8.97e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 89.60 E-value: 8.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 23 LKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEistlkekelalfrrhKIGFIFQQFNLIPVFNA 102
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGA---------------RVAYVPQRSEVPDSLPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 103 --EENVGL----PLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGALDS 176
Cdd:NF040873 73 tvRDLVAMgrwaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446943912 177 ENSKNIIAALRNACDElGQTAVIVTHDPFVAAHADKVVFL 216
Cdd:NF040873 153 ESRERIIALLAEEHAR-GATVVVVTHDLELVRRADPCVLL 191
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
3-229 |
1.07e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 91.31 E-value: 1.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 3 IIEIEGLEKSFDiGDSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalf 82
Cdd:PRK13642 4 ILEVENLVFKYE-KESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNL--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 83 rRHKIGFIFQQ-FNLIPVFNAEENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANE 161
Cdd:PRK13642 80 -RRKIGMVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446943912 162 PAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVAAHADKVVFLLDGEVIHEHAESK 229
Cdd:PRK13642 159 PEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSE 226
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-219 |
1.18e-21 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 92.09 E-value: 1.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 1 MNIIEIEGLEKSFDIGDSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPS---VGSIRVDGTEISTLKEK 77
Cdd:PRK09473 10 DALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 78 ELALFRRHKIGFIFQQ--FNLIPVFNAEENVGLPLLL-DNVSQKKATVTANRLLELVGLKGKEKHL---PAQLSGGQQQR 151
Cdd:PRK09473 90 ELNKLRAEQISMIFQDpmTSLNPYMRVGEQLMEVLMLhKGMSKAEAFEESVRMLDAVKMPEARKRMkmyPHEFSGGMRQR 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446943912 152 VAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHD-PFVAAHADKVVFLLDG 219
Cdd:PRK09473 170 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDlGVVAGICDKVLVMYAG 238
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-222 |
1.26e-21 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 93.71 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 3 IIEIEGLEKSF-DIGDSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVD-GTEISTLKEKELA 80
Cdd:TIGR03269 279 IIKVRNVSKRYiSVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 81 LFRRHK--IGFIFQQFNLIP----VFNAEENVGLPLLlDNVSQKKATVTanrlLELVGLKGKE-----KHLPAQLSGGQQ 149
Cdd:TIGR03269 359 GRGRAKryIGILHQEYDLYPhrtvLDNLTEAIGLELP-DELARMKAVIT----LKMVGFDEEKaeeilDKYPDELSEGER 433
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446943912 150 QRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHD-PFVAAHADKVVFLLDGEVI 222
Cdd:TIGR03269 434 HRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDmDFVLDVCDRAALMRDGKIV 507
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-224 |
1.66e-21 |
|
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: 89.20 E-value: 1.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFdigdSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKelalfr 83
Cdd:cd03268 1 LKTNDLTKTY----GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 RHKIGFIFQQFNLIPVFNAEENVGLPLLLDNVSQKKatvtANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPA 163
Cdd:cd03268 71 LRRIGALIEAPGFYPNLTARENLRLLARLLGIRKKR----IDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446943912 164 IILADEPTGALDSENSKNIIAALRNACDElGQTAVIVTHD-PFVAAHADKVVFLLDGEVIHE 224
Cdd:cd03268 147 LLILDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLlSEIQKVADRIGIINKGKLIEE 207
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-204 |
2.55e-21 |
|
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: 92.81 E-value: 2.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFDiGDSKVkiLKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfr 83
Cdd:TIGR02868 335 LELRDLSAGYP-GAPPV--LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEV---- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 RHKIGFIFQQFNLipvFNAEenvglplLLDNVSQKKATVT---ANRLLELVGLKGKEKHLP-----------AQLSGGQQ 149
Cdd:TIGR02868 408 RRRVSVCAQDAHL---FDTT-------VRENLRLARPDATdeeLWAALERVGLADWLRALPdgldtvlgeggARLSGGER 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446943912 150 QRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDelGQTAVIVTHDP 204
Cdd:TIGR02868 478 QRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALS--GRTVVLITHHL 530
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-224 |
2.58e-21 |
|
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: 88.97 E-value: 2.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFDigdsKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEIStlkeKELALFR 83
Cdd:cd03265 1 IEVENLVKKYG----DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV----REPREVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 RhKIGFIFQQFNLIPVFNAEENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPA 163
Cdd:cd03265 73 R-RIGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446943912 164 IILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVA-AHADKVVFLLDGEVIHE 224
Cdd:cd03265 152 VLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAE 213
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
23-224 |
2.81e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 90.22 E-value: 2.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 23 LKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEI-STLKEKELALFRRhKIGFIFQqFNLIPVFn 101
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITItHKTKDKYIRPVRK-RIGMVFQ-FPESQLF- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 102 aEENVGLPLLLD----NVSQKKATVTANRLLELVGLKGKEKHL-PAQLSGGQQQRVAIARAFANEPAIILADEPTGALDS 176
Cdd:PRK13646 100 -EDTVEREIIFGpknfKMNLDEVKNYAHRLLMDLGFSRDVMSQsPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446943912 177 ENSKNIIAALRNACDELGQTAVIVTHD-PFVAAHADKVVFLLDGEVIHE 224
Cdd:PRK13646 179 QSKRQVMRLLKSLQTDENKTIILVSHDmNEVARYADEVIVMKEGSIVSQ 227
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
2-224 |
4.37e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 89.43 E-value: 4.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 2 NIIEIEGLekSFDIGDSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELal 81
Cdd:PRK13648 6 SIIVFKNV--SFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKL-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 82 fRRHkIGFIFQ----QFNLIPVfnaEENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARA 157
Cdd:PRK13648 82 -RKH-IGIVFQnpdnQFVGSIV---KYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446943912 158 FANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVAAHADKVVFLLDGEVIHE 224
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKE 223
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-221 |
4.87e-21 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 90.67 E-value: 4.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 1 MNIIEIEGLEKSFDigdSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKEla 80
Cdd:PRK11650 1 MAGLKLQAVRKSYD---GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 81 lfrrHKIGFIFQQFNLIPVFNAEENVGLPLLLDNVSqkKATVT-----ANRLLELvglkgkEKHL---PAQLSGGQQQRV 152
Cdd:PRK11650 76 ----RDIAMVFQNYALYPHMSVRENMAYGLKIRGMP--KAEIEervaeAARILEL------EPLLdrkPRELSGGQRQRV 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446943912 153 AIARAFANEPAIILADEPTGALDsenskniiAALRNA-CDE-------LGQTAVIVTHDPfVAAH--ADKVVFLLDGEV 221
Cdd:PRK11650 144 AMGRAIVREPAVFLFDEPLSNLD--------AKLRVQmRLEiqrlhrrLKTTSLYVTHDQ-VEAMtlADRVVVMNGGVA 213
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
17-222 |
6.63e-21 |
|
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: 88.10 E-value: 6.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 17 DSKVKILKDINLQIQKGDFVCIMGASGSGK----TTLLQLLGGLDIPSvGSIRVDGTEISTlkekelALFRRHkIGFIFQ 92
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKttllDAISGRVEGGGTTS-GQILFNGQPRKP------DQFQKC-VAYVRQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 93 QFNLIPVFNAEE------NVGLPLLLDN-VSQKKATVTANRLLELVGLKGKekhLPAQLSGGQQQRVAIARAFANEPAII 165
Cdd:cd03234 89 DDILLPGLTVREtltytaILRLPRKSSDaIRKKRVEDVLLRDLALTRIGGN---LVKGISGGERRRVSIAVQLLWDPKVL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446943912 166 LADEPTGALDSENSKNIIAALRNACDelGQTAVIVT-HDP----FvaAHADKVVFLLDGEVI 222
Cdd:cd03234 166 ILDEPTSGLDSFTALNLVSTLSQLAR--RNRIVILTiHQPrsdlF--RLFDRILLLSSGEIV 223
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
16-213 |
8.23e-20 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 86.94 E-value: 8.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 16 GDSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALFRRhKIGFIFQqfN 95
Cdd:PRK11308 24 PERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQ-KIQIVFQ--N 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 96 LIPVFNAEENVGL----PLLLD---NVSQKKATVTAnrLLELVGLKGKE-KHLPAQLSGGQQQRVAIARAFANEPAIILA 167
Cdd:PRK11308 101 PYGSLNPRKKVGQileePLLINtslSAAERREKALA--MMAKVGLRPEHyDRYPHMFSGGQRQRIAIARALMLDPDVVVA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446943912 168 DEPTGALD-SENSK--NIIAALRnacDELGQTAVIVTHDPFVAAH-ADKV 213
Cdd:PRK11308 179 DEPVSALDvSVQAQvlNLMMDLQ---QELGLSYVFISHDLSVVEHiADEV 225
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
21-223 |
1.03e-19 |
|
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: 85.14 E-value: 1.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 21 KILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVG-SIRV-----DGTEISTLkekelalfrRHKIGFI---F 91
Cdd:COG1119 17 TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLfgerrGGEDVWEL---------RKRIGLVspaL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 92 QQFnlipvFNAEENV------------GLPLLLDNVSQKKatvtANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFA 159
Cdd:COG1119 88 QLR-----FPRDETVldvvlsgffdsiGLYREPTDEQRER----ARELLELLGLAHLADRPFGTLSQGEQRRVLIARALV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446943912 160 NEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHD-----PFVaahaDKVVFLLDGEVIH 223
Cdd:COG1119 159 KDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHveeipPGI----THVLLLKDGRVVA 223
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
2-224 |
1.10e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 86.05 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 2 NIIEIEGLEKSFDIGdskVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELAL 81
Cdd:PRK13636 4 YILKVEELNYNYSDG---THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 82 frRHKIGFIFQQFNLiPVFNAE--ENVGLPLLLDNVSQKKATVTANRLLELVG---LKGKEKHLpaqLSGGQQQRVAIAR 156
Cdd:PRK13636 81 --RESVGMVFQDPDN-QLFSASvyQDVSFGAVNLKLPEDEVRKRVDNALKRTGiehLKDKPTHC---LSFGQKKRVAIAG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446943912 157 AFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHD-PFVAAHADKVVFLLDGEVIHE 224
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDiDIVPLYCDNVFVMKEGRVILQ 223
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
3-222 |
2.74e-19 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 84.21 E-value: 2.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 3 IIEIEGLEKSFDigdsKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDG-----TEISTLKEK 77
Cdd:PRK11701 6 LLSVRGLTKLYG----PRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYALSEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 78 ELALFRRHKIGFIFQ--QFNLIPVFNAEENVGLPLLldNVSQK---KATVTANRLLELVGLKGKE-KHLPAQLSGGQQQR 151
Cdd:PRK11701 82 ERRRLLRTEWGFVHQhpRDGLRMQVSAGGNIGERLM--AVGARhygDIRATAGDWLERVEIDAARiDDLPTTFSGGMQQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446943912 152 VAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVAA-HADKVVFLLDGEVI 222
Cdd:PRK11701 160 LQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARlLAHRLLVMKQGRVV 231
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
4-222 |
3.27e-19 |
|
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: 83.54 E-value: 3.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFDI--------GDSK---------VKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRV 66
Cdd:cd03267 1 IEVSNLSKSYRVyskepgliGSLKslfkrkyreVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 67 DGTEISTLKEKELalfrrHKIGFIFQQFNL----IPVFNaeenvGLPLLLD--NVSQKKATVTANRLLELVGLkGKEKHL 140
Cdd:cd03267 81 AGLVPWKRRKKFL-----RRIGVVFGQKTQlwwdLPVID-----SFYLLAAiyDLPPARFKKRLDELSELLDL-EELLDT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 141 PA-QLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHD-PFVAAHADKVVFLLD 218
Cdd:cd03267 150 PVrQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYmKDIEALARRVLVIDK 229
|
....
gi 446943912 219 GEVI 222
Cdd:cd03267 230 GRLL 233
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-224 |
6.15e-19 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 84.41 E-value: 6.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 1 MNIIEIEGLEKSFDIGDSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLG-GLDIP---SVGSIRVDGTEISTLKE 76
Cdd:PRK11022 1 MALLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMgLIDYPgrvMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 77 KElalfRRHKIG----FIFQqfNLIPVFNAEENVGLPLL-----LDNVSQKKATVTANRLLELVGLKGKEKHL---PAQL 144
Cdd:PRK11022 81 KE----RRNLVGaevaMIFQ--DPMTSLNPCYTVGFQIMeaikvHQGGNKKTRRQRAIDLLNQVGIPDPASRLdvyPHQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 145 SGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHD-PFVAAHADKVVFLLDGEVIH 223
Cdd:PRK11022 155 SGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDlALVAEAAHKIIVMYAGQVVE 234
|
.
gi 446943912 224 E 224
Cdd:PRK11022 235 T 235
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-221 |
1.37e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 84.12 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 1 MNIIEIEGLEKSFdiGDskVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELA 80
Cdd:PRK09536 1 MPMIDVSDLSVEF--GD--TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 81 lfRRhkIGFIFQQFNLIPVFNAEENVGL---PLL--LDNVSQKKATVTaNRLLELVGLKGKEKHLPAQLSGGQQQRVAIA 155
Cdd:PRK09536 77 --RR--VASVPQDTSLSFEFDVRQVVEMgrtPHRsrFDTWTETDRAAV-ERAMERTGVAQFADRPVTSLSGGERQRVLLA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446943912 156 RAFANEPAIILADEPTGALDSENSKNIIAALRNACDElGQTAVIVTHDPFVAA-HADKVVFLLDGEV 221
Cdd:PRK09536 152 RALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAArYCDELVLLADGRV 217
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
21-227 |
1.45e-18 |
|
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: 84.87 E-value: 1.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 21 KILKDINLQIQKGDFVCIMGASGSGKTTllqllggldI---------PSVGSIRVDGTEISTLKEKELalfrRHKIGFIF 91
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKST---------LarllfrfydVTSGRILIDGQDIRDVTQASL----RAAIGIVP 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 92 QQFNLipvFNA--------------EENV--------------GLPllldnvsQKKATVTANRllelvGLKgkekhlpaq 143
Cdd:COG5265 439 QDTVL---FNDtiayniaygrpdasEEEVeaaaraaqihdfieSLP-------DGYDTRVGER-----GLK--------- 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 144 LSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNAcdELGQTAVIVTHDPFVAAHADKVVFLLDGEVIH 223
Cdd:COG5265 495 LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREV--ARGRTTLVIAHRLSTIVDADEILVLEAGRIVE 572
|
....*.
gi 446943912 224 E--HAE 227
Cdd:COG5265 573 RgtHAE 578
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
18-221 |
1.50e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 84.77 E-value: 1.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 18 SKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEK-----------ELALFR--- 83
Cdd:TIGR00958 492 PDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHylhrqvalvgqEPVLFSgsv 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 RHKIGFIFQQFNLIPVFNAEENVGLPLLLDNVSQKKATVtanrllelVGLKGkekhlpAQLSGGQQQRVAIARAFANEPA 163
Cdd:TIGR00958 572 RENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTE--------VGEKG------SQLSGGQKQRIAIARALVRKPR 637
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446943912 164 IILADEPTGALDSEnsknIIAALRNACDELGQTAVIVTHDPFVAAHADKVVFLLDGEV 221
Cdd:TIGR00958 638 VLILDEATSALDAE----CEQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSV 691
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
5-224 |
3.50e-18 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 80.39 E-value: 3.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 5 EIEGLEKSFDIGDSKVK--ILKDINLQIQKGDFVCIMGASGSGKttllqllggldipsvgsirvdgteiSTLKEkelALF 82
Cdd:COG2401 26 RVAIVLEAFGVELRVVEryVLRDLNLEIEPGEIVLIVGASGSGK-------------------------STLLR---LLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 83 RRHKiGFIFQQFNLIPVFNAEENVGlplLLDNVSQKKATVTANRLLELVGLKGKEKHL--PAQLSGGQQQRVAIARAFAN 160
Cdd:COG2401 78 GALK-GTPVAGCVDVPDNQFGREAS---LIDAIGRKGDFKDAVELLNAVGLSDAVLWLrrFKELSTGQKFRFRLALLLAE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446943912 161 EPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVAA--HADKVVFLLDGEVIHE 224
Cdd:COG2401 154 RPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDVIDdlQPDLLIFVGYGGVPEE 219
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
20-221 |
3.62e-18 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 80.59 E-value: 3.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 20 VKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfrRHKIGFIFQQfnliPV 99
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYL----HSKVSLVGQE----PV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 100 FNA---EENV--GLPLLLDNvSQKKATVTAN-----RLLEL-----VGLKGkekhlpAQLSGGQQQRVAIARAFANEPAI 164
Cdd:cd03248 99 LFArslQDNIayGLQSCSFE-CVKEAAQKAHahsfiSELASgydteVGEKG------SQLSGGQKQRVAIARALIRNPQV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446943912 165 ILADEPTGALDSENSKNIIAALRnaCDELGQTAVIVTHDPFVAAHADKVVFLLDGEV 221
Cdd:cd03248 172 LILDEATSALDAESEQQVQQALY--DWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-188 |
6.52e-18 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 79.89 E-value: 6.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFdigdSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELAlfr 83
Cdd:cd03218 1 LRAENLSKRY----GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 RHKIGFIFQQFNLIPVFNAEENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPA 163
Cdd:cd03218 74 RLGIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPK 153
|
170 180
....*....|....*....|....*...
gi 446943912 164 IILADEPTGALDS---ENSKNIIAALRN 188
Cdd:cd03218 154 FLLLDEPFAGVDPiavQDIQKIIKILKD 181
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-223 |
7.94e-18 |
|
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: 79.25 E-value: 7.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFdigdSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKekelalfr 83
Cdd:cd03269 1 LEVENVTKRF----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 RHKIGFIFQQFNLIPVFNAEENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPA 163
Cdd:cd03269 69 RNRIGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446943912 164 IILADEPTGALDSENS---KNIIAALRNAcdelGQTAVIVTHD-PFVAAHADKVVFLLDGEVIH 223
Cdd:cd03269 149 LLILDEPFSGLDPVNVellKDVIRELARA----GKTVILSTHQmELVEELCDRVLLLNKGRAVL 208
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
13-216 |
9.31e-18 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 79.37 E-value: 9.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 13 FDIGDSKvkILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfrRHKIGFIFQ 92
Cdd:PRK10247 15 YLAGDAK--ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIY----RQQVSYCAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 93 QfnliPVFNAE---ENVGLPLLLDNVSQKKATVTANrlLELVGLKGK--EKHLpAQLSGGQQQRVAIARAFANEPAIILA 167
Cdd:PRK10247 89 T----PTLFGDtvyDNLIFPWQIRNQQPDPAIFLDD--LERFALPDTilTKNI-AELSGGEKQRISLIRNLQFMPKVLLL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446943912 168 DEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVAAHADKVVFL 216
Cdd:PRK10247 162 DEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITL 210
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
22-219 |
1.56e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 81.78 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 22 ILKDINLQIQKGDFVCIMGASGSGKttllqllggldipsvgsirvdgteiSTLkekelalFR-----------------R 84
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGK-------------------------STL-------LRaiaglwpygsgriarpaG 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 85 HKIGFIFQQfNLIPVFNAEENVGLPLLLDNVSQkkATVTAnrLLELVGLK------GKEKHLPAQLSGGQQQRVAIARAF 158
Cdd:COG4178 426 ARVLFLPQR-PYLPLGTLREALLYPATAEAFSD--AELRE--ALEAVGLGhlaerlDEEADWDQVLSLGEQQRLAFARLL 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446943912 159 ANEPAIILADEPTGALDSENSKNIIAALRnacDELGQTAVI-VTHDPFVAAHADKVVFLLDG 219
Cdd:COG4178 501 LHKPDWLFLDEATSALDEENEAALYQLLR---EELPGTTVIsVGHRSTLAAFHDRVLELTGD 559
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-224 |
2.62e-17 |
|
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: 78.49 E-value: 2.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 1 MNIIEIEGLEKSFDigdsKVKILKDINLQIQKGDFVCIMGASGSGKttllqllggldiPSVGSIRVDGTEISTLKEKELA 80
Cdd:COG0410 1 MPMLEVENLHAGYG----GIHVLHGVSLEVEEGEIVALLGRNGAGKttllkaisgllpPRSGSIRFDGEDITGLPPHRIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 81 lfrRHKIGFIFQQFNLIPVFNAEEN--VGLPLLLDNVSQKKatvTANRLLEL--VgLKGKEKHLPAQLSGGQQQRVAIAR 156
Cdd:COG0410 77 ---RLGIGYVPEGRRIFPSLTVEENllLGAYARRDRAEVRA---DLERVYELfpR-LKERRRQRAGTLSGGEQQMLAIGR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446943912 157 AFANEPAIILADEPTGALdsenS----KNIIAALRNACDElGQTAVIVTHD-PFVAAHADKVVFLLDGEVIHE 224
Cdd:COG0410 150 ALMSRPKLLLLDEPSLGL----AplivEEIFEIIRRLNRE-GVTILLVEQNaRFALEIADRAYVLERGRIVLE 217
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
22-222 |
2.81e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 81.04 E-value: 2.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 22 ILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLdIPSVGSIRVDGTEistLKEKELALFRRHkIGFIFQqfnlipvfn 101
Cdd:PRK11174 365 LAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIE---LRELDPESWRKH-LSWVGQ--------- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 102 aeeNVGLPL--LLDNVSQKKATVT---ANRLLELVGLKGKEKHLP-----------AQLSGGQQQRVAIARAFANEPAII 165
Cdd:PRK11174 431 ---NPQLPHgtLRDNVLLGNPDASdeqLQQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQLL 507
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446943912 166 LADEPTGALDSENSKNIIAALRNAcdELGQTAVIVTH--DPFvaAHADKVVFLLDGEVI 222
Cdd:PRK11174 508 LLDEPTASLDAHSEQLVMQALNAA--SRRQTTLMVTHqlEDL--AQWDQIWVMQDGQIV 562
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-224 |
3.58e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 78.69 E-value: 3.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 1 MNIIEIEGLEKSFDigdSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELa 80
Cdd:PRK13652 1 MHLIETRDLCYSYS---GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREV- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 81 lfrRHKIGFIFQqfnlipvfNAEENVGLPLLLD-------NVSQKKATVtANRL---LELVGLKGKEKHLPAQLSGGQQQ 150
Cdd:PRK13652 77 ---RKFVGLVFQ--------NPDDQIFSPTVEQdiafgpiNLGLDEETV-AHRVssaLHMLGLEELRDRVPHHLSGGEKK 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446943912 151 RVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHD-PFVAAHADKVVFLLDGEVIHE 224
Cdd:PRK13652 145 RVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQlDLVPEMADYIYVMDKGRIVAY 219
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-202 |
4.26e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 79.08 E-value: 4.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 3 IIEIEGLEKSFdiGDSKVkiLKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEIStlkekELALF 82
Cdd:PRK13537 7 PIDFRNVEKRY--GDKLV--VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVP-----SRARH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 83 RRHKIGFIFQQFNLIPVFNAEENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEP 162
Cdd:PRK13537 78 ARQRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446943912 163 AIILADEPTGALDSENSKNIIAALRNACDElGQTAVIVTH 202
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTH 196
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-222 |
5.15e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 79.12 E-value: 5.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 3 IIEIEGLEKSFDIGDS-KVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRV----------DGTEI 71
Cdd:PRK13631 21 ILRVKNLYCVFDEKQEnELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 72 STLKEKELALFR--RHKIGFIFQqFNLIPVF--NAEENVGL-PLLLdNVSQKKATVTANRLLELVGLKgkEKHL---PAQ 143
Cdd:PRK13631 101 TNPYSKKIKNFKelRRRVSMVFQ-FPEYQLFkdTIEKDIMFgPVAL-GVKKSEAKKLAKFYLNKMGLD--DSYLersPFG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 144 LSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDElGQTAVIVTHD-PFVAAHADKVVFLLDGEVI 222
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTmEHVLEVADEVIVMDKGKIL 255
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
11-226 |
5.30e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 78.10 E-value: 5.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 11 KSFDIGDSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELAlfRRhkIGFI 90
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA--RR--IGLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 91 FQQFNLIPVFNAEENVG------LPLLLDNVSQKKATVtaNRLLELVGLkgkeKHLPAQ----LSGGQQQRVAIARAFAN 160
Cdd:PRK10253 87 AQNATTPGDITVQELVArgryphQPLFTRWRKEDEEAV--TKAMQATGI----THLADQsvdtLSGGQRQRAWIAMVLAQ 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446943912 161 EPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVAA-HADKVVFLLDGEVIHEHA 226
Cdd:PRK10253 161 ETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACrYASHLIALREGKIVAQGA 227
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
21-222 |
7.32e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 78.13 E-value: 7.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 21 KILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEI-STLKE-KELALFRRhKIGFIFQqFNLIP 98
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpANLKKiKEVKRLRK-EIGLVFQ-FPEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 99 VFNA--EENVGLPLLLDNVSQKKATVTANRLLELVGL-KGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGALD 175
Cdd:PRK13645 103 LFQEtiEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446943912 176 SENSKNIIAALRNACDELGQTAVIVTHD-PFVAAHADKVVFLLDGEVI 222
Cdd:PRK13645 183 PKGEEDFINLFERLNKEYKKRIIMVTHNmDQVLRIADEVIVMHEGKVI 230
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-203 |
8.43e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 79.51 E-value: 8.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 19 KVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALFRRhKIGFIFQQ--FNL 96
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRR-DIQFIFQDpyASL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 97 IPVFNAEENVGLPLLLDNVSQKKATvtANR---LLELVGLKGKEK-HLPAQLSGGQQQRVAIARAFANEPAIILADEPTG 172
Cdd:PRK10261 415 DPRQTVGDSIMEPLRVHGLLPGKAA--AARvawLLERVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVIIADEAVS 492
|
170 180 190
....*....|....*....|....*....|.
gi 446943912 173 ALDSENSKNIIAALRNACDELGQTAVIVTHD 203
Cdd:PRK10261 493 ALDVSIRGQIINLLLDLQRDFGIAYLFISHD 523
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-225 |
1.09e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 78.92 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 3 IIEIEGLEKSFDigdsKVKILKDINLQIQKGDFVCIMGASGSGKttllqllggldipSV-------------GSIRVDGT 69
Cdd:COG3845 5 ALELRGITKRFG----GVVANDDVSLTVRPGEIHALLGENGAGK-------------STlmkilyglyqpdsGEILIDGK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 70 E--ISTLKEkelAlfRRHKIGFIFQQFNLIPVFNAEENVGL---PLLLDNVSQKKAtvtANRLLELvglkGKEKHLP--- 141
Cdd:COG3845 68 PvrIRSPRD---A--IALGIGMVHQHFMLVPNLTVAENIVLglePTKGGRLDRKAA---RARIREL----SERYGLDvdp 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 142 ----AQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDElGQTAVIVTHD-PFVAAHADKVVFL 216
Cdd:COG3845 136 dakvEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAE-GKSIIFITHKlREVMAIADRVTVL 214
|
....*....
gi 446943912 217 LDGEVIHEH 225
Cdd:COG3845 215 RRGKVVGTV 223
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
23-224 |
1.36e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 77.33 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 23 LKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGteISTLKEKELALFRRhKIGFIFQ----QFNLIP 98
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG--IDTGDFSKLQGIRK-LVGIVFQnpetQFVGRT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 99 VfnaEENVGL---PLLLDNVSQKKatvTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGALD 175
Cdd:PRK13644 95 V---EEDLAFgpeNLCLPPIEIRK---RVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446943912 176 SENSKNIIAALRNaCDELGQTAVIVTHDPFVAAHADKVVFLLDGEVIHE 224
Cdd:PRK13644 169 PDSGIAVLERIKK-LHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLE 216
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-188 |
2.98e-16 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 75.45 E-value: 2.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 1 MNIIEIEGLEKSFdigdSKVKILKDINLQIQKGDFVCIMGASGSGK-----------TtllqllggldiPSVGSIRVDGT 69
Cdd:COG1137 1 MMTLEAENLVKSY----GKRTVVKDVSLEVNQGEIVGLLGPNGAGKtttfymivglvK-----------PDSGRIFLDGE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 70 EISTLkekelALFRRHK--IGF------IFQqfNLipvfNAEENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLP 141
Cdd:COG1137 66 DITHL-----PMHKRARlgIGYlpqeasIFR--KL----TVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKA 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446943912 142 AQLSGGQQQRVAIARAFANEPAIILADEPTGALDS---ENSKNIIAALRN 188
Cdd:COG1137 135 YSLSGGERRRVEIARALATNPKFILLDEPFAGVDPiavADIQKIIRHLKE 184
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-222 |
3.70e-16 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 74.84 E-value: 3.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFDIGDSKVkiLKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfr 83
Cdd:cd03244 3 IEFKNVSLRYRPNLPPV--LKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 RHKIGFIFQ---------QFNLIP--------VFNAEENVGLpllldnvsqkKATVTAnrllELVGLKGKEKHLPAQLSG 146
Cdd:cd03244 77 RSRISIIPQdpvlfsgtiRSNLDPfgeysdeeLWQALERVGL----------KEFVES----LPGGLDTVVEEGGENLSV 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446943912 147 GQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDelGQTAVIVTHDPFVAAHADKVVFLLDGEVI 222
Cdd:cd03244 143 GQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFK--DCTVLTIAHRLDTIIDSDRILVLDKGRVV 216
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-224 |
4.39e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 75.90 E-value: 4.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 15 IGDSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDiPSVGSIRVDGTEI----STLKEKELALFRRhKIGFI 90
Cdd:PRK14271 29 LGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMN-DKVSGYRYSGDVLlggrSIFNYRDVLEFRR-RVGML 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 91 FQQFNLIPVFNAEENVGLPLLLDNVSQKKATVTANRLLELVGL----KGKEKHLPAQLSGGQQQRVAIARAFANEPAIIL 166
Cdd:PRK14271 107 FQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLL 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446943912 167 ADEPTGALDSENSKNIIAALRNACDELgqTAVIVTHDPFVAAH-ADKVVFLLDGEVIHE 224
Cdd:PRK14271 187 LDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARiSDRAALFFDGRLVEE 243
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-202 |
4.98e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 76.41 E-value: 4.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFdiGDSKVkiLKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTlkEKELAlfr 83
Cdd:PRK13536 42 IDLAGVSKSY--GDKAV--VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA--RARLA--- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 RHKIGFIFQQFNLIPVFNAEENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPA 163
Cdd:PRK13536 113 RARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQ 192
|
170 180 190
....*....|....*....|....*....|....*....
gi 446943912 164 IILADEPTGALDSENSKNIIAALRnACDELGQTAVIVTH 202
Cdd:PRK13536 193 LLILDEPTTGLDPHARHLIWERLR-SLLARGKTILLTTH 230
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
4-220 |
5.55e-16 |
|
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: 74.04 E-value: 5.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFDIGDSKVK-ILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTeistlkekelalf 82
Cdd:cd03250 1 ISVEDASFTWDSGEQETSfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 83 rrhkIGFIFQQfnliP-VFNA--EENV--GLPLllDnvSQK-KATVTANRL---LEL--------VGLKGkekhlpAQLS 145
Cdd:cd03250 68 ----IAYVSQE----PwIQNGtiRENIlfGKPF--D--EERyEKVIKACALepdLEIlpdgdlteIGEKG------INLS 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 146 GGQQQRVAIARAFANEPAIILADEPTGALDSENSKNII-----AALRNacdelGQTAVIVTHDPFVAAHADKVVFLLDGE 220
Cdd:cd03250 130 GGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFencilGLLLN-----NKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
23-227 |
6.73e-16 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 76.98 E-value: 6.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 23 LKDINLQIQKGDFVCIMGASGSGKTTLLQLLGG-LDIPSvGSIRVDGTEistLKEKELALFRRHkIGFIFQQFNLipvFN 101
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRfYDIDE-GEILLDGHD---LRDYTLASLRNQ-VALVSQNVHL---FN 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 102 -------------------AEENVGLPLLLDNVSQKKatvtaNRLLELVGLKGkekhlpAQLSGGQQQRVAIARA-FANE 161
Cdd:PRK11176 431 dtianniayarteqysreqIEEAARMAYAMDFINKMD-----NGLDTVIGENG------VLLSGGQRQRIAIARAlLRDS 499
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 162 PAIILaDEPTGALDSENSKNIIAALrnacDEL--GQTAVIVTHDPFVAAHADKVVFLLDGEVIH--EHAE 227
Cdd:PRK11176 500 PILIL-DEATSALDTESERAIQAAL----DELqkNRTSLVIAHRLSTIEKADEILVVEDGEIVErgTHAE 564
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-220 |
8.26e-16 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 72.10 E-value: 8.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFDigdsKVKILKDINLQIQKGDFVCIMGASGSGKttllqllggldipsvgsirvdgteiSTLkekelalfr 83
Cdd:cd03221 1 IELENLSKTYG----GKLLLKDISLTINPGDRIGLVGRNGAGK-------------------------STL--------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 rhkigfifqqfnlipvfnaeenvgLPLLLDNVSQKKATVTANRLLELVglkgkekHLPaQLSGGQQQRVAIARAFANEPA 163
Cdd:cd03221 43 ------------------------LKLIAGELEPDEGIVTWGSTVKIG-------YFE-QLSGGEKMRLALAKLLLENPN 90
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446943912 164 IILADEPTGALDSENskniIAALRNACDELGQTAVIVTHDP-FVAAHADKVVFLLDGE 220
Cdd:cd03221 91 LLLLDEPTNHLDLES----IEALEEALKEYPGTVILVSHDRyFLDQVATKIIELEDGK 144
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-223 |
8.58e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 76.26 E-value: 8.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 3 IIEIEGLEKSFDigdsKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVdGTEIstlkekelalf 82
Cdd:COG0488 315 VLELEGLSKSYG----DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 83 rrhKIGFiFQQFNLipVFNAEENVglpllLDNVSQ---KKATVTANRLLELVGLKGKEKHLP-AQLSGGQQQRVAIARAF 158
Cdd:COG0488 379 ---KIGY-FDQHQE--ELDPDKTV-----LDELRDgapGGTEQEVRGYLGRFLFSGDDAFKPvGVLSGGEKARLALAKLL 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446943912 159 ANEPAIILADEPTGALDSENskniIAALRNACDELGQTAVIVTHDP-FVAAHADKVVFLLDGEVIH 223
Cdd:COG0488 448 LSPPNVLLLDEPTNHLDIET----LEALEEALDDFPGTVLLVSHDRyFLDRVATRILEFEDGGVRE 509
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
23-221 |
1.06e-15 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 72.85 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 23 LKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKElalFRRHKIGFI---FQQFNLIPV 99
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRD---AIRAGIAYVpedRKREGLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 100 FNAEENVGLPLLLdnvsqkkatvtanrllelvglkgkekhlpaqlSGGQQQRVAIARAFANEPAIILADEPTGALDSENS 179
Cdd:cd03215 93 LSVAENIALSSLL--------------------------------SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAK 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446943912 180 KNIIAALRNACDElGqTAVIV--THDPFVAAHADKVVFLLDGEV 221
Cdd:cd03215 141 AEIYRLIRELADA-G-KAVLLisSELDELLGLCDRILVMYEGRI 182
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
22-222 |
1.37e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 75.85 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 22 ILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSV---GSIRVDGTEISTLKEKELAlfrrhkiGFIFQQFNLIP 98
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVkgsGSVLLNGMPIDAKEMRAIS-------AYVQQDDLFIP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 99 VFNAEENVGLPLLL---DNVSQKKATVTANRLLELVGLK-------GKEKHLPAqLSGGQQQRVAIARAFANEPAIILAD 168
Cdd:TIGR00955 113 TLTVREHLMFQAHLrmpRRVTKKEKRERVDEVLQALGLRkcantriGVPGRVKG-LSGGERKRLAFASELLTDPPLLFCD 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446943912 169 EPTGALDSENSKNIIAALRNACDElGQTAVIVTHDPfvAAHA----DKVVFLLDGEVI 222
Cdd:TIGR00955 192 EPTSGLDSFMAYSVVQVLKGLAQK-GKTIICTIHQP--SSELfelfDKIILMAEGRVA 246
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
4-227 |
1.41e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 73.97 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFDigdskVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSV----GSIRVDGTEIStlkekeL 79
Cdd:PRK10418 5 IELRNIALQAA-----QPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGVrqtaGRVLLDGKPVA------P 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 80 ALFRRHKIGFIFQQ----FNliPVFNAEENVGLPLLLDNVSQKKATVTAnrLLELVGLKGKEKHL---PAQLSGGQQQRV 152
Cdd:PRK10418 74 CALRGRKIATIMQNprsaFN--PLHTMHTHARETCLALGKPADDATLTA--ALEAVGLENAARVLklyPFEMSGGMLQRM 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446943912 153 AIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVAAH-ADKVVFLLDGEVIhEHAE 227
Cdd:PRK10418 150 MIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARlADDVAVMSHGRIV-EQGD 224
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
23-222 |
1.91e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 73.34 E-value: 1.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 23 LKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLdIPSVGSIRVDGTEISTLKEKELALFRrhkiGFIFQQ----FnLIP 98
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAELARHR----AYLSQQqsppF-AMP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 99 VFNAeenvgLPLLL-DNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAF------AN-EPAIILADEP 170
Cdd:COG4138 86 VFQY-----LALHQpAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwptINpEGQLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446943912 171 TGALDsenskniIA------ALRNACDELGQTAVIVTHD-PFVAAHADKVVFLLDGEVI 222
Cdd:COG4138 161 MNSLD-------VAqqaaldRLLRELCQQGITVVMSSHDlNHTLRHADRVWLLKQGKLV 212
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
3-253 |
2.30e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 73.51 E-value: 2.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 3 IIEIEGLeksfDIGDSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELAlf 82
Cdd:PRK11231 2 TLRTENL----TVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 83 rRHkIGFIFQQfNLIPV-FNAEENVG------LPL----------LLDNVSQKKATVT-ANRLLElvglkgkekhlpaQL 144
Cdd:PRK11231 76 -RR-LALLPQH-HLTPEgITVRELVAygrspwLSLwgrlsaednaRVNQAMEQTRINHlADRRLT-------------DL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 145 SGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDElGQTAVIVTHDPFVAA-HADKVVFLLDGEVIH 223
Cdd:PRK11231 140 SGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASrYCDHLVVLANGHVMA 218
|
250 260 270
....*....|....*....|....*....|
gi 446943912 224 EHAeskgwkfrniPQQVIhIQEIMNRHFKV 253
Cdd:PRK11231 219 QGT----------PEEVM-TPGLLRTVFDV 237
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-202 |
2.59e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 75.21 E-value: 2.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFdigdSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELAlfr 83
Cdd:PRK09700 6 ISMAGIGKSF----GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAA--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 RHKIGFIFQQFNLIPVFNAEENVGLPLLL-------DNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIAR 156
Cdd:PRK09700 79 QLGIGIIYQELSVIDELTVLENLYIGRHLtkkvcgvNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAK 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446943912 157 AFANEPAIILADEPTGALDSENSKNIIAALRNACDElGQTAVIVTH 202
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISH 203
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-222 |
5.96e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 73.98 E-value: 5.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLekSFDIGDSKVkILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfr 83
Cdd:PRK10790 341 IDIDNV--SFAYRDDNL-VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL---- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 RHKIGFIFQQfnliPVFNAE---ENV--GLPLLLDNVSQKKATVtanRLLELV-GL-KGKEKHLPAQ---LSGGQQQRVA 153
Cdd:PRK10790 414 RQGVAMVQQD----PVVLADtflANVtlGRDISEEQVWQALETV---QLAELArSLpDGLYTPLGEQgnnLSVGQKQLLA 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446943912 154 IARAFANEPAIILADEPTGALDSENSKNIIAALRNACDElgQTAVIVTHDPFVAAHADKVVFLLDGEVI 222
Cdd:PRK10790 487 LARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAHRLSTIVEADTILVLHRGQAV 553
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-189 |
9.05e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 71.46 E-value: 9.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 1 MNIIEIEGLEKSFdigdSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELA 80
Cdd:PRK10895 1 MATLTAKNLAKAY----KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 81 lfrRHKIGFIFQQFNLIPVFNAEENVGLPL-LLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFA 159
Cdd:PRK10895 77 ---RRGIGYLPQEASIFRRLSVYDNLMAVLqIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALA 153
|
170 180 190
....*....|....*....|....*....|...
gi 446943912 160 NEPAIILADEPTGALDS---ENSKNIIAALRNA 189
Cdd:PRK10895 154 ANPKFILLDEPFAGVDPisvIDIKRIIEHLRDS 186
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
25-202 |
1.26e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 70.60 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 25 DINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELA--LFRRHKIGfifqqfnLIPVFNA 102
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQdlLYLGHQPG-------IKTELTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 103 EENVGLPLLLDNVSQKKATVTAnrlLELVGLKGKEkHLPA-QLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKN 181
Cdd:PRK13538 92 LENLRFYQRLHGPGDDEALWEA---LAQVGLAGFE-DVPVrQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVAR 167
|
170 180
....*....|....*....|.
gi 446943912 182 IIAALRNACDElGQTAVIVTH 202
Cdd:PRK13538 168 LEALLAQHAEQ-GGMVILTTH 187
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
23-215 |
1.56e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 71.35 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 23 LKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLD--IPSV---GSIRVDGTEISTLKEKELALFRRhkIGFIFQQFNLI 97
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNdlIPGFrveGKVTFHGKNLYAPDVDPVEVRRR--IGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 98 P-------VFNAEENvGLPLLLDNVSQKKATVTAnrLLELVglKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEP 170
Cdd:PRK14243 104 PksiydniAYGARIN-GYKGDMDELVERSLRQAA--LWDEV--KDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446943912 171 TGALDSenskniIAALR--NACDELGQ--TAVIVTHDPFVAAH-ADKVVF 215
Cdd:PRK14243 179 CSALDP------ISTLRieELMHELKEqyTIIIVTHNMQQAARvSDMTAF 222
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-220 |
1.68e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 71.22 E-value: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFDIGdskvKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDiPSVGSIRVDG-TEI--STLKEKELA 80
Cdd:PRK14258 8 IKVNNLSFYYDTQ----KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMN-ELESEVRVEGrVEFfnQNIYERRVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 81 LFR-RHKIGFIFQQFNLIPVfNAEENV--GLPLL-------LDNVSQkkATVTANRLLELVglKGKEKHLPAQLSGGQQQ 150
Cdd:PRK14258 83 LNRlRRQVSMVHPKPNLFPM-SVYDNVayGVKIVgwrpkleIDDIVE--SALKDADLWDEI--KHKIHKSALDLSGGQQQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446943912 151 RVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHD-PFVAAHADKVVFLLDGE 220
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNlHQVSRLSDFTAFFKGNE 228
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
2-222 |
5.82e-14 |
|
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: 68.44 E-value: 5.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 2 NIIEIEGLeksfdiGDSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSV---GSIRVDGTEIstlkeKE 78
Cdd:cd03233 8 NISFTTGK------GRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPY-----KE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 79 LALFRRHKIgfifqqfnlipVFNAEENVGLPLLldnvsqkkatvTANRLLELVG-LKGKEkhLPAQLSGGQQQRVAIARA 157
Cdd:cd03233 77 FAEKYPGEI-----------IYVSEEDVHFPTL-----------TVRETLDFALrCKGNE--FVRGISGGERKRVSIAEA 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446943912 158 FANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVAAHA--DKVVFLLDGEVI 222
Cdd:cd03233 133 LVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASDEIYDlfDKVLVLYEGRQI 199
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-226 |
6.89e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 70.80 E-value: 6.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 3 IIEIEGLEKSFdigdSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEIS--TLKEKELA 80
Cdd:PRK10762 4 LLQLKGIDKAF----PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfnGPKSSQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 81 lfrrhKIGFIFQQFNLIPVFNAEENVGLPLLLDN----VSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIAR 156
Cdd:PRK10762 80 -----GIGIIHQELNLIPQLTIAENIFLGREFVNrfgrIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446943912 157 AFANEPAIILADEPTGAL-DSENskniiAALRNACDEL---GQTAVIVTH---DPFVAahADKVVFLLDGEVIHEHA 226
Cdd:PRK10762 155 VLSFESKVIIMDEPTDALtDTET-----ESLFRVIRELksqGRGIVYISHrlkEIFEI--CDDVTVFRDGQFIAERE 224
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
22-212 |
7.02e-14 |
|
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: 68.15 E-value: 7.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 22 ILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKelalfRRHKIGFIFQQFNLIPVFN 101
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDE-----PHENILYLGHLPGLKPELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 102 AEENvglpLLLDNVSQKKATVTANRLLELVGLKGKEkHLPA-QLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSK 180
Cdd:TIGR01189 90 ALEN----LHFWAAIHGGAQRTIEDALAAVGLTGFE-DLPAaQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVA 164
|
170 180 190
....*....|....*....|....*....|..
gi 446943912 181 NIIAALRNACdELGQTAVIVTHDPFVAAHADK 212
Cdd:TIGR01189 165 LLAGLLRAHL-ARGGIVLLTTHQDLGLVEARE 195
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
3-213 |
7.21e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 70.12 E-value: 7.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 3 IIEIEGLEKSFDIGDSK---------VKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEIST 73
Cdd:PRK15079 8 LLEVADLKVHFDIKDGKqwfwqppktLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 74 LKEKELALFRRhKIGFIFQQ--FNLIPVFNAEENVGLPLLLDNVSQKKATVTaNRLLEL---VGLKGKE-KHLPAQLSGG 147
Cdd:PRK15079 88 MKDDEWRAVRS-DIQMIFQDplASLNPRMTIGEIIAEPLRTYHPKLSRQEVK-DRVKAMmlkVGLLPNLiNRYPHEFSGG 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446943912 148 QQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVAAH-ADKV 213
Cdd:PRK15079 166 QCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHiSDRV 232
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-224 |
1.06e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 69.37 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 3 IIEIEGLEKSFDigdsKVKILKDINLQIQKGDFVCIMGASGSGK-----------TtllqllggldiPSVGSIRVDGTEI 71
Cdd:COG4152 1 MLELKGLTKRFG----DKTAVDDVSFTVPKGEIFGLLGPNGAGKtttiriilgilA-----------PDSGEVLWDGEPL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 72 STLKekelalfrRHKIGFIfqqfnliPvfnaEE-------NVGLPLL----LDNVSQKKATVTANRLLELVGLKGKEKHL 140
Cdd:COG4152 66 DPED--------RRRIGYL-------P----EErglypkmKVGEQLVylarLKGLSKAEAKRRADEWLERLGLGDRANKK 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 141 PAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENS---KNIIAALRNAcdelGQTAVIVTHD-PFVAAHADKVVFL 216
Cdd:COG4152 127 VEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVellKDVIRELAAK----GTTVIFSSHQmELVEELCDRIVII 202
|
....*...
gi 446943912 217 LDGEVIHE 224
Cdd:COG4152 203 NKGRKVLS 210
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-224 |
1.93e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 69.28 E-value: 1.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 3 IIEIEGLeksfdigdSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKElALf 82
Cdd:COG1129 256 VLEVEGL--------SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRD-AI- 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 83 rRHKIGFI---FQQFNLIPVFNAEENVGLPLLLDN-----VSQKKATVTANRLLELVGLKGKEKHLPAQ-LSGGQQQRVA 153
Cdd:COG1129 326 -RAGIAYVpedRKGEGLVLDLSIRENITLASLDRLsrgglLDRRRERALAEEYIKRLRIKTPSPEQPVGnLSGGNQQKVV 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446943912 154 IARAFANEPAIILADEPT-----GAldsensKN-IIAALRNACDElGqTAVIVTHD--PFVAAHADKVVFLLDGEVIHE 224
Cdd:COG1129 405 LAKWLATDPKVLILDEPTrgidvGA------KAeIYRLIRELAAE-G-KAVIVISSelPELLGLSDRILVMREGRIVGE 475
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
4-224 |
2.81e-13 |
|
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: 67.17 E-value: 2.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFDIGDS------------------KVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIR 65
Cdd:cd03220 1 IELENVSKSYPTYKGgssslkklgilgrkgevgEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 66 VDGTEISTLkekELALFrrhkigfifqqFNliPVFNAEENVGLPLLLDNVSQKKATVTANRLLELVGLkGKEKHLP-AQL 144
Cdd:cd03220 81 VRGRVSSLL---GLGGG-----------FN--PELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSEL-GDFIDLPvKTY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 145 SGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDElGQTAVIVTHDP-FVAAHADKVVFLLDGEVIH 223
Cdd:cd03220 144 SSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPsSIKRLCDRALVLEKGKIRF 222
|
.
gi 446943912 224 E 224
Cdd:cd03220 223 D 223
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
21-222 |
7.55e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 66.57 E-value: 7.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 21 KILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALfrRHKIGFIFQQFNLiPVF 100
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLAL--RQQVATVFQDPEQ-QIF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 101 NAEENVGLPLLLDNVSQKKATVT--ANRLLELVGLKGKeKHLPAQ-LSGGQQQRVAIARAFANEPAIILADEPTGALDSE 177
Cdd:PRK13638 92 YTDIDSDIAFSLRNLGVPEAEITrrVDEALTLVDAQHF-RHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446943912 178 NSKNIIAALRNACDElGQTAVIVTHD-PFVAAHADKVVFLLDGEVI 222
Cdd:PRK13638 171 GRTQMIAIIRRIVAQ-GNHVIISSHDiDLIYEISDAVYVLRQGQIL 215
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
25-222 |
7.95e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 67.21 E-value: 7.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 25 DINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTeisTLKEKELALF----RRHkIGFIFQQFNLIPVF 100
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGR---VLFDAEKGIClppeKRR-IGYVFQDARLFPHY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 101 NAEENvglplLLDNVSqKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSK 180
Cdd:PRK11144 92 KVRGN-----LRYGMA-KSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKR 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446943912 181 NIIAALRNACDELGQTAVIVTH--DPFVAAhADKVVFLLDGEVI 222
Cdd:PRK11144 166 ELLPYLERLAREINIPILYVSHslDEILRL-ADRVVVLEQGKVK 208
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
16-200 |
1.84e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 66.59 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 16 GDSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKElalFRRHKIGFI---FQ 92
Cdd:COG3845 267 DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRE---RRRLGVAYIpedRL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 93 QFNLIPVFNAEENvglpLLLDN-----------VSQKKATVTANRLLELVGLKGKEKHLPA-QLSGGQQQRVAIARAFAN 160
Cdd:COG3845 344 GRGLVPDMSVAEN----LILGRyrrppfsrggfLDRKAIRAFAEELIEEFDVRTPGPDTPArSLSGGNQQKVILARELSR 419
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446943912 161 EPAIILADEPTGALDSENSKNIIAALRNACDElGqTAVIV 200
Cdd:COG3845 420 DPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-G-AAVLL 457
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
22-222 |
2.13e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 65.23 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 22 ILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGlDIPS---------VGSIRVDGTEISTLKEKELALFRrhkiGFIFQ 92
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG-DLTGggaprgarvTGDVTLNGEPLAAIDAPRLARLR----AVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 93 QFNLIPVFNAEENVGL---PllldNVSQKKATV-----TANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFAN---- 160
Cdd:PRK13547 91 AAQPAFAFSAREIVLLgryP----HARRAGALThrdgeIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpp 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446943912 161 -----EPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVAA-HADKVVFLLDGEVI 222
Cdd:PRK13547 167 hdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAArHADRIAMLADGAIV 234
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
3-222 |
3.02e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 64.81 E-value: 3.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 3 IIEIEGLEKSFD-----IGDSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEK 77
Cdd:PRK15112 4 LLEVRNLSKTFRyrtgwFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 78 elalFRRHKIGFIFQ--QFNLIPVFNAEENVGLPLLLD-NVSQKKATVTANRLLELVGLKGKE-KHLPAQLSGGQQQRVA 153
Cdd:PRK15112 84 ----YRSQRIRMIFQdpSTSLNPRQRISQILDFPLRLNtDLEPEQREKQIIETLRQVGLLPDHaSYYPHMLAPGQKQRLG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 154 IARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVAAH-ADKVVFLLDGEVI 222
Cdd:PRK15112 160 LARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVV 229
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
22-224 |
9.66e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 63.27 E-value: 9.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 22 ILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELAlfrrHKIGFIFQQFNLIPVFN 101
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFA----RKVAYLPQQLPAAEGMT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 102 AEENVGL-------PLLLDNVSQKKATVTAnrlLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGAL 174
Cdd:PRK10575 102 VRELVAIgrypwhgALGRFGAADREKVEEA---ISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSAL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446943912 175 DSENSKNIIAALRNACDELGQTAVIVTHDPFVAA-HADKVVFLLDGEVIHE 224
Cdd:PRK10575 179 DIAHQVDVLALVHRLSQERGLTVIAVLHDINMAArYCDYLVALRGGEMIAQ 229
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-222 |
1.10e-11 |
|
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: 62.16 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFDigdsKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSV--GSIRVDGTEISTLKEKELAl 81
Cdd:cd03217 1 LEIKDLHVSVG----GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVteGEILFKGEDITDLPPEERA- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 82 frRHKIGFIFQqfnlIPVfnAEENVGLPLLLDNVSqkkatvtanrllelVGlkgkekhlpaqLSGGQQQRVAIARAFANE 161
Cdd:cd03217 76 --RLGIFLAFQ----YPP--EIPGVKNADFLRYVN--------------EG-----------FSGGEKKRNEILQLLLLE 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446943912 162 PAIILADEPTGALDSENSK---NIIAALRNAcdelGQTAVIVTHDPFVAAH--ADKVVFLLDGEVI 222
Cdd:cd03217 123 PDLAILDEPDSGLDIDALRlvaEVINKLREE----GKSVLIITHYQRLLDYikPDRVHVLYDGRIV 184
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-203 |
1.42e-11 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 63.39 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 1 MNIIEIEGLEKSFDIGDSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLggldipsVGSI-----------RVDGT 69
Cdd:COG4170 1 MPLLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAI-------CGITkdnwhvtadrfRWNGI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 70 EISTLKEKELALFRRHKIGFIFQ--QFNLIPvfnaEENVGlPLLLDNVSQKKATVT-----------ANRLLELVGLKGK 136
Cdd:COG4170 74 DLLKLSPRERRKIIGREIAMIFQepSSCLDP----SAKIG-DQLIEAIPSWTFKGKwwqrfkwrkkrAIELLHRVGIKDH 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446943912 137 EKHL---PAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSeNSKNIIAALRNACDELGQTAV-IVTHD 203
Cdd:COG4170 149 KDIMnsyPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMES-TTQAQIFRLLARLNQLQGTSIlLISHD 218
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-202 |
1.56e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.78 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 20 VKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKElALfrRHKIGFIFQQFNLIPV 99
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTA-AL--AAGVAIIYQELHLVPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 100 FNAEENV---GLPLLLDNVSQKKATVTANRLLELVGLK----GKEKHlpaqLSGGQQQRVAIARAFANEPAIILADEPTG 172
Cdd:PRK11288 94 MTVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDidpdTPLKY----LSIGQRQMVEIAKALARNARVIAFDEPTS 169
|
170 180 190
....*....|....*....|....*....|...
gi 446943912 173 AL---DSENSKNIIAALRnacDElGQTAVIVTH 202
Cdd:PRK11288 170 SLsarEIEQLFRVIRELR---AE-GRVILYVSH 198
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-229 |
1.73e-11 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 63.28 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 1 MNIIEIEGLEKSFDIGDSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLL--GGLDIPSVGS--IRVDGTEISTLKE 76
Cdd:PRK15093 1 MPLLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAIcgVTKDNWRVTAdrMRFDDIDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 77 KELALFRRHKIGFIFQ--QFNLIPvfnaEENVGLPLLLD--------------NVSQKKATvtanRLLELVGLKGKE--- 137
Cdd:PRK15093 81 RERRKLVGHNVSMIFQepQSCLDP----SERVGRQLMQNipgwtykgrwwqrfGWRKRRAI----ELLHRVGIKDHKdam 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 138 KHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVAAH-ADKVVFL 216
Cdd:PRK15093 153 RSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQwADKINVL 232
|
250
....*....|...
gi 446943912 217 LDGEVIhEHAESK 229
Cdd:PRK15093 233 YCGQTV-ETAPSK 244
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
23-203 |
1.91e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 62.59 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 23 LKDINLQIQKGDFVCIMGASGSGKTTLLQLLggldipsVGSIRVDGTEISTLKEKELALFRRHKIGFIFQqfnlipvfNA 102
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKAL-------MGFVRLASGKISILGQPTRQALQKNLVAYVPQ--------SE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 103 EENVGLPLLLDNV----------------SQKKATVTAnrLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIIL 166
Cdd:PRK15056 88 EVDWSFPVLVEDVvmmgryghmgwlrrakKRDRQIVTA--ALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVIL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 446943912 167 ADEPTGALDSENSKNIIAALRNACDElGQTAVIVTHD 203
Cdd:PRK15056 166 LDEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHN 201
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-226 |
1.94e-11 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 61.66 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFdiGDSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfr 83
Cdd:cd03369 7 IEVENLSVRY--APDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 RHKIGFIFQQfnlipvfnaeenvglPLLLDnvsqkkATVTANrlLELVG----------LKGKEKHLpaQLSGGQQQRVA 153
Cdd:cd03369 81 RSSLTIIPQD---------------PTLFS------GTIRSN--LDPFDeysdeeiygaLRVSEGGL--NLSQGQRQLLC 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446943912 154 IARAFANEPAIILADEPTGALDSENSKNIIAALRNACDelGQTAVIVTHDPFVAAHADKVVFLLDGEVIhEHA 226
Cdd:cd03369 136 LARALLKRPRVLVLDEATASIDYATDALIQKTIREEFT--NSTILTIAHRLRTIIDYDKILVMDAGEVK-EYD 205
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
3-222 |
2.13e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 63.27 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 3 IIEIEGLEKSFdigdSKVKILKDINLQIQKGDFVCIMGASGSGKttllqllggldipSV---------------GSIRVD 67
Cdd:NF040905 1 ILEMRGITKTF----PGVKALDDVNLSVREGEIHALCGENGAGK-------------STlmkvlsgvyphgsyeGEILFD 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 68 GTEI--STLKEKElalfrRHKIGFIFQQFNLIPVFNAEENvglpLLLDNVSQKK-------ATVTANRLLELVGLKGKEK 138
Cdd:NF040905 64 GEVCrfKDIRDSE-----ALGIVIIHQELALIPYLSIAEN----IFLGNERAKRgvidwneTNRRARELLAKVGLDESPD 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 139 HLPAQLSGGQQQRVAIARAFANEPAIILADEPTGAL---DSENSKNIIAALRnacdELGQTAVIVTHD-PFVAAHADKVV 214
Cdd:NF040905 135 TLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALneeDSAALLDLLLELK----AQGITSIIISHKlNEIRRVADSIT 210
|
....*...
gi 446943912 215 FLLDGEVI 222
Cdd:NF040905 211 VLRDGRTI 218
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
144-220 |
2.60e-11 |
|
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: 60.63 E-value: 2.60e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446943912 144 LSGGQQQRVAIARAFANEPAIILADEPTGALDSENSkniiAALRNACDELGQTAVIVTHDPFVAAHADKVVfLLDGE 220
Cdd:cd03223 92 LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESE----DRLYQLLKELGITVISVGHRPSLWKFHDRVL-DLDGE 163
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-221 |
2.79e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 63.43 E-value: 2.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 22 ILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfrRHKIGFIFQQfnliPVFN 101
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDL----RFKITIIPQD----PVLF 1372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 102 AEEnvgLPLLLDNVSQ--KKATVTAnrlLELVGLKGKEKHLPAQ-----------LSGGQQQRVAIARAFANEPAIILAD 168
Cdd:TIGR00957 1373 SGS---LRMNLDPFSQysDEEVWWA---LELAHLKTFVSALPDKldhecaeggenLSVGQRQLVCLARALLRKTKILVLD 1446
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446943912 169 EPTGALDSENSKNIIAALRNACDELgqTAVIVTHDPFVAAHADKVVFLLDGEV 221
Cdd:TIGR00957 1447 EATAAVDLETDNLIQSTIRTQFEDC--TVLTIAHRLNTIMDYTRVIVLDKGEV 1497
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
131-214 |
4.91e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 62.74 E-value: 4.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 131 VGLKGKekhlpaQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVAAHA 210
Cdd:PTZ00265 1352 VGPYGK------SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRS 1425
|
....
gi 446943912 211 DKVV 214
Cdd:PTZ00265 1426 DKIV 1429
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-216 |
5.47e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 60.90 E-value: 5.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 1 MNIIEIEGLEKSFdiGDSKVkiLKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIrvdgteistlkEKELA 80
Cdd:PRK09544 2 TSLVSLENVSVSF--GQRRV--LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRNGK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 81 LfrrhKIGFIFQQFNLIPVfnaeenvgLPLLLDNVSQKKATVTANRLLELVGlKGKEKHL---PAQ-LSGGQQQRVAIAR 156
Cdd:PRK09544 67 L----RIGYVPQKLYLDTT--------LPLTVNRFLRLRPGTKKEDILPALK-RVQAGHLidaPMQkLSGGETQRVLLAR 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446943912 157 AFANEPAIILADEPTGALDSENS---KNIIAALRNacdELGQTAVIVTHD-PFVAAHADKVVFL 216
Cdd:PRK09544 134 ALLNRPQLLVLDEPTQGVDVNGQvalYDLIDQLRR---ELDCAVLMVSHDlHLVMAKTDEVLCL 194
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-223 |
5.58e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 61.64 E-value: 5.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 3 IIEIEGLEKSFDIGDSK-----------------VKILKDINLQIQKGDFVCIMGASGSGKTTLlqllggldI------- 58
Cdd:COG4586 1 IIEVENLSKTYRVYEKEpglkgalkglfrreyreVEAVDDISFTIEPGEIVGFIGPNGAGKSTT--------Ikmltgil 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 59 -PSVGSIRVDGtEISTLKEKELAlfrrHKIGFIFQQFN-LIPvfnaeenvGLPLL--------LDNVSQKKATVTANRLL 128
Cdd:COG4586 73 vPTSGEVRVLG-YVPFKRRKEFA----RRIGVVFGQRSqLWW--------DLPAIdsfrllkaIYRIPDAEYKKRLDELV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 129 ELVGLKGKeKHLPA-QLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPF-V 206
Cdd:COG4586 140 ELLDLGEL-LDTPVrQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDdI 218
|
250
....*....|....*..
gi 446943912 207 AAHADKVVFLLDGEVIH 223
Cdd:COG4586 219 EALCDRVIVIDHGRIIY 235
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
26-222 |
6.20e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 60.72 E-value: 6.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 26 INLQIQKGDFVCIMGASGSGKTTLLQLLGGLdIPSVGSIRVDGTEISTLKEKELALFRrhkiGFIFQQFN---LIPVFNA 102
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELARHR----AYLSQQQTppfAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 103 eenvgLPLLLDNVSQKKATVTA-NRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAF-----ANEPA--IILADEPTGAL 174
Cdd:PRK03695 90 -----LTLHQPDKTRTEAVASAlNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPAgqLLLLDEPMNSL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446943912 175 DSENsKNIIAALRNACDELGQTAVIVTHD-PFVAAHADKVVFLLDGEVI 222
Cdd:PRK03695 165 DVAQ-QAALDRLLSELCQQGIAVVMSSHDlNHTLRHADRVWLLKQGKLL 212
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
2-222 |
6.81e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 60.48 E-value: 6.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 2 NIIEIEGLEKSFDIGDSK------------------VKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGS 63
Cdd:COG1134 3 SMIEVENVSKSYRLYHEPsrslkelllrrrrtrreeFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 64 IRVDGTeISTLkekeLALfrrhkiGFIFQqfnliPVFNAEENVGLPLLLDNVSQKKATVTANRLLELVGLkGKEKHLPAQ 143
Cdd:COG1134 83 VEVNGR-VSAL----LEL------GAGFH-----PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAEL-GDFIDQPVK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 144 -LSGGQQQRVAIARAFANEPAIILADEPTGALDS---ENSKNIIAALRNAcdelGQTAVIVTHDP-FVAAHADKVVFLLD 218
Cdd:COG1134 146 tYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAafqKKCLARIRELRES----GRTVIFVSHSMgAVRRLCDRAIWLEK 221
|
....
gi 446943912 219 GEVI 222
Cdd:COG1134 222 GRLV 225
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
12-204 |
1.36e-10 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 59.18 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 12 SFDIGDSKVK--ILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSV--GSIRVDGteistlKEKELALFRRhkI 87
Cdd:cd03232 10 NYTVPVKGGKrqLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGVitGEILING------RPLDKNFQRS--T 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 88 GFIFQQfnliPVFNAEENVGLPLLLdnvsqkkatvTANrllelvgLKGkekhlpaqLSGGQQQRVAIARAFANEPAIILA 167
Cdd:cd03232 82 GYVEQQ----DVHSPNLTVREALRF----------SAL-------LRG--------LSVEQRKRLTIGVELAAKPSILFL 132
|
170 180 190
....*....|....*....|....*....|....*..
gi 446943912 168 DEPTGALDSENSKNIIAALRNACDElGQTAVIVTHDP 204
Cdd:cd03232 133 DEPTSGLDSQAAYNIVRFLKKLADS-GQAILCTIHQP 168
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
22-220 |
1.42e-10 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 60.26 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 22 ILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGteistlkekelalfrrhKIGFIfQQFNLIPVFN 101
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-----------------RISFS-SQFSWIMPGT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 102 AEENVGLPLLLDNVsQKKATVTANRLLE-LVGLKGKEKHLPAQ----LSGGQQQRVAIARAFANEPAIILADEPTGALDS 176
Cdd:cd03291 114 IKENIIFGVSYDEY-RYKSVVKACQLEEdITKFPEKDNTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446943912 177 ENSKNIIAALrnACDELG-QTAVIVTHDPFVAAHADKVVFLLDGE 220
Cdd:cd03291 193 FTEKEIFESC--VCKLMAnKTRILVTSKMEHLKKADKILILHEGS 235
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-221 |
1.43e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 61.33 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 21 KILKDINLQIQKGDFVCIMGASGSGKttllqllggldipsvgsirvdgteiSTLKEKELALFRRHK--------IGFIFQ 92
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGK-------------------------STLLQSLLSQFEISEgrvwaersIAYVPQ 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 93 Q---FNL-----IPVFNAEENVGLPLLLdNVSQKKATVT--ANRLLELVGLKGkekhlpAQLSGGQQQRVAIARA-FANE 161
Cdd:PTZ00243 729 QawiMNAtvrgnILFFDEEDAARLADAV-RVSQLEADLAqlGGGLETEIGEKG------VNLSGGQKARVSLARAvYANR 801
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446943912 162 PAIILaDEPTGALDSENSKNII-----AALRnacdelGQTAVIVTHDPFVAAHADKVVFLLDGEV 221
Cdd:PTZ00243 802 DVYLL-DDPLSALDAHVGERVVeecflGALA------GKTRVLATHQVHVVPRADYVVALGDGRV 859
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-203 |
1.52e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 60.85 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 6 IEGLEKSFDigdsKVKILKDINLQIQKGDFVCIMGASGSGKttllqllggldipS------VGSIRVDGTEISTLKEKel 79
Cdd:COG0488 1 LENLSKSFG----GRPLLDDVSLSINPGDRIGLVGRNGAGK-------------StllkilAGELEPDSGEVSIPKGL-- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 80 alfrrhKIGFIFQQFNLIPVFNAEENV--GLPLLLDNVSQKKATVT------------------------------ANRL 127
Cdd:COG0488 62 ------RIGYLPQEPPLDDDLTVLDTVldGDAELRALEAELEELEAklaepdedlerlaelqeefealggweaearAEEI 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446943912 128 LELVGLKGKEKHLP-AQLSGGQQQRVAIARAFANEPAIILADEPTGALDSEnsknIIAALRNACDELGQTAVIVTHD 203
Cdd:COG0488 136 LSGLGFPEEDLDRPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLE----SIEWLEEFLKNYPGTVLVVSHD 208
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
22-219 |
1.71e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 61.08 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 22 ILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGtEIS-----------TLKEKELalfrrhkIGFI 90
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-RISfspqtswimpgTIKDNII-------FGLS 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 91 FQQFNLIPVFNA---EENVGLPLLLDNVSQKKATVTanrllelvglkgkekhlpaqLSGGQQQRVAIARAFANEPAIILA 167
Cdd:TIGR01271 513 YDEYRYTSVIKAcqlEEDIALFPEKDKTVLGEGGIT--------------------LSGGQRARISLARAVYKDADLYLL 572
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446943912 168 DEPTGALDSENSKNIIAalRNACDEL-GQTAVIVTHDPFVAAHADKVVFLLDG 219
Cdd:TIGR01271 573 DSPFTHLDVVTEKEIFE--SCLCKLMsNKTRILVTSKLEHLKKADKILLLHEG 623
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-222 |
2.33e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 60.33 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 3 IIEIEGLEKSFDigdsKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQllggldIPS--------VGSIRVDGTEI--S 72
Cdd:PRK13549 5 LLEMKNITKTFG----GVKALDNVSLKVRAGEIVSLCGENGAGKSTLMK------VLSgvyphgtyEGEIIFEGEELqaS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 73 TLKEKElalfrRHKIGFIFQQFNLIPVFNAEENVGL---PLLLDNVSQKKATVTANRLLELVGLkGKEKHLP-AQLSGGQ 148
Cdd:PRK13549 75 NIRDTE-----RAGIAIIHQELALVKELSVLENIFLgneITPGGIMDYDAMYLRAQKLLAQLKL-DINPATPvGNLGLGQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446943912 149 QQRVAIARAFANEPAIILADEPTGAL-DSENS--KNIIAALRNAcdelGQTAVIVTHD-PFVAAHADKVVFLLDGEVI 222
Cdd:PRK13549 149 QQLVEIAKALNKQARLLILDEPTASLtESETAvlLDIIRDLKAH----GIACIYISHKlNEVKAISDTICVIRDGRHI 222
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
23-229 |
2.57e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 60.37 E-value: 2.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 23 LKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEIStlkEKELALFRRHkIGFIFQQFNLIP-VFN 101
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT---AEQPEDYRKL-FSAVFTDFHLFDqLLG 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 102 AEENVGLPLLLDN-----VSQKKATVTANRLLELvglkgkekhlpaQLSGGQQQRVAIARAFANEPAIILADEPTGALDS 176
Cdd:PRK10522 415 PEGKPANPALVEKwlerlKMAHKLELEDGRISNL------------KLSKGQKKRLALLLALAEERDILLLDEWAADQDP 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446943912 177 ENSKNIIAALRNACDELGQTAVIVTHDPFVAAHADKVVFLLDGEVIHEHAESK 229
Cdd:PRK10522 483 HFRREFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSELTGEER 535
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
18-219 |
3.25e-10 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 58.50 E-value: 3.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 18 SKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALFRRHKIGFIFQQFNLI 97
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 98 pvfNA--EENV--GLPLlldNVSQKKATVTANRLLELVGL--KGKEKHLPAQ---LSGGQQQRVAIARAFANEPAIILAD 168
Cdd:cd03290 92 ---NAtvEENItfGSPF---NKQRYKAVTDACSLQPDIDLlpFGDQTEIGERginLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446943912 169 EPTGALDSENSKNII-AALRNACDELGQTAVIVTHDPFVAAHADKVVFLLDG 219
Cdd:cd03290 166 DPFSALDIHLSDHLMqEGILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
18-220 |
3.79e-10 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 58.57 E-value: 3.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 18 SKVKILKDINLQIQKGDF-----VCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALFR---RHKIGF 89
Cdd:cd03237 5 TMKKTLGEFTLEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKADYEgtvRDLLSS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 90 IFQQFNLIPVFNAEenVGLPLLLDnvsqkkatvtanRLLElvglkgkeKHLPaQLSGGQQQRVAIARAFANEPAIILADE 169
Cdd:cd03237 85 ITKDFYTHPYFKTE--IAKPLQIE------------QILD--------REVP-ELSGGELQRVAIAACLSKDADIYLLDE 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446943912 170 PTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVAAH-ADKV-VFllDGE 220
Cdd:cd03237 142 PSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYlADRLiVF--EGE 192
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
19-174 |
3.98e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 58.35 E-value: 3.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 19 KVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEIStlkEKELALFRRHKIGFIFQQFNLIP 98
Cdd:PRK11614 17 KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDIT---DWQTAKIMREAVAIVPEGRRVFS 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446943912 99 VFNAEENVGLPLLLDNVSQKKATVTanRLLELVGLKGKEKHLPA-QLSGGQQQRVAIARAFANEPAIILADEPTGAL 174
Cdd:PRK11614 94 RMTVEENLAMGGFFAERDQFQERIK--WVYELFPRLHERRIQRAgTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL 168
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
17-224 |
4.84e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 59.75 E-value: 4.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 17 DSKVK--ILKDINLQIQKGDFVCIMGASGSGKTtllqllggldipSVGSIRVDgtEISTLKEKELALfrRHKIGFIFQqf 94
Cdd:PLN03130 625 DSKAErpTLSNINLDVPVGSLVAIVGSTGEGKT------------SLISAMLG--ELPPRSDASVVI--RGTVAYVPQ-- 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 95 nLIPVFNA--EENV--GLPLllDNVSQKKAT-VTA-NRLLEL--------VGLKGkekhlpAQLSGGQQQRVAIARAFAN 160
Cdd:PLN03130 687 -VSWIFNAtvRDNIlfGSPF--DPERYERAIdVTAlQHDLDLlpggdlteIGERG------VNISGGQKQRVSMARAVYS 757
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446943912 161 EPAIILADEPTGALDSENSKNIIaalrNAC--DELGQ-TAVIVTHDPFVAAHADKVVFLLDGEVIHE 224
Cdd:PLN03130 758 NSDVYIFDDPLSALDAHVGRQVF----DKCikDELRGkTRVLVTNQLHFLSQVDRIILVHEGMIKEE 820
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
26-203 |
6.20e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 58.08 E-value: 6.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 26 INLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELAlfrRHKIGFIFQQFNLIPVFNAEEN 105
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIA---RMGVVRTFQHVRLFREMTVIEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 106 vglpLLLDNVSQKKATVTANRL-------------------LELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIIL 166
Cdd:PRK11300 101 ----LLVAQHQQLKTGLFSGLLktpafrraesealdraatwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILM 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446943912 167 ADEPTGAL---DSENSKNIIAALRnacDELGQTAVIVTHD 203
Cdd:PRK11300 177 LDEPAAGLnpkETKELDELIAELR---NEHNVTVLLIEHD 213
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
4-224 |
6.43e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 59.22 E-value: 6.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 4 IEIEGLEKSFDIGDSKvKILKDINLQIQKGDFVCIMGASGSGKTTLlqllggldipsvgsIRVDGTEISTLKEKELALfr 83
Cdd:PLN03232 615 ISIKNGYFSWDSKTSK-PTLSDINLEIPVGSLVAIVGGTGEGKTSL--------------ISAMLGELSHAETSSVVI-- 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 84 RHKIGFIFQqfnlIP-VFNA--EENVGLPLLLDNVSQKKAT-VTA---------NRLLELVGLKGkekhlpAQLSGGQQQ 150
Cdd:PLN03232 678 RGSVAYVPQ----VSwIFNAtvRENILFGSDFESERYWRAIdVTAlqhdldllpGRDLTEIGERG------VNISGGQKQ 747
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446943912 151 RVAIARAFANEPAIILADEPTGALDSENSKNIIaalrNAC--DEL-GQTAVIVTHDPFVAAHADKVVFLLDGEVIHE 224
Cdd:PLN03232 748 RVSMARAVYSNSDIYIFDDPLSALDAHVAHQVF----DSCmkDELkGKTRVLVTNQLHFLPLMDRIILVSEGMIKEE 820
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
128-204 |
9.38e-10 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 56.73 E-value: 9.38e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446943912 128 LELVGLKGKEkHLP-AQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACdELGQTAVIVTHDP 204
Cdd:cd03231 110 LARVGLNGFE-DRPvAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHC-ARGGMVVLTTHQD 185
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
5-224 |
1.46e-09 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 57.00 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 5 EIEGLekSFDIGDskVKILKDINLQIQKGDFVCIMGASGSGKttllqllggldipSV---------------GSIRVDGT 69
Cdd:COG0396 2 EIKNL--HVSVEG--KEILKGVNLTIKPGEVHAIMGPNGSGK-------------STlakvlmghpkyevtsGSILLDGE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 70 EISTLKEKELAlfrRHKIGFIFQQfnliPV---------F-------NAEENVGLPLLLDNVSQKkatvtanrlLELVGL 133
Cdd:COG0396 65 DILELSPDERA---RAGIFLAFQY----PVeipgvsvsnFlrtalnaRRGEELSAREFLKLLKEK---------MKELGL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 134 KGK--EKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGALDsenskniIAALR---NACDEL---GQTAVIVTHDP- 204
Cdd:COG0396 129 DEDflDRYVNEGFSGGEKKRNEILQMLLLEPKLAILDETDSGLD-------IDALRivaEGVNKLrspDRGILIITHYQr 201
|
250 260
....*....|....*....|...
gi 446943912 205 ---FVaaHADKVVFLLDGEVIHE 224
Cdd:COG0396 202 ildYI--KPDFVHVLVDGRIVKS 222
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
26-218 |
1.91e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 58.10 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 26 INLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKElalfrRHKIGFIFQQFNLIPVFNAEEN 105
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAV-----RQSLGMCPQHNILFHHLTVAEH 1023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 106 VGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAA 185
Cdd:TIGR01257 1024 ILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDL 1103
|
170 180 190
....*....|....*....|....*....|...
gi 446943912 186 LRNAcdELGQTAVIVTHdpfvaaHADKVVFLLD 218
Cdd:TIGR01257 1104 LLKY--RSGRTIIMSTH------HMDEADLLGD 1128
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
144-220 |
3.32e-09 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 54.89 E-value: 3.32e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446943912 144 LSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVAAHADKVVFLLDGE 220
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEGE 148
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
21-221 |
6.99e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 55.95 E-value: 6.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 21 KILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKE-----KELALF--RRHKIGFiFQQ 93
Cdd:PRK09700 277 KKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPldavkKGMAYIteSRRDNGF-FPN 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 94 FNL---IPVFNAEENVGLPLLLDNVSQKKATVTANRLLELVGLK--GKEKHLpAQLSGGQQQRVAIARAFANEPAIILAD 168
Cdd:PRK09700 356 FSIaqnMAISRSLKDGGYKGAMGLFHEVDEQRTAENQRELLALKchSVNQNI-TELSGGNQQKVLISKWLCCCPEVIIFD 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446943912 169 EPTGALDSENSKNIIAALRNACDElGQTAVIVTHD-PFVAAHADKVVFLLDGEV 221
Cdd:PRK09700 435 EPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSElPEIITVCDRIAVFCEGRL 487
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
15-216 |
1.19e-08 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 53.10 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 15 IGDSKVKILKDINLQIQKGDFVCIMGASGSGKTtllqllggldipsvgSIRVDG--TEISTLKEKELALFRRHKIGFIFQ 92
Cdd:cd03238 3 VSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKS---------------TLVNEGlyASGKARLISFLPKFSRNKLIFIDQ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 93 QFNLIpvfnaeeNVGLPLLldnvsqkkatvTANRLLelvglkgkekhlpAQLSGGQQQRVAIARAFANEP--AIILADEP 170
Cdd:cd03238 68 LQFLI-------DVGLGYL-----------TLGQKL-------------STLSGGELQRVKLASELFSEPpgTLFILDEP 116
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446943912 171 TGALDSENSKNIIAALRNACDeLGQTAVIVTHDPFVAAHADKVVFL 216
Cdd:cd03238 117 STGLHQQDINQLLEVIKGLID-LGNTVILIEHNLDVLSSADWIIDF 161
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-209 |
1.71e-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: 54.56 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 2 NIIEIEGLEKSFdiGDskvKIL-KDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEistlkekela 80
Cdd:TIGR03719 321 KVIEAENLTKAF--GD---KLLiDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETV---------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 81 lfrrhKIGFIFQQF-NLIPVFNAEENV--GLPLLLDNvsqkKATVTANRLLELVGLKGKEKH-LPAQLSGGQQQRVAIAR 156
Cdd:TIGR03719 386 -----KLAYVDQSRdALDPNKTVWEEIsgGLDIIKLG----KREIPSRAYVGRFNFKGSDQQkKVGQLSGGERNRVHLAK 456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446943912 157 AFANEPAIILADEPTGALDSENskniIAALRNACDELGQTAVIVTHDPF----VAAH 209
Cdd:TIGR03719 457 TLKSGGNVLLLDEPTNDLDVET----LRALEEALLNFAGCAVVISHDRWfldrIATH 509
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-222 |
1.90e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 54.45 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 3 IIEIEGLEKSFDigdsKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSV--GSIRVDGTEI--STLKEKE 78
Cdd:TIGR02633 1 LLEMKGIVKTFG----GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLkaSNIRDTE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 79 lalfrRHKIGFIFQQFNLIPVFNAEENV--GLPLLLDNVSQKKATVT--ANRLLELVGLKGKEKHLP-AQLSGGQQQRVA 153
Cdd:TIGR02633 77 -----RAGIVIIHQELTLVPELSVAENIflGNEITLPGGRMAYNAMYlrAKNLLRELQLDADNVTRPvGDYGGGQQQLVE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 154 IARAFANEPAIILADEPTGALDSENSKNIIAALRNaCDELGQTAVIVTHD-PFVAAHADKVVFLLDGEVI 222
Cdd:TIGR02633 152 IAKALNKQARLLILDEPSSSLTEKETEILLDIIRD-LKAHGVACVYISHKlNEVKAVCDTICVIRDGQHV 220
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
128-204 |
2.29e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 52.95 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 128 LELVGLKGKEkHLPAQ-LSGGQQQRVAIAR-AFANEPAIILaDEPTGALDSENSK---NIIAALRNAcdelGQTAVIVTH 202
Cdd:PRK13539 112 LEAVGLAPLA-HLPFGyLSAGQKRRVALARlLVSNRPIWIL-DEPTAALDAAAVAlfaELIRAHLAQ----GGIVIAATH 185
|
..
gi 446943912 203 DP 204
Cdd:PRK13539 186 IP 187
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-221 |
3.41e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.90 E-value: 3.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 3 IIEIEGLEKSFdigdSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKelalf 82
Cdd:PRK15439 11 LLCARSISKQY----SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 83 RRHKIG--FIFQQFNLIPVFNAEENV--GLPllldnvsqkKATVTANRLLELVGLKGKEKHLPAQ---LSGGQQQRVAIA 155
Cdd:PRK15439 82 KAHQLGiyLVPQEPLLFPNLSVKENIlfGLP---------KRQASMQKMKQLLAALGCQLDLDSSagsLEVADRQIVEIL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446943912 156 RAFANEPAIILADEPTGALDSENSKNIIAALRnACDELGQTAVIVTHD-PFVAAHADKVVFLLDGEV 221
Cdd:PRK15439 153 RGLMRDSRILILDEPTASLTPAETERLFSRIR-ELLAQGVGIVFISHKlPEIRQLADRISVMRDGTI 218
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
22-207 |
4.77e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 52.16 E-value: 4.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 22 ILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALFRRHKIGfifqqfnLIPVFN 101
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLPG-------LKADLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 102 AEENVGLpllLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSEN--- 178
Cdd:PRK13543 99 TLENLHF---LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGitl 175
|
170 180 190
....*....|....*....|....*....|
gi 446943912 179 -SKNIIAALRNacdelGQTAVIVTHDPFVA 207
Cdd:PRK13543 176 vNRMISAHLRG-----GGAALVTTHGAYAA 200
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
5-203 |
6.16e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.03 E-value: 6.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 5 EIEGLekSFDIGDSKvkILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVdGTEIstlkekELALFRR 84
Cdd:PRK11147 321 EMENV--NYQIDGKQ--LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKL------EVAYFDQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 85 HKIgfifqqfNLIPvfnaEENVglpllLDNVSQKKATVTANrllelvglkGKEKHL----------PAQ-------LSGG 147
Cdd:PRK11147 390 HRA-------ELDP----EKTV-----MDNLAEGKQEVMVN---------GRPRHVlgylqdflfhPKRamtpvkaLSGG 444
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446943912 148 QQQRVAIARAFANEPAIILADEPTGALDSENskniIAALRNACDELGQTAVIVTHD 203
Cdd:PRK11147 445 ERNRLLLARLFLKPSNLLILDEPTNDLDVET----LELLEELLDSYQGTVLLVSHD 496
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
142-203 |
6.92e-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: 53.02 E-value: 6.92e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446943912 142 AQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENskniIAALRNACDELGQTAVIVTHD 203
Cdd:TIGR03719 160 TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES----VAWLERHLQEYPGTVVAVTHD 217
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-221 |
7.05e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 53.03 E-value: 7.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 23 LKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTeistlkekelalfrrhkIGFIFQQfNLIPVFNA 102
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-----------------VAYVPQQ-AWIQNDSL 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 103 EENV--GLPLlldNVSQKKATVTANRLL---EL--------VGLKGkekhlpAQLSGGQQQRVAIARAFANEPAIILADE 169
Cdd:TIGR00957 716 RENIlfGKAL---NEKYYQQVLEACALLpdlEIlpsgdrteIGEKG------VNLSGGQKQRVSLARAVYSNADIYLFDD 786
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446943912 170 PTGALDSENSKNIIAALRNACDEL-GQTAVIVTHDPFVAAHADKVVFLLDGEV 221
Cdd:TIGR00957 787 PLSAVDAHVGKHIFEHVIGPEGVLkNKTRILVTHGISYLPQVDVIIVMSGGKI 839
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
22-224 |
7.35e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 52.96 E-value: 7.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 22 ILKDINLQIQKGDFVCIMGASGSGKTTLLQLLggldipsVGSIR---VDGTEISTLKEKELALFRRhkIGFIFQQFNLIP 98
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNAL-------AGRIQgnnFTGTILANNRKPTKQILKR--TGFVTQDDILYP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 99 VFNAEEN---VGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQ-----LSGGQQQRVAIARAFANEPAIILADEP 170
Cdd:PLN03211 154 HLTVRETlvfCSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEP 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446943912 171 TGALDSENSKNIIAALRNACDElGQTAVIVTHDPF--VAAHADKVVFLLDGEVIHE 224
Cdd:PLN03211 234 TSGLDATAAYRLVLTLGSLAQK-GKTIVTSMHQPSsrVYQMFDSVLVLSEGRCLFF 288
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
17-222 |
8.86e-08 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 51.83 E-value: 8.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 17 DSKVK-ILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfrRHKIGFIFQ--- 92
Cdd:cd03288 30 ENNLKpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTL----RSRLSIILQdpi 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 93 ------QFNLIPvfnaeenvglpllldnvsqkKATVTANRL---LELVGLKGKEKHLPAQL-----------SGGQQQRV 152
Cdd:cd03288 106 lfsgsiRFNLDP--------------------ECKCTDDRLweaLEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLF 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446943912 153 AIARAFANEPAIILADEPTGALD--SEN--SKNIIAALRNacdelgQTAVIVTHDPFVAAHADKVVFLLDGEVI 222
Cdd:cd03288 166 CLARAFVRKSSILIMDEATASIDmaTENilQKVVMTAFAD------RTVVTIAHRVSTILDADLVLVLSRGILV 233
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
6-188 |
2.27e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.27 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 6 IEGLEKSFdigdSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKElALfrRH 85
Cdd:PRK10982 1 MSNISKSF----PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKE-AL--EN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 86 KIGFIFQQFNLIPVFNAEENVGL---PLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEP 162
Cdd:PRK10982 74 GISMVHQELNLVLQRSVMDNMWLgryPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNA 153
|
170 180 190
....*....|....*....|....*....|
gi 446943912 163 AIILADEPTGALdSENSKN----IIAALRN 188
Cdd:PRK10982 154 KIVIMDEPTSSL-TEKEVNhlftIIRKLKE 182
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
127-204 |
2.78e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.39 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 127 LLELVGLKGKEKHLPA--QLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDElGQTAVIVTHDP 204
Cdd:PLN03140 1001 LVELDNLKDAIVGLPGvtGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDT-GRTVVCTIHQP 1079
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
141-214 |
3.69e-07 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 49.53 E-value: 3.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 141 PAQLSGGQQQ------RVAIARAF-ANEPAIILaDEPTGALDSENSKNiiaALRNACDELGQTAV----IVTHDPFVAAH 209
Cdd:cd03240 113 RGRCSGGEKVlasliiRLALAETFgSNCGILAL-DEPTTNLDEENIEE---SLAEIIEERKSQKNfqliVITHDEELVDA 188
|
....*
gi 446943912 210 ADKVV 214
Cdd:cd03240 189 ADHIY 193
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
17-232 |
4.61e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.49 E-value: 4.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 17 DSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLdipSVGSIRVDGTEIS----TLKEkelalFRRHKIGFIfq 92
Cdd:TIGR00956 71 TKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASN---TDGFHIGVEGVITydgiTPEE-----IKKHYRGDV-- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 93 qfnlipVFNAEENVGLPLL------------------LDNVSQKkatVTANRLLELV----GLK-------GKEkhLPAQ 143
Cdd:TIGR00956 141 ------VYNAETDVHFPHLtvgetldfaarcktpqnrPDGVSRE---EYAKHIADVYmatyGLShtrntkvGND--FVRG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 144 LSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVAAHA--DKVVFLLDGEV 221
Cdd:TIGR00956 210 VSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCSQDAYElfDKVIVLYEGYQ 289
|
250
....*....|....*....
gi 446943912 222 IH----EHA----ESKGWK 232
Cdd:TIGR00956 290 IYfgpaDKAkqyfEKMGFK 308
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
144-231 |
5.23e-07 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 50.10 E-value: 5.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 144 LSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDelGQTAVIVTHDPFVAAHADKVVFLLDGEVI- 222
Cdd:PRK10789 452 LSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGE--GRTVIISAHRLSALTEASEILVMQHGHIAq 529
|
90
....*....|...
gi 446943912 223 ---HEH-AESKGW 231
Cdd:PRK10789 530 rgnHDQlAQQSGW 542
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
144-203 |
5.35e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.19 E-value: 5.35e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 144 LSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHD 203
Cdd:PRK13409 454 LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHD 513
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
142-220 |
8.63e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.03 E-value: 8.63e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446943912 142 AQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHDPFVAAHADKVVFLLDGE 220
Cdd:PTZ00265 578 SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRYANTIFVLSNRE 656
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
144-203 |
9.22e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 49.40 E-value: 9.22e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 144 LSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVIVTHD 203
Cdd:COG1245 456 LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHD 515
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
125-222 |
9.81e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.56 E-value: 9.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 125 NRLLELVGLKGkEKHLpAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENskniIAALRNACDELGQTAVIVTHD- 203
Cdd:PRK11147 140 NEVLAQLGLDP-DAAL-SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET----IEWLEGFLKTFQGSIIFISHDr 213
|
90
....*....|....*....
gi 446943912 204 PFVAAHADKVVFLLDGEVI 222
Cdd:PRK11147 214 SFIRNMATRIVDLDRGKLV 232
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-223 |
9.87e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.51 E-value: 9.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 2 NIIEIEGLEKSFDIGdskvKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLggldipsVGSIRVDGTEIstlKEKELAl 81
Cdd:PRK15064 318 NALEVENLTKGFDNG----PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTL-------VGELEPDSGTV---KWSENA- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 82 frrhKIGFIFQQFNliPVFNAEENvglplLLDNVSQKKAT--------VTANRLLelvgLKGKEKHLPAQ-LSGGQQQRV 152
Cdd:PRK15064 383 ----NIGYYAQDHA--YDFENDLT-----LFDWMSQWRQEgddeqavrGTLGRLL----FSQDDIKKSVKvLSGGEKGRM 447
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446943912 153 AIARAFANEPAIILADEPTGALDSENskniIAALRNACDELGQTAVIVTHD-PFVAAHADKVVFLLDGEVIH 223
Cdd:PRK15064 448 LFGKLMMQKPNVLVMDEPTNHMDMES----IESLNMALEKYEGTLIFVSHDrEFVSSLATRIIEITPDGVVD 515
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
23-214 |
1.08e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 48.41 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 23 LKDINLQIQKGDFVCIMGASGSGK---------------------TTLLQLLGGLDIPSVGSIRVDGTEIStLKEKELAL 81
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKsslafdtiyaegqrryveslsAYARQFLGQMDKPDVDSIEGLSPAIA-IDQKTTSR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 82 FRRHKIGFIFQQFNLIPVFNAeeNVGLpllldnvsqkkatVTANRLLELVGLKgkekHL-----PAQLSGGQQQRVAIAR 156
Cdd:cd03270 90 NPRSTVGTVTEIYDYLRLLFA--RVGI-------------RERLGFLVDVGLG----YLtlsrsAPTLSGGEAQRIRLAT 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 157 AFANEPAIIL--ADEPTGALDSENSKNIIAALRNACDeLGQTAVIVTHDPFVAAHADKVV 214
Cdd:cd03270 151 QIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRD-LGNTVLVVEHDEDTIRAADHVI 209
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
22-221 |
1.34e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 49.39 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 22 ILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfRRhkigfifqQFNLIPvfn 101
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLREL---RR--------QFSMIP--- 1390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 102 aeenvGLPLLLDnvsqkkATVTAN-------------RLLELVGLKGkekHLPAQLSG--------------GQQQRVAI 154
Cdd:PTZ00243 1391 -----QDPVLFD------GTVRQNvdpfleassaevwAALELVGLRE---RVASESEGidsrvleggsnysvGQRQLMCM 1456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446943912 155 ARAFANE-PAIILADEPTGALDSENSKNIIAALRNACDelGQTAVIVTHDPFVAAHADKVVFLLDGEV 221
Cdd:PTZ00243 1457 ARALLKKgSGFILMDEATANIDPALDRQIQATVMSAFS--AYTVITIAHRLHTVAQYDKIIVMDHGAV 1522
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
143-214 |
1.84e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 46.58 E-value: 1.84e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446943912 143 QLSGGQQQRVAIARAFANE-----PAIILaDEPTGALDSENSKNIIAALRNACDELGQTAVIvTHDPFVAAHADKVV 214
Cdd:cd03227 77 QLSGGEKELSALALILALAslkprPLYIL-DEIDRGLDPRDGQALAEAILEHLVKGAQVIVI-THLPELAELADKLI 151
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
100-202 |
2.38e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 47.81 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 100 FNAEENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENS 179
Cdd:NF000106 101 FSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTR 180
|
90 100
....*....|....*....|...
gi 446943912 180 KNIIAALRNACDElGQTAVIVTH 202
Cdd:NF000106 181 NEVWDEVRSMVRD-GATVLLTTQ 202
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
24-251 |
4.38e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 47.35 E-value: 4.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 24 KDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKElalfrRHKIGFifqqfnlipVFNAE 103
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ-----RLARGL---------VYLPE 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 104 ENVGLPLLLD-----NVS------------QKKATVTANRLLELVGLKGKEKHLPAQ-LSGGQQQRVAIARAFANEPAII 165
Cdd:PRK15439 346 DRQSSGLYLDaplawNVCalthnrrgfwikPARENAVLERYRRALNIKFNHAEQAARtLSGGNQQKVLIAKCLEASPQLL 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 166 LADEPTGALDSENSKNIIAALRNACDElgQTAVIVTHDPF--VAAHADKVVFLLDGEVIHEhaeskgwkfrnIPQQVIHI 243
Cdd:PRK15439 426 IVDEPTRGVDVSARNDIYQLIRSIAAQ--NVAVLFISSDLeeIEQMADRVLVMHQGEISGA-----------LTGAAINV 492
|
....*...
gi 446943912 244 QEIMNRHF 251
Cdd:PRK15439 493 DTIMRLAF 500
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-221 |
5.49e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 47.13 E-value: 5.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 3 IIEIEGLeKSFDIGDSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLdIPSV--GSIRVDGTEISTlkeKELA 80
Cdd:TIGR02633 257 ILEARNL-TCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGA-YPGKfeGNVFINGKPVDI---RNPA 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 81 LFRRHKIGFI---FQQFNLIPVFNAEENVGLPLL--------LDNVSQKKATVTANRLLELvglKGKEKHLP-AQLSGGQ 148
Cdd:TIGR02633 332 QAIRAGIAMVpedRKRHGIVPILGVGKNITLSVLksfcfkmrIDAAAELQIIGSAIQRLKV---KTASPFLPiGRLSGGN 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446943912 149 QQRVAIARAFANEPAIILADEPTGALDSeNSKNIIAALRNACDELGQTAVIVTHD-PFVAAHADKVVFLLDGEV 221
Cdd:TIGR02633 409 QQKAVLAKMLLTNPRVLILDEPTRGVDV-GAKYEIYKLINQLAQEGVAIIVVSSElAEVLGLSDRVLVIGEGKL 481
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
142-203 |
1.17e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.88 E-value: 1.17e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446943912 142 AQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENskniIAALRNACDELGQTAVIVTHD 203
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES----VAWLEQFLHDYPGTVVAVTHD 219
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-187 |
1.61e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 44.56 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 1 MNIIEIEgleksFDIGDSKvkILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEIstlkEKELA 80
Cdd:PRK13540 2 LDVIELD-----FDYHDQP--LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLC 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 81 LFRRhKIGFIFQQFNLIPVFNAEENVGLPLlldnvsqkKATVTANRLLELVGLKGKEKHLP---AQLSGGQQQRVAIARA 157
Cdd:PRK13540 71 TYQK-QLCFVGHRSGINPYLTLRENCLYDI--------HFSPGAVGITELCRLFSLEHLIDypcGLLSSGQKRQVALLRL 141
|
170 180 190
....*....|....*....|....*....|
gi 446943912 158 FANEPAIILADEPTGALDSENSKNIIAALR 187
Cdd:PRK13540 142 WMSKAKLWLLDEPLVALDELSLLTIITKIQ 171
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
144-204 |
3.96e-05 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 44.35 E-value: 3.96e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446943912 144 LSGGQQQRVAIARAFANEPAIILADEPTGALdsenSKNIIAALRNACDELGQTAVIVTHDP 204
Cdd:TIGR00954 583 LSGGEKQRIAMARLFYHKPQFAILDECTSAV----SVDVEGYMYRLCREFGITLFSVSHRK 639
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
144-232 |
4.32e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.47 E-value: 4.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 144 LSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALrnacdELGQTAVI-VTHDP-FVAAHADKVVFLLDGEV 221
Cdd:PLN03073 628 LSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGL-----VLFQGGVLmVSHDEhLISGSVDELWVVSEGKV 702
|
90
....*....|.
gi 446943912 222 IHEHAESKGWK 232
Cdd:PLN03073 703 TPFHGTFHDYK 713
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
143-209 |
5.95e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 43.95 E-value: 5.95e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446943912 143 QLSGGQQQRVAIARAFANEPAIILADEPTGALDSENskniIAALRNACDELGQTAVIVTHDPF----VAAH 209
Cdd:PRK11819 445 VLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVET----LRALEEALLEFPGCAVVISHDRWfldrIATH 511
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-202 |
7.01e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 43.09 E-value: 7.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 2 NIIEIEGLEKSfdIGDskVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSV--GSIRVDGTEISTLKEKEl 79
Cdd:CHL00131 6 PILEIKNLHAS--VNE--NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKIleGDILFKGESILDLEPEE- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 80 alfRRHKIGFI-FQQFNLIPVFNAEENVGLPLLLDNVSQKKATVTA-------NRLLELVGLKGK--EKHLPAQLSGGQQ 149
Cdd:CHL00131 81 ---RAHLGIFLaFQYPIEIPGVSNADFLRLAYNSKRKFQGLPELDPlefleiiNEKLKLVGMDPSflSRNVNEGFSGGEK 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446943912 150 QRVAIARAFANEPAIILADEPTGALDSENSKnIIAALRNACDELGQTAVIVTH 202
Cdd:CHL00131 158 KRNEILQMALLDSELAILDETDSGLDIDALK-IIAEGINKLMTSENSIILITH 209
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
144-224 |
8.40e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 43.45 E-value: 8.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 144 LSGGQQQRVAIARAFANEPAIILADEPTGALDSeNSKNIIAALRNACDELGQTAVIVTHD-PFVAAHADKVVflldgeVI 222
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDV-GAKKEIYQLINQFKAEGLSIILVSSEmPEVLGMSDRIL------VM 468
|
..
gi 446943912 223 HE 224
Cdd:PRK10762 469 HE 470
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
112-203 |
9.67e-05 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 42.74 E-value: 9.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 112 LDNVSQKKATVTANRLLELVGLKG-KEKHLpAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNAC 190
Cdd:cd03236 108 GELLKKKDERGKLDELVDQLELRHvLDRNI-DQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELA 186
|
90
....*....|...
gi 446943912 191 DElGQTAVIVTHD 203
Cdd:cd03236 187 ED-DNYVLVVEHD 198
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
142-214 |
1.47e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.89 E-value: 1.47e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446943912 142 AQLSGGQQQRVAIARAFANEPAII--LADEPTGAL---DSENSKNIIAALRNAcdelGQTAVIVTHDPFVAAHADKVV 214
Cdd:PRK00635 475 ATLSGGEQERTALAKHLGAELIGItyILDEPSIGLhpqDTHKLINVIKKLRDQ----GNTVLLVEHDEQMISLADRII 548
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
144-224 |
1.65e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 42.69 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 144 LSGGQQQRVAIARAFANEPAIIL--ADEPTGALDSENSKNIIAALRNACDeLGQTAVIVTHDPFVAAHADKVVFL----- 216
Cdd:TIGR00630 489 LSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHQRDNRRLINTLKRLRD-LGNTLIVVEHDEDTIRAADYVIDIgpgag 567
|
....*....
gi 446943912 217 -LDGEVIHE 224
Cdd:TIGR00630 568 eHGGEVVAS 576
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
30-202 |
2.13e-04 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 42.69 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 30 IQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTlkekelalfrrhKIGFIFQQFNLIPVFNA------- 102
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT------------NISDVHQNMGYCPQFDAiddlltg 2029
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 103 EENVGLPLLLDNVSQKKATVTANRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNI 182
Cdd:TIGR01257 2030 REHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRML 2109
|
170 180
....*....|....*....|
gi 446943912 183 IAALRNACDElGQTAVIVTH 202
Cdd:TIGR01257 2110 WNTIVSIIRE-GRAVVLTSH 2128
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
144-226 |
2.30e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 42.21 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 144 LSGGQQQRVAIARAFANEPAIILADEPTGALDSeNSKNIIAALRNACDELGQTAVIVTHD-PFVAAHADKVVFL----LD 218
Cdd:PRK11288 397 LSGGNQQKAILGRWLSEDMKVILLDEPTRGIDV-GAKHEIYNVIYELAAQGVAVLFVSSDlPEVLGVADRIVVMregrIA 475
|
....*...
gi 446943912 219 GEVIHEHA 226
Cdd:PRK11288 476 GELAREQA 483
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-220 |
2.66e-04 |
|
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: 40.43 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 32 KGDFVCIMGASGSGKttllqllggldipsvgsirvdgteiSTLKEKELALFRRHKIGFIfqqfnlipVFNAEENvglpll 111
Cdd:smart00382 1 PGEVILIVGPPGSGK-------------------------TTLARALARELGPPGGGVI--------YIDGEDI------ 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 112 ldnvsqkkatvtaNRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALR---- 187
Cdd:smart00382 42 -------------LEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrll 108
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446943912 188 -NACDELGQTAVIVTHDPFV------AAHADKVVFLLDGE 220
Cdd:smart00382 109 lLLKSEKNLTVILTTNDEKDlgpallRRRFDRRIVLLLIL 148
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-222 |
3.89e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 41.65 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 22 ILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfrRHKIGFIFQ--------- 92
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDL----RKVLGIIPQapvlfsgtv 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 93 QFNLIPvFNAEENVGLPLLLDNvSQKKATVTANRLlelvGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTG 172
Cdd:PLN03130 1330 RFNLDP-FNEHNDADLWESLER-AHLKDVIRRNSL----GLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATA 1403
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446943912 173 ALDSENSKNIIAALR---NACdelgqTAVIVTHDPFVAAHADKVVFLLDGEVI 222
Cdd:PLN03130 1404 AVDVRTDALIQKTIReefKSC-----TMLIIAHRLNTIIDCDRILVLDAGRVV 1451
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
13-224 |
4.24e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 41.07 E-value: 4.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 13 FDIGDSKVKILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLdIP--SVGSIRVDGTEIsTLKEKELALfrRHKIGFI 90
Cdd:PRK13549 268 WDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGA-YPgrWEGEIFIDGKPV-KIRNPQQAI--AQGIAMV 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 91 FQ---QFNLIPVFNAEENVGLPLL--------LDNVSQKKatvTANRLLELVGLKGKEKHLP-AQLSGGQQQRVAIARAF 158
Cdd:PRK13549 344 PEdrkRDGIVPVMGVGKNITLAALdrftggsrIDDAAELK---TILESIQRLKVKTASPELAiARLSGGNQQKAVLAKCL 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446943912 159 ANEPAIILADEPTGALDSeNSKNIIAALRNACDELGQTAVIVTHD-PFVAAHADKVVflldgeVIHE 224
Cdd:PRK13549 421 LLNPKILILDEPTRGIDV-GAKYEIYKLINQLVQQGVAIIVISSElPEVLGLSDRVL------VMHE 480
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
126-219 |
4.28e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 41.63 E-value: 4.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 126 RLLE-------LVGLKGKekhlpaQLSGGQQQRVAIARAFANEPAIIL-ADEPTGALDSENSKNIIAALRNACDElGQTA 197
Cdd:TIGR00956 883 KLLEmesyadaVVGVPGE------GLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADH-GQAI 955
|
90 100
....*....|....*....|....
gi 446943912 198 VIVTHDP--FVAAHADKVVFLLDG 219
Cdd:TIGR00956 956 LCTIHQPsaILFEEFDRLLLLQKG 979
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
22-189 |
4.55e-04 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 40.61 E-value: 4.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 22 ILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLdIPSVGSIRVDGTEISTLKEKELalfrRHKIG------FIFQ--- 92
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGVSWNSVPLQKW----RKAFGvipqkvFIFSgtf 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 93 QFNLIP--------VFNAEENVGLPLLLDNVSQKkatvtanrlLELVGLKGKekhlpAQLSGGQQQRVAIARAFANEPAI 164
Cdd:cd03289 94 RKNLDPygkwsdeeIWKVAEEVGLKSVIEQFPGQ---------LDFVLVDGG-----CVLSHGHKQLMCLARSVLSKAKI 159
|
170 180
....*....|....*....|....*
gi 446943912 165 ILADEPTGALDSENSKNIIAALRNA 189
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQA 184
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
26-228 |
4.72e-04 |
|
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: 40.94 E-value: 4.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 26 INLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEIStlkEKELALFRRHkigF--IFQQFNLipvFnaE 103
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT---ADNREAYRQL---FsaVFSDFHL---F--D 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 104 ENVGLPlllDNVSQKKatvtANRLLELVGLKGKEKH-----LPAQLSGGQQQRVAIARAFANEPAIILADEptGALD--- 175
Cdd:COG4615 420 RLLGLD---GEADPAR----ARELLERLELDHKVSVedgrfSTTDLSQGQRKRLALLVALLEDRPILVFDE--WAADqdp 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 176 -------SEnsknIIAALRnacdELGQTAVIVTHDPFVAAHADKVVFLLDGEVIHEHAES 228
Cdd:COG4615 491 efrrvfyTE----LLPELK----ARGKTVIAISHDDRYFDLADRVLKMDYGKLVELTGPA 542
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
68-203 |
4.88e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 40.95 E-value: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 68 GTEIST----LKEKELalfrR--HKIgfifQQFNLIP-VF--NAEEnvglplLLDNVSQKKAtvtANRLLELVGLKGKEK 138
Cdd:PRK13409 145 GTELQNyfkkLYNGEI----KvvHKP----QYVDLIPkVFkgKVRE------LLKKVDERGK---LDEVVERLGLENILD 207
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446943912 139 HLPAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRnacdEL--GQTAVIVTHD 203
Cdd:PRK13409 208 RDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIR----ELaeGKYVLVVEHD 270
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
139-216 |
6.64e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 6.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 139 HLP-----AQLSGGQQQRVAIARAFAN---EPAIILADEPTGALDSENSKNIIAALRNACDElGQTAVIVTHDPFVAAHA 210
Cdd:PRK00635 800 YLPlgrplSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQ-GHTVVIIEHNMHVVKVA 878
|
....*.
gi 446943912 211 DKVVFL 216
Cdd:PRK00635 879 DYVLEL 884
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
68-203 |
7.77e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 40.54 E-value: 7.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 68 GTEIST----LKEKELalfrR--HKIgfifQQFNLIP-VF--NAEEnvglplLLDNVSQKKAtvtANRLLELVGLKGKEK 138
Cdd:COG1245 145 GTELQDyfkkLANGEI----KvaHKP----QYVDLIPkVFkgTVRE------LLEKVDERGK---LDELAEKLGLENILD 207
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446943912 139 HLPAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDElGQTAVIVTHD 203
Cdd:COG1245 208 RDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHD 271
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
143-175 |
1.12e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.23 E-value: 1.12e-03
10 20 30
....*....|....*....|....*....|...
gi 446943912 143 QLSGGQQQRVAIARAFANEPAIILADEPTGALD 175
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
23-46 |
1.58e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 39.61 E-value: 1.58e-03
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
144-214 |
1.66e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 38.75 E-value: 1.66e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446943912 144 LSGGQQQRVAIARAFANE---PAIILADEPTGALDSENSKNIIAALrNACDELGQTAVIVTHDPFVAAHADKVV 214
Cdd:cd03271 170 LSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVL-QRLVDKGNTVVVIEHNLDVIKCADWII 242
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
22-202 |
2.41e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 38.23 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 22 ILKDINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSV--GSIRVDGTEISTLKEKELAlfrRHKIGFIFQQFNLIPv 99
Cdd:PRK09580 16 ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVtgGTVEFKGKDLLELSPEDRA---GEGIFMAFQYPVEIP- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 100 fNAEENVGLPLLLDNVSQKKATVTANR--LLELVGLKGKEKHLPAQL---------SGGQQQRVAIARAFANEPAIILAD 168
Cdd:PRK09580 92 -GVSNQFFLQTALNAVRSYRGQEPLDRfdFQDLMEEKIALLKMPEDLltrsvnvgfSGGEKKRNDILQMAVLEPELCILD 170
|
170 180 190
....*....|....*....|....*....|....
gi 446943912 169 EPTGALDSENSKnIIAALRNACDELGQTAVIVTH 202
Cdd:PRK09580 171 ESDSGLDIDALK-IVADGVNSLRDGKRSFIIVTH 203
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
144-175 |
2.72e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 38.56 E-value: 2.72e-03
10 20 30
....*....|....*....|....*....|..
gi 446943912 144 LSGGQQQRVAIARAFANEPAIILADEPTGALD 175
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGID 423
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
121-203 |
3.76e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 37.68 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943912 121 TVTANRLLELVGLKGkekhlPAQLSGGQQQRVAIARAFanepAIILaDepTGALDSENSKNIIAALRNacdelgqtAVIV 200
Cdd:COG0419 141 KLKQEILAQLSGLDP-----IETLSGGERLRLALADLL----SLIL-D--FGSLDEERLERLLDALEE--------LAII 200
|
...
gi 446943912 201 THD 203
Cdd:COG0419 201 THV 203
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
23-46 |
4.46e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 38.13 E-value: 4.46e-03
10 20
....*....|....*....|....
gi 446943912 23 LKDINLQIQKGDFVCIMGASGSGK 46
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGK 648
|
|
| |
