|
Name |
Accession |
Description |
Interval |
E-value |
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-226 |
6.28e-116 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 331.24 E-value: 6.28e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 1 MN-IIEIKRLEKSFDIGDSKVKILKGINLQIQKGDFVCIMGASGSGKttllqllgglDIPSVGSIRVDGTEISTLKEKEL 79
Cdd:COG1136 1 MSpLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKstllnilgglDRPTSGEVLIDGQDISSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 80 ALFRRHKIGFIFQQFNLIPVFSAEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFA 159
Cdd:COG1136 81 ARLRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 872553587 160 NEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVAAHADKVVFLLDGEVIHEHA 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 |
4.31e-102 |
|
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: 295.94 E-value: 4.31e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLEKSFDIGDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALFR 83
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 84 RHKIGFIFQQFNLIPVFSAEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPA 163
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 872553587 164 IILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVAAHADKVVFLLDGEV 221
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-228 |
1.05e-84 |
|
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: 252.35 E-value: 1.05e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 2 NIIEIKRLEKSFDIGDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELAL 81
Cdd:COG4181 7 PIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 82 FRRHKIGFIFQQFNLIPVFSAEENVGLPLLLDNVSQKKAtmTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANE 161
Cdd:COG4181 87 LRARHVGFVFQSFQLLPTLTALENVMLPLELAGRRDARA--RARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 872553587 162 PAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVAAHADKVVFLLDGEVIHEHAES 228
Cdd:COG4181 165 PAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTAAT 231
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-224 |
1.39e-70 |
|
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: 216.68 E-value: 1.39e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 3 IIEIKRLEKSFDIGDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALF 82
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 83 RRHkIGFIFQQFNLIPVFSAEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEP 162
Cdd:cd03258 81 RRR-IGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 872553587 163 AIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHD-PFVAAHADKVVFLLDGEVIHE 224
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEmEVVKRICDRVAVMEKGEVVEE 222
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
3-222 |
3.34e-70 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 219.18 E-value: 3.34e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 3 IIEIKRLEKSFDIGDSKVKILKGINLQIQKGDFVCIMGASGSGKttllqllggldiPSVGSIRVDGTEISTLKEKELALF 82
Cdd:COG1135 1 MIELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKstlircinllerPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 83 RRhKIGFIFQQFNLIPVFSAEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEP 162
Cdd:COG1135 81 RR-KIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 872553587 163 AIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVAAH-ADKVVFLLDGEVI 222
Cdd:COG1135 160 KVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRiCDRVAVLENGRIV 220
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-227 |
2.28e-69 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 212.99 E-value: 2.28e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 3 IIEIKRLEKSFDIGdskVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALF 82
Cdd:COG2884 1 MIRFENVSKRYPGG---REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 83 RRhKIGFIFQQFNLIPVFSAEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEP 162
Cdd:COG2884 78 RR-RIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 872553587 163 AIILADEPTGALDSENSKNIIAALRNACdELGQTAVVVTHDP-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 |
2.11e-68 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 211.39 E-value: 2.11e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 3 IIEIKRLEKSFdiGDSKVkiLKGINLQIQKGDFVCIMGASGSGKttllqllgglDIPSVGSIRVDGTEIsTLKEKELALF 82
Cdd:COG1126 1 MIEIENLHKSF--GDLEV--LKGISLDVEKGEVVVIIGPSGSGKstllrcinllEEPDSGTITVDGEDL-TDSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 83 RRhKIGFIFQQFNLIPVFSAEENVGL-PLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANE 161
Cdd:COG1126 76 RR-KVGMVFQQFNLFPHLTVLENVTLaPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAME 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 872553587 162 PAIILADEPTGALDSENSKNIIAALRNACDElGQTAVVVTHD-PFVAAHADKVVFLLDGEVIHE 224
Cdd:COG1126 155 PKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEmGFAREVADRVVFMDGGRIVEE 217
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
3-219 |
5.23e-65 |
|
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: 202.20 E-value: 5.23e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 3 IIEIKRLEKSFDIGDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALF 82
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 83 RRHKIGFIFQQFNLIPVFSAEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEP 162
Cdd:TIGR02211 81 RNKKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 872553587 163 AIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVAAHADKVVFLLDG 219
Cdd:TIGR02211 161 SLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVLEMKDG 217
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-216 |
3.28e-64 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 201.09 E-value: 3.28e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 1 MNIIEIKRLEKSFDIGDSKVKILKGINLQIQKGDFVCIMGASGSGKttllqllgglDIPSVGSIRVDGTEISTLkekela 80
Cdd:COG1116 5 APALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKstllrliaglEKPTSGEVLVDGKPVTGP------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 81 lfrRHKIGFIFQQFNLIPVFSAEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFAN 160
Cdd:COG1116 79 ---GPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 872553587 161 EPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVAAH-ADKVVFL 216
Cdd:COG1116 156 DPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFlADRVVVL 212
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
3-223 |
3.43e-63 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 208.81 E-value: 3.43e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 3 IIEIKRLEKSFDIGDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALF 82
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 83 RRHKIGFIFQQFNLIPVFSAEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEP 162
Cdd:PRK10535 84 RREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 872553587 163 AIILADEPTGALDSENSKNIIAALRNACDElGQTAVVVTHDPFVAAHADKVVFLLDGEVIH 223
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVAAQAERVIEIRDGEIVR 223
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
3-222 |
1.69e-62 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 196.43 E-value: 1.69e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 3 IIEIKRLEKSFDigdSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALF 82
Cdd:COG3638 2 MLELRNLSKRYP---GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 83 RRhKIGFIFQQFNLIPVFSAEENV---------GLPLLLDNVSqKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVA 153
Cdd:COG3638 79 RR-RIGMIFQQFNLVPRLSVLTNVlagrlgrtsTWRSLLGLFP-PEDRERALEALERVGLADKAYQRADQLSGGQQQRVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 154 IARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVA-AHADKVVFLLDGEVI 222
Cdd:COG3638 157 IARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLArRYADRIIGLRDGRVV 226
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
3-219 |
6.85e-61 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 191.47 E-value: 6.85e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 3 IIEIKRLEKSFDIGDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALF 82
Cdd:NF038007 1 MLNMQNAEKCYITKTIKTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKIIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 83 RRHKIGFIFQQFNLIPVFSAEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEP 162
Cdd:NF038007 81 RRELIGYIFQSFNLIPHLSIFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 872553587 163 AIILADEPTGALDSENSKNIIAALRNaCDELGQTAVVVTHDPFVAAHADKVVFLLDG 219
Cdd:NF038007 161 ALLLADEPTGNLDSKNARAVLQQLKY-INQKGTTIIMVTHSDEASTYGNRIINMKDG 216
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-221 |
8.21e-61 |
|
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: 190.82 E-value: 8.21e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLEKSFdiGDSKVkiLKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEIsTLKEKELALFR 83
Cdd:cd03262 1 IEIKNLHKSF--GDFHV--LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL-TDDKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 84 RhKIGFIFQQFNLIPVFSAEENVGL-PLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEP 162
Cdd:cd03262 76 Q-KVGMVFQQFNLFPHLTVLENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 163 AIILADEPTGALDSENSKNIIAALRNACDElGQTAVVVTHD-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 |
1.47e-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: 190.79 E-value: 1.47e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 3 IIEIKRLEKSFDIGDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALf 82
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKI- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 83 RRHKIGFIFQ--QFNLIPVFSAEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHL---PAQLSGGQQQRVAIARA 157
Cdd:cd03257 80 RRKEIQMVFQdpMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLnryPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 158 FANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVAAH-ADKVVFLLDGEVIhEHA 226
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKiADRVAVMYAGKIV-EEG 228
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
3-220 |
3.03e-60 |
|
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: 189.77 E-value: 3.03e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 3 IIEIKRLEKSFDIGdskVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALF 82
Cdd:TIGR02673 1 MIEFHNVSKAYPGG---VAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 83 RRHkIGFIFQQFNLIPVFSAEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEP 162
Cdd:TIGR02673 78 RRR-IGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 872553587 163 AIILADEPTGALDSENSKNIIAALRNACDeLGQTAVVVTHDP-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 |
7.68e-60 |
|
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: 189.42 E-value: 7.68e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 2 NIIEIKRLEKSFDigdsKVKILKGINLQIQKGDFVCIMGASGSGKttllqllggldipSV-------------GSIRVDG 68
Cdd:COG1127 4 PMIEVRNLTKSFG----DRVVLDGVSLDVPRGEILAIIGGSGSGK-------------SVllkliigllrpdsGEILVDG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 69 TEISTLKEKELALFRRhKIGFIFQQ---FNLIPVFsaeENVGLPLL-LDNVSQKKATMTATRLLELVGLKGKEKHLPAQL 144
Cdd:COG1127 67 QDITGLSEKELYELRR-RIGMLFQGgalFDSLTVF---ENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSEL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 145 SGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHD-PFVAAHADKVVFLLDGEVIH 223
Cdd:COG1127 143 SGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDlDSAFAIADRVAVLADGKIIA 222
|
.
gi 872553587 224 E 224
Cdd:COG1127 223 E 223
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-222 |
1.29e-59 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 192.32 E-value: 1.29e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLEKSFDIGDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALFR 83
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 84 RhKIGFIFQQFNLIPVFSAEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPA 163
Cdd:PRK11153 82 R-QIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 164 IILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVAAH-ADKVVFLLDGEVI 222
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRiCDRVAVIDAGRLV 220
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-222 |
1.55e-58 |
|
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: 186.23 E-value: 1.55e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLEKSFDigdSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALFR 83
Cdd:cd03256 1 IEVENLSKTYP---NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 84 RHkIGFIFQQFNLIPVFSAEENVGLPLL--------LDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIA 155
Cdd:cd03256 78 RQ-IGMIFQQFNLIERLSVLENVLSGRLgrrstwrsLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 872553587 156 RAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDP-FVAAHADKVVFLLDGEVI 222
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVdLAREYADRIVGLKDGRIV 224
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-216 |
1.82e-58 |
|
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: 185.37 E-value: 1.82e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLEKSFDIGDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTlkekelalfR 83
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG---------P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 84 RHKIGFIFQQFNLIPVFSAEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPA 163
Cdd:cd03293 72 GPDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 872553587 164 IILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVAAH-ADKVVFL 216
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFlADRVVVL 205
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-216 |
2.52e-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: 182.04 E-value: 2.52e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 6 IKRLEKSFdiGDSKvkILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALFRRH 85
Cdd:TIGR03608 1 LKNISKKF--GDKV--ILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 86 KIGFIFQQFNLIPVFSAEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAII 165
Cdd:TIGR03608 77 KLGYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 872553587 166 LADEPTGALDSENSKNIIAALRNACDElGQTAVVVTHDPFVAAHADKVVFL 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 |
3.15e-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: 182.14 E-value: 3.15e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 3 IIEIKRLEKSFDIGDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALF 82
Cdd:TIGR02982 1 VISIRNLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 83 RRHkIGFIFQQFNLIPVFSAEENVGLPL-LLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANE 161
Cdd:TIGR02982 81 RRR-IGYIFQAHNLLGFLTARQNVQMALeLQPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHH 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 872553587 162 PAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVAAHADKVVFLLDG 219
Cdd:TIGR02982 160 PKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDNRILDVADRILQMEDG 217
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-222 |
4.93e-57 |
|
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: 181.93 E-value: 4.93e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLEKSFDigdSKVkILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALFR 83
Cdd:cd03261 1 IELRGLTKSFG---GRT-VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 84 RhKIGFIFQQFNLIPVFSAEENVGLPL-----LLDNVSQKKATMTatrlLELVGLKGKEKHLPAQLSGGQQQRVAIARAF 158
Cdd:cd03261 77 R-RMGMLFQSGALFDSLTVFENVAFPLrehtrLSEEEIREIVLEK----LEAVGLRGAEDLYPAELSGGMKKRVALARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 872553587 159 ANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHD-PFVAAHADKVVFLLDGEVI 222
Cdd:cd03261 152 ALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDlDTAFAIADRIAVLYDGKIV 216
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-224 |
8.93e-57 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 181.13 E-value: 8.93e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 2 NIIEIKRLEKSFDIGDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELAL 81
Cdd:PRK10584 5 NIVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 82 FRRHKIGFIFQQFNLIPVFSAEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANE 161
Cdd:PRK10584 85 LRAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGR 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 872553587 162 PAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVAAHADKVVFLLDGEVIHE 224
Cdd:PRK10584 165 PDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-229 |
5.67e-56 |
|
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: 179.80 E-value: 5.67e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 3 IIEIKRLEKSFDIGdskVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALF 82
Cdd:TIGR02315 1 MLEVENLSKVYPNG---KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 83 RRHkIGFIFQQFNLIPVFSAEENV---------GLPLLLDNVSqKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVA 153
Cdd:TIGR02315 78 RRR-IGMIFQHYNLIERLTVLENVlhgrlgykpTWRSLLGRFS-EEDKERALSALERVGLADKAYQRADQLSGGQQQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 872553587 154 IARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVA-AHADKVVFLLDGEVIHEHAESK 229
Cdd:TIGR02315 156 IARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAkKYADRIVGLKAGEIVFDGAPSE 232
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-221 |
2.56e-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: 177.21 E-value: 2.56e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLEKSFDIGdskVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALFR 83
Cdd:cd03292 1 IEFINVTKTYPNG---TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 84 RHkIGFIFQQFNLIPVFSAEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPA 163
Cdd:cd03292 78 RK-IGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 872553587 164 IILADEPTGALDSENSkNIIAALRNACDELGQTAVVVTHDP-FVAAHADKVVFLLDGEV 221
Cdd:cd03292 157 ILIADEPTGNLDPDTT-WEIMNLLKKINKAGTTVVVATHAKeLVDTTRHRVIALERGKL 214
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-222 |
5.82e-55 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 180.29 E-value: 5.82e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 1 MNIIEIKRLEKSFDigdsKVKILKGINLQIQKGDFVCIMGASGSGK-----------TtllqllggldiPSVGSIRVDGT 69
Cdd:COG3842 3 MPALELENVSKRYG----DVTALDDVSLSIEPGEFVALLGPSGCGKttllrmiagfeT-----------PDSGRILLDGR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 70 EIStlkekELALFRRHkIGFIFQQFNLIPVFSAEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQ 149
Cdd:COG3842 68 DVT-----GLPPEKRN-VGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 872553587 150 QRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVA-AHADKVVFLLDGEVI 222
Cdd:COG3842 142 QRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEAlALADRIAVMNDGRIE 215
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-222 |
1.30e-54 |
|
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: 175.02 E-value: 1.30e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLEKSFDigdsKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEkelalfR 83
Cdd:cd03259 1 LELKGLSKTYG----SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPP------E 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 84 RHKIGFIFQQFNLIPVFSAEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPA 163
Cdd:cd03259 71 RRNIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 164 IILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVA-AHADKVVFLLDGEVI 222
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEAlALADRIAVMNEGRIV 210
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-222 |
1.24e-52 |
|
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: 178.17 E-value: 1.24e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 3 IIEIKRLEKSFDI-GDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELAL 81
Cdd:COG1123 260 LLEVRNLSKRYPVrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 82 FRRHkIGFIFQ----QFNliPVFSAEENVGLPL-LLDNVSQKKATMTATRLLELVGLkgKEKHL---PAQLSGGQQQRVA 153
Cdd:COG1123 340 LRRR-VQMVFQdpysSLN--PRMTVGDIIAEPLrLHGLLSRAERRERVAELLERVGL--PPDLAdryPHELSGGQRQRVA 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 154 IARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHD-PFVAAHADKVVFLLDGEVI 222
Cdd:COG1123 415 IARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDlAVVRYIADRVAVMYDGRIV 484
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-229 |
9.13e-51 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 166.46 E-value: 9.13e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 1 MNIIEIKRLEKSFDiGDSkvkILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLK--EKE 78
Cdd:PRK11264 1 MSAIEVKNLVKKFH-GQT---VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARslSQQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 79 LALFR--RHKIGFIFQQFNLIPVFSAEENV--GlPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAI 154
Cdd:PRK11264 77 KGLIRqlRQHVGFVFQNFNLFPHRTVLENIieG-PVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 872553587 155 ARAFANEPAIILADEPTGALDSENSKNIIAALRNACDElGQTAVVVTHD-PFVAAHADKVVFlLDGEVIHEHAESK 229
Cdd:PRK11264 156 ARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEmSFARDVADRAIF-MDQGRIVEQGPAK 229
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
4-221 |
6.44e-50 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 164.59 E-value: 6.44e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLEKSFdiGDSKVkiLKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLK-------- 75
Cdd:COG4598 9 LEVRDLHKSF--GDLEV--LKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPdrdgelvp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 76 --EKELALFRRhKIGFIFQQFNLIPVFSAEENVGL-PLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRV 152
Cdd:COG4598 85 adRRQLQRIRT-RLGMVFQSFNLWSHMTVLENVIEaPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 153 AIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDElGQTAVVVTHDPFVAAH-ADKVVFLLDGEV 221
Cdd:COG4598 164 AIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDvSSHVVFLHQGRI 232
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-214 |
1.08e-49 |
|
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: 166.00 E-value: 1.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 3 IIEIKRLEKSFDIGDSKVKILKGINLQIQKGDFVCIMGASGSGKttllqllggldipSV----------------GSIRV 66
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGK-------------STlarailgllpppgitsGEILF 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 67 DGTEISTLKEKELALFRRHKIGFIFQQ----FNliPVFSAEENVGLPLLL-DNVSQKKATMTATRLLELVGLKGKEKHL- 140
Cdd:COG0444 68 DGEDLLKLSEKELRKIRGREIQMIFQDpmtsLN--PVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPDPERRLd 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 872553587 141 --PAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVAAH-ADKVV 214
Cdd:COG0444 146 ryPHELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEiADRVA 222
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
8-224 |
1.17e-49 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 163.06 E-value: 1.17e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 8 RLEKSFDIGDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALFRRHKI 87
Cdd:PRK11629 10 NLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 88 GFIFQQFNLIPVFSAEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILA 167
Cdd:PRK11629 90 GFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 872553587 168 DEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVAAHADKVVFLLDGEVIHE 224
Cdd:PRK11629 170 DEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAE 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-222 |
1.26e-49 |
|
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: 170.47 E-value: 1.26e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 3 IIEIKRLEKSFDIGDskVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLdIPSV----GSIRVDGTEISTLKEKE 78
Cdd:COG1123 4 LLEVRDLSVRYPGGD--VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGL-LPHGgrisGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 79 lalfRRHKIGFIFQ----QFNLIPVfsaEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAI 154
Cdd:COG1123 81 ----RGRRIGMVFQdpmtQLNPVTV---GDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 872553587 155 ARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVAAH-ADKVVFLLDGEVI 222
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEiADRVVVMDDGRIV 222
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-220 |
1.84e-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: 160.82 E-value: 1.84e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLEKSFdigdSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLkEKELALFR 83
Cdd:cd03229 1 LELKNVSKRY----GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDL-EDELPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 84 RhKIGFIFQQFNLIPVFSAEENVGLPllldnvsqkkatmtatrllelvglkgkekhlpaqLSGGQQQRVAIARAFANEPA 163
Cdd:cd03229 76 R-RIGMVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 872553587 164 IILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVAAH-ADKVVFLLDGE 220
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
4-222 |
9.61e-49 |
|
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: 162.04 E-value: 9.61e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLEKSF-----------DIGDSKVKILKG---------INLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGS 63
Cdd:cd03294 1 IKIKGLYKIFgknpqkafkllAKGKSKEEILKKtgqtvgvndVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 64 IRVDGTEISTLKEKELALFRRHKIGFIFQQFNLIPVFSAEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQ 143
Cdd:cd03294 81 VLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 144 LSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVAAH-ADKVVFLLDGEVI 222
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRlGDRIAIMKDGRLV 240
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-220 |
3.40e-48 |
|
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: 158.78 E-value: 3.40e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 5 EIKRLekSFDIGDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfrR 84
Cdd:cd03225 1 ELKNL--SFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKEL----R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 85 HKIGFIFQ----QFnlipvFSA--EENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAF 158
Cdd:cd03225 75 RKVGLVFQnpddQF-----FGPtvEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 872553587 159 ANEPAIILADEPTGALDSENSKNIIAALRNACDElGQTAVVVTHDP-FVAAHADKVVFLLDGE 220
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLdLLLELADRVIVLEDGK 211
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-229 |
9.98e-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: 158.11 E-value: 9.98e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLEKSFDigdsKVKILKGINLQIQKGDFVCIMGASGSGK-----TTLLQLLGGLDIPSVGSIRVDGTEISTLKEKE 78
Cdd:cd03260 1 IELRDLNVYYG----DKHALKDISLDIPKGEITALIGPSGCGKstllrLLNRLNDLIPGAPDEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 79 LALfrRHKIGFIFQQFNLIPvFSAEENVGLPLLLDNVSQKKATMTATR-LLELVGLKGKEK-HLPA-QLSGGQQQRVAIA 155
Cdd:cd03260 77 LEL--RRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVEeALRKAALWDEVKdRLHAlGLSGGQQQRLCLA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 872553587 156 RAFANEPAIILADEPTGALDSENSKNIIAALRNACDELgqTAVVVTHDPFVAAH-ADKVVFLLDGEVIhEHAESK 229
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARvADRTAFLLNGRLV-EFGPTE 225
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
3-224 |
1.53e-47 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 157.95 E-value: 1.53e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 3 IIEIKRLEKSFdiGDSKVkiLKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALf 82
Cdd:PRK09493 1 MIEFKNVSKHF--GPTQV--LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLI- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 83 rRHKIGFIFQQFNLIPVFSAEENVGL-PLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANE 161
Cdd:PRK09493 76 -RQEAGMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 872553587 162 PAIILADEPTGALDSENSKNIIAALRNACDElGQTAVVVTHD-PFVAAHADKVVFLLDGEVIHE 224
Cdd:PRK09493 155 PKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEiGFAEKVASRLIFIDKGRIAED 217
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-222 |
4.41e-47 |
|
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: 156.89 E-value: 4.41e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLEKSFDIGDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKElalfR 83
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKA----F 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 84 RHKIGFIFQQ----FNliPVFSAEENVGLPLLLDNVSQKKATmtATRLLELVGLKGKEKH-LPAQLSGGQQQRVAIARAF 158
Cdd:COG1124 78 RRRVQMVFQDpyasLH--PRHTVDRILAEPLRIHGLPDREER--IAELLEQVGLPPSFLDrYPHQLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 872553587 159 ANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVAAH-ADKVVFLLDGEVI 222
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIV 218
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-222 |
2.67e-46 |
|
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: 154.77 E-value: 2.67e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLEKSFdiGDSKvKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfr 83
Cdd:cd03295 1 IEFENVTKRY--GGGK-KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVEL---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 84 RHKIGFIFQQFNLIPVFSAEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKE--KHLPAQLSGGQQQRVAIARAFANE 161
Cdd:cd03295 74 RRKIGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEfaDRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 872553587 162 PAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVAAH-ADKVVFLLDGEVI 222
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRlADRIAIMKNGEIV 215
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-224 |
5.39e-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: 153.64 E-value: 5.39e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLekSFDIGDSKvKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfr 83
Cdd:COG1122 1 IELENL--SFSYPGGT-PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLREL---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 84 RHKIGFIFQ----QFnlipvFSA--EENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARA 157
Cdd:COG1122 74 RRKVGLVFQnpddQL-----FAPtvEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 872553587 158 FANEPAIILADEPTGALDSENSKNIIAALRNACDElGQTAVVVTHDP-FVAAHADKVVFLLDGEVIHE 224
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLdLVAELADRVIVLDDGRIVAD 215
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-221 |
7.91e-46 |
|
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: 153.16 E-value: 7.91e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLEKSFDigdsKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEIStlkekELALFR 83
Cdd:cd03300 1 IELENVSKFYG----GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT-----NLPPHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 84 RHkIGFIFQQFNLIPVFSAEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPA 163
Cdd:cd03300 72 RP-VNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 872553587 164 IILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVA-AHADKVVFLLDGEV 221
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEAlTMSDRIAVMNKGKI 209
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
4-222 |
1.03e-43 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 148.02 E-value: 1.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLEKSFdiGDSKVkiLKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKekelalFR 83
Cdd:TIGR00968 1 IEIANISKRF--GSFQA--LDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVH------AR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 84 RHKIGFIFQQFNLIPVFSAEENV--GLPLLLDNVSQKKATMTatRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANE 161
Cdd:TIGR00968 71 DRKIGFVFQHYALFKHLTVRDNIafGLEIRKHPKAKIKARVE--ELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 872553587 162 PAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVAAH-ADKVVFLLDGEVI 222
Cdd:TIGR00968 149 PQVLLLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEvADRIVVMSNGKIE 210
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
4-221 |
1.15e-42 |
|
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: 148.65 E-value: 1.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLEKSFDigdsKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKelalfr 83
Cdd:TIGR03265 5 LSIDNIRKRFG----AFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQ------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 84 RHKIGFIFQQFNLIPVFSAEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPA 163
Cdd:TIGR03265 75 KRDYGIVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 872553587 164 IILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVA-AHADKVVFLLDGEV 221
Cdd:TIGR03265 155 LLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEAlSMADRIVVMNHGVI 213
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-221 |
2.67e-42 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 143.42 E-value: 2.67e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLekSFDIGDSKvkILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfr 83
Cdd:COG4619 1 LELEGL--SFRVGGKP--ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEW---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 84 RHKIGFIFQQFNLIP--VfsaEENVGLPLLLDNvsQKKATMTATRLLELVGLKGKEKHLPA-QLSGGQQQRVAIARAFAN 160
Cdd:COG4619 73 RRQVAYVPQEPALWGgtV---RDNLPFPFQLRE--RKFDRERALELLERLGLPPDILDKPVeRLSGGERQRLALIRALLL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 872553587 161 EPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVAAH-ADKVVFLLDGEV 221
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
4-222 |
3.91e-42 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 146.00 E-value: 3.91e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLEKSFdiGDSKVkILKGINLQIQKGDFVCIMGASGSGKttllqllggldiPSVGSIRVDGTEISTLKEKELalfR 83
Cdd:COG1125 2 IEFENVTKRY--PDGTV-AVDDLSLTIPAGEFTVLVGPSGCGKtttlrminrliePTSGRILIDGEDIRDLDPVEL---R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 84 RHkIGFIFQQFNLIPVFSAEENVGL-PLLLdNVSQKKATMTATRLLELVGLKGKE--KHLPAQLSGGQQQRVAIARAFAN 160
Cdd:COG1125 76 RR-IGYVIQQIGLFPHMTVAENIATvPRLL-GWDKERIRARVDELLELVGLDPEEyrDRYPHELSGGQQQRVGVARALAA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 872553587 161 EPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVAAH-ADKVVFLLDGEVI 222
Cdd:COG1125 154 DPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKlGDRIAVMREGRIV 216
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-224 |
7.43e-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: 143.65 E-value: 7.43e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 3 IIEIKRLekSFDIGDskVKILKGINLQIQKGDFVCIMGASGSGK---------TTLlqllggldiPSVGSIRVDGTEIST 73
Cdd:COG1120 1 MLEAENL--SVGYGG--RPVLDDVSLSLPPGEVTALLGPNGSGKstllralagLLK---------PSSGEVLLDGRDLAS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 74 LKEKELAlfRRhkIGFIFQQFNLIPVFSAEENVGL---PLL--LDNVSQKKATMtATRLLELVGLKGKEKHLPAQLSGGQ 148
Cdd:COG1120 68 LSRRELA--RR--IAYVPQEPPAPFGLTVRELVALgryPHLglFGRPSAEDREA-VEEALERTGLEHLADRPVDELSGGE 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 872553587 149 QQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDP-FVAAHADKVVFLLDGEVIHE 224
Cdd:COG1120 143 RQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLnLAARYADRLVLLKDGRIVAQ 219
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-222 |
1.39e-41 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 145.67 E-value: 1.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLEKSFDigdsKVKILKGINLQIQKGDFVCIMGASGSGKttllqllgglDIPSVGSIRVDGTEISTlkekELALFR 83
Cdd:COG1118 3 IEVRNISKRFG----SFTLLDDVSLEIASGELVALLGPSGSGKttllriiaglETPDSGRIVLNGRDLFT----NLPPRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 84 RHkIGFIFQQFNLIPVFSAEENV--GLPLLLDNVSQKKATmtATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANE 161
Cdd:COG1118 75 RR-VGFVFQHYALFPHMTVAENIafGLRVRPPSKAEIRAR--VEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 872553587 162 PAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVAAH-ADKVVFLLDGEVI 222
Cdd:COG1118 152 PEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALElADRVVVMNQGRIE 213
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-227 |
4.20e-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: 147.91 E-value: 4.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 1 MNIIEIKRLEKSFDIGDSKVKILKGINLQIQKGDFVCIMGASGSGKttllqllggldipSV-----------------GS 63
Cdd:COG4172 4 MPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGK-------------SVtalsilrllpdpaahpsGS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 64 IRVDGTEISTLKEKELALFRRHKIGFIFQQ----FNliPVFSAEENVGLPLLL-DNVSQKKATMTATRLLELVGLKGKEK 138
Cdd:COG4172 71 ILFDGQDLLGLSERELRRIRGNRIAMIFQEpmtsLN--PLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDPER 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 139 HL---PAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHD-PFVAAHADKVV 214
Cdd:COG4172 149 RLdayPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDlGVVRRFADRVA 228
|
250
....*....|...
gi 872553587 215 FLLDGEVIhEHAE 227
Cdd:COG4172 229 VMRQGEIV-EQGP 240
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-222 |
4.33e-41 |
|
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: 141.32 E-value: 4.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLEKSFDigdsKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKekelalFR 83
Cdd:cd03296 3 IEVRNVSKRFG----DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP------VQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 84 RHKIGFIFQQFNLIPVFSAEENVGLPLLLDNVSQK--KATMTA--TRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFA 159
Cdd:cd03296 73 ERNVGFVFQHYALFRHMTVFDNVAFGLRVKPRSERppEAEIRAkvHELLKLVQLDWLADRYPAQLSGGQRQRVALARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 872553587 160 NEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVAAH-ADKVVFLLDGEVI 222
Cdd:cd03296 153 VEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEvADRVVVMNKGRIE 216
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-222 |
6.19e-41 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 140.58 E-value: 6.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLEKSFDigdsKVKILKGINLQIQKGDFVCIMGASGSGK----------TTllqllggldiPSVGSIRVDGTEIST 73
Cdd:COG1131 1 IEVRGLTKRYG----DKTALDGVSLTVEPGEIFGLLGPNGAGKtttirmllglLR----------PTSGEVRVLGEDVAR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 74 LKEKelalfRRHKIGFIFQQFNLIPVFSAEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVA 153
Cdd:COG1131 67 DPAE-----VRRRIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 154 IARAFANEPAIILADEPTGALDSENSKNIIAALRNACDElGQTAVVVTHDPFVAAH-ADKVVFLLDGEVI 222
Cdd:COG1131 142 LALALLHDPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERlCDRVAIIDKGRIV 210
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-221 |
1.14e-40 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 143.29 E-value: 1.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 1 MNIIEIKRLEKSFDigdsKVKILKGINLQIQKGDFVCIMGASGSGKttllqllgglDIPSVGSIRVDGTEISTLKEKEla 80
Cdd:COG3839 1 MASLELENVSKSYG----GVEALKDIDLDIEDGEFLVLLGPSGCGKstllrmiaglEDPTSGEILIGGRDVTDLPPKD-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 81 lfRRhkIGFIFQQFNLIPVFSAEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFAN 160
Cdd:COG3839 75 --RN--IAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 161 EPAIILADEPTGALDsenskniiAALRNA--------CDELGQTAVVVTHDPFVA-AHADKVVFLLDGEV 221
Cdd:COG3839 151 EPKVFLLDEPLSNLD--------AKLRVEmraeikrlHRRLGTTTIYVTHDQVEAmTLADRIAVMNDGRI 212
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
4-222 |
1.58e-40 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 139.76 E-value: 1.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLEKSFdigdSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEIS---TLKEKELA 80
Cdd:COG4161 3 IQLKNINCFY----GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsqKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 81 LFRRhKIGFIFQQFNLIPVFSAEEN-VGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFA 159
Cdd:COG4161 79 LLRQ-KVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 872553587 160 NEPAIILADEPTGALDSENSKNIIAALRnacdELGQTA---VVVTHDPFVAAH-ADKVVFLLDGEVI 222
Cdd:COG4161 158 MEPQVLLFDEPTAALDPEITAQVVEIIR----ELSQTGitqVIVTHEVEFARKvASQVVYMEKGRII 220
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-220 |
2.53e-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: 137.13 E-value: 2.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLekSFDIGDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfr 83
Cdd:cd03228 1 IEFKNV--SFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESL---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 84 RHKIGFIFQQFNLipvFSAeenvglpLLLDNVsqkkatmtatrllelvglkgkekhlpaqLSGGQQQRVAIARAFANEPA 163
Cdd:cd03228 75 RKNIAYVPQDPFL---FSG-------TIRENI----------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 872553587 164 IILADEPTGALDSENSKNIIAALRNACDelGQTAVVVTHDPFVAAHADKVVFLLDGE 220
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
4-221 |
1.08e-39 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 140.60 E-value: 1.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLEKSFDigdsKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKElalfr 83
Cdd:PRK10851 3 IEIANIKKSFG----RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 84 rHKIGFIFQQFNLIPVFSAEENV--GLPLL-------LDNVSQKkatmtATRLLELVGLKGKEKHLPAQLSGGQQQRVAI 154
Cdd:PRK10851 74 -RKVGFVFQHYALFRHMTVFDNIafGLTVLprrerpnAAAIKAK-----VTQLLEMVQLAHLADRYPAQLSGGQKQRVAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 872553587 155 ARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVAAH-ADKVVFLLDGEV 221
Cdd:PRK10851 148 ARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEvADRVVVMSQGNI 215
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-224 |
3.10e-39 |
|
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: 137.18 E-value: 3.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLekSFDIGDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGteISTLKEKELALFR 83
Cdd:TIGR04520 1 IEVENV--SFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENLWEIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 84 RhKIGFIFQ----QFNLIPV-----FSAEeNVGLPLllDNVSQKkatmtATRLLELVGLKGKEKHLPAQLSGGQQQRVAI 154
Cdd:TIGR04520 77 K-KVGMVFQnpdnQFVGATVeddvaFGLE-NLGVPR--EEMRKR-----VDEALKLVGMEDFRDREPHLLSGGQKQRVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 155 ARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVAAHADKVVFLLDGEVIHE 224
Cdd:TIGR04520 148 AGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAE 217
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-203 |
1.02e-38 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 135.76 E-value: 1.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 1 MNIIEIKRLEKSFDIGDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKEla 80
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 81 lfrrhkiGFIFQQFNLIPVFSAEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFAN 160
Cdd:COG4525 79 -------GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 872553587 161 EPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHD 203
Cdd:COG4525 152 DPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS 194
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
4-228 |
6.30e-38 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 133.22 E-value: 6.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLEKSFdiGDSKVkiLKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEI---STLKEKELA 80
Cdd:PRK11124 3 IQLNGINCFY--GAHQA--LFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 81 LFRRhKIGFIFQQFNLIPVFSAEEN-VGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFA 159
Cdd:PRK11124 79 ELRR-NVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 872553587 160 NEPAIILADEPTGALDSENSKNIIAALRnacdELGQTA---VVVTHDPFVAAH-ADKVVFLLDGEVIhEHAES 228
Cdd:PRK11124 158 MEPQVLLFDEPTAALDPEITAQIVSIIR----ELAETGitqVIVTHEVEVARKtASRVVYMENGHIV-EQGDA 225
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-226 |
1.16e-37 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 132.52 E-value: 1.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 1 MNIIEIKRLekSFDIGDskVKILKGINLQIQKGDFVCIMGASGSGKttllqllggldiPSVGSIRVDGTEISTlkekela 80
Cdd:COG1121 4 MPAIELENL--TVSYGG--RPVLEDVSLTIPPGEFVAIVGPNGAGKstllkailgllpPTSGTVRLFGKPPRR------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 81 lfRRHKIGFIFQQFNLIPVF--SAEENVGLPL-----LLDNVSqKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVA 153
Cdd:COG1121 73 --ARRRIGYVPQRAEVDWDFpiTVRDVVLMGRygrrgLFRRPS-RADREAVDEALERVGLEDLADRPIGELSGGQQQRVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 872553587 154 IARAFANEPAIILADEPTGALDSENSKNIIAALRNACDElGQTAVVVTHDP-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 ... |
21-224 |
1.87e-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: 1.87e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 21 KILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALfrrhKIGFIFQqfnlipvf 100
Cdd:cd03214 13 TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELAR----KIAYVPQ-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 101 saeenvglpllldnvsqkkatmtatrLLELVGLKG-KEKHLpAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENS 179
Cdd:cd03214 81 --------------------------ALELLGLAHlADRPF-NELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQ 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 872553587 180 KNIIAALRNACDELGQTAVVVTHDP-FVAAHADKVVFLLDGEVIHE 224
Cdd:cd03214 134 IELLELLRRLARERGKTVVMVLHDLnLAARYADRVILLKDGRIVAQ 179
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-227 |
2.91e-37 |
|
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: 138.81 E-value: 2.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLekSFDIGDSKVKILKGINLQIQKGDFVCIMGASGSGK-----------TtllqllggldiPSVGSIRVDGTEIS 72
Cdd:COG2274 474 IELENV--SFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKstllklllglyE-----------PTSGRILIDGIDLR 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 73 TLkekELALFRRHkIGFIFQQFNLipvFSAEenvglplLLDNVSQKKATMTATRL---LELVGLKGKEKHLP-------- 141
Cdd:COG2274 541 QI---DPASLRRQ-IGVVLQDVFL---FSGT-------IRENITLGDPDATDEEIieaARLAGLHDFIEALPmgydtvvg 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 142 ---AQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDelGQTAVVVTHDPFVAAHADKVVFLLD 218
Cdd:COG2274 607 eggSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRLADRIIVLDK 684
|
250
....*....|.
gi 872553587 219 GEVIHE--HAE 227
Cdd:COG2274 685 GRIVEDgtHEE 695
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-221 |
5.55e-37 |
|
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: 129.68 E-value: 5.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLEKSFDigdsKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKElalfr 83
Cdd:cd03301 1 VELENVTKRFG----NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 84 rHKIGFIFQQFNLIPVFSAEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPA 163
Cdd:cd03301 72 -RDIAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 872553587 164 IILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVA-AHADKVVFLLDGEV 221
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAmTMADRIAVMNDGQI 209
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
26-222 |
6.16e-37 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 130.26 E-value: 6.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 26 INLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLkekelALFRRhKIGFIFQQFNLIPVFSAEEN 105
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTAL-----PPAER-PVSMLFQENNLFPHLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 106 VGL---PLLLDNVSQKKATMTAtrlLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNI 182
Cdd:COG3840 92 IGLglrPGLKLTAEQRAQVEQA---LERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEM 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 872553587 183 IAALRNACDELGQTAVVVTHDPFVAAH-ADKVVFLLDGEVI 222
Cdd:COG3840 169 LDLVDELCRERGLTVLMVTHDPEDAARiADRVLLVADGRIA 209
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
23-225 |
6.40e-37 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 129.99 E-value: 6.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 23 LKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALFRRhKIGFIFQQFNLIPVFSA 102
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRR-QIGMIFQDHHLLMDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 103 EENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNI 182
Cdd:PRK10908 97 YDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 872553587 183 IaALRNACDELGQTAVVVTHD-PFVAAHADKVVFLLDGEVIHEH 225
Cdd:PRK10908 177 L-RLFEEFNRVGVTVLMATHDiGLISRRSYRMLTLSDGHLHGGV 219
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
21-224 |
9.51e-37 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 130.47 E-value: 9.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 21 KILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEK--ELALFRRH-------KIGFIF 91
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgQLKVADKNqlrllrtRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 92 QQFNLIPVFSAEENV-GLPLLLDNVSQKKATMTATRLLELVGLKGKEK-HLPAQLSGGQQQRVAIARAFANEPAIILADE 169
Cdd:PRK10619 99 QHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAQgKYPVHLSGGQQQRVSIARALAMEPEVLLFDE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 872553587 170 PTGALDSENSKNIIAALRNACDElGQTAVVVTHDPFVAAH-ADKVVFLLDGEVIHE 224
Cdd:PRK10619 179 PTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHvSSHVIFLHQGKIEEE 233
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
21-223 |
1.08e-36 |
|
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: 128.95 E-value: 1.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 21 KILKGINLQIQ---KGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTeisTLKEKELALF---RRHKIGFIFQQF 94
Cdd:cd03297 8 KRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGT---VLFDSRKKINlppQQRKIGLVFQQY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 95 NLIPVFSAEENV--GLPLLldnvSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTG 172
Cdd:cd03297 85 ALFPHLNVRENLafGLKRK----RNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 872553587 173 ALDSENSKNIIAALRNACDELGQTAVVVTHDPFVAAH-ADKVVFLLDGEVIH 223
Cdd:cd03297 161 ALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQY 212
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
23-219 |
1.54e-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: 1.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 23 LKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELAlfrrhkigfIFQQFNLIPVFSA 102
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV---------VFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 103 EENVGLPL--LLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSK 180
Cdd:TIGR01184 72 RENIALAVdrVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 872553587 181 NIIAALRNACDELGQTAVVVTHDPFVAAH-ADKVVFLLDG 219
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTHDVDEALLlSDRVVMLTNG 191
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
38-221 |
1.60e-36 |
|
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: 131.85 E-value: 1.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 38 IMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEIStlkekELALFRRHkIGFIFQQFNLIPVFSAEENVGLPLLLDNVSQ 117
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVT-----NVPPHLRH-INMVFQSYALFPHMTVEENVAFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 118 KKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTA 197
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITF 154
|
170 180
....*....|....*....|....*
gi 872553587 198 VVVTHDPFVA-AHADKVVFLLDGEV 221
Cdd:TIGR01187 155 VFVTHDQEEAmTMSDRIAIMRKGKI 179
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-219 |
3.24e-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: 128.32 E-value: 3.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 1 MN-IIEIKRLEKSFDI---GDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVD----GTEIS 72
Cdd:COG4778 1 MTtLLEVENLSKTFTLhlqGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 73 TLKEKELALFRRHKIGFIFQQFNLIPVFSAEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHL-PAQLSGGQQQR 151
Cdd:COG4778 81 QASPREILALRRRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERLWDLpPATFSGGEQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 152 VAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDElGqTAVV-VTHDP-FVAAHADKVVFLLDG 219
Cdd:COG4778 161 VNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-G-TAIIgIFHDEeVREAVADRVVDVTPF 228
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
21-222 |
7.73e-36 |
|
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: 128.72 E-value: 7.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 21 KILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALFRRhKIGFIFQQfnliP-- 98
Cdd:TIGR04521 19 KALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLRK-KVGLVFQF----Peh 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 99 -VFsaEENV------GlPLLLdNVSQKKATMTATRLLELVGLKG--KEKHlPAQLSGGQQQRVAIARAFANEPAIILADE 169
Cdd:TIGR04521 94 qLF--EETVykdiafG-PKNL-GLSEEEAEERVKEALELVGLDEeyLERS-PFELSGGQMRRVAIAGVLAMEPEVLILDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 872553587 170 PTGALDSENSKNIIAALRNACDELGQTAVVVTHD-PFVAAHADKVVFLLDGEVI 222
Cdd:TIGR04521 169 PTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSmEDVAEYADRVIVMHKGKIV 222
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-224 |
8.57e-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: 127.67 E-value: 8.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLEKSFDigdsKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKelalfR 83
Cdd:COG4555 2 IEVENLSKKYG----KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-----A 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 84 RHKIGFIFQQFNLIPVFSAEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPA 163
Cdd:COG4555 73 RRQIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 872553587 164 IILADEPTGALDSENSKNIIAALRNACDElGQTAVVVTHDPFVAAH-ADKVVFLLDGEVIHE 224
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQ 213
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
22-222 |
2.06e-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: 2.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 22 ILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTlkekelalfRRHKIGFIFQQFNLIPVF- 100
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK---------ERKRIGYVPQRRSIDRDFp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 101 -SAEENVGLPLLLDNVSQKKATMT----ATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGALD 175
Cdd:cd03235 85 iSVRDVVLMGLYGHKGLFRRLSKAdkakVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 872553587 176 SENSKNIIAALRNACDElGQTAVVVTHDPF-VAAHADKVVfLLDGEVI 222
Cdd:cd03235 165 PKTQEDIYELLRELRRE-GMTILVVTHDLGlVLEYFDRVL-LLNRTVV 210
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-227 |
2.54e-35 |
|
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: 132.58 E-value: 2.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLekSFDIGDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfr 83
Cdd:COG4987 334 LELEDV--SFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDL---- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 84 RHKIGFIFQQfnlIPVFSA--EENvglpLLLdnvsqkkATMTAT-----RLLELVGLKGKEKHLP-----------AQLS 145
Cdd:COG4987 408 RRRIAVVPQR---PHLFDTtlREN----LRL-------ARPDATdeelwAALERVGLGDWLAALPdgldtwlgeggRRLS 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 146 GGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDelGQTAVVVTHDPFVAAHADKVVFLLDGEVIHE- 224
Cdd:COG4987 474 GGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLERMDRILVLEDGRIVEQg 551
|
....
gi 872553587 225 -HAE 227
Cdd:COG4987 552 tHEE 555
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
23-171 |
3.41e-35 |
|
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: 123.14 E-value: 3.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 23 LKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKelalFRRHKIGFIFQQFNLIPVFSA 102
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERK----SLRKEIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 872553587 103 EENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHL----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 |
9.29e-35 |
|
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: 123.84 E-value: 9.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLEKSFDigdsKVKILKGINLQIQKGDFVcIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKelalFR 83
Cdd:cd03264 1 LQLENLTKRYG----KKRALDGVSLTLGPGMYG-LLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK----LR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 84 RHkIGFIFQQFNLIPVFSAEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPA 163
Cdd:cd03264 72 RR-IGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 872553587 164 IILADEPTGALDSENSkniiAALRNACDELGQTAVVV--TH---DpfVAAHADKVVFLLDGEVIHE 224
Cdd:cd03264 151 ILIVDEPTAGLDPEER----IRFRNLLSELGEDRIVIlsTHiveD--VESLCNQVAVLNKGKLVFE 210
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
22-227 |
1.84e-34 |
|
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: 129.88 E-value: 1.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 22 ILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfrRHKIGFIFQQfnliPVF- 100
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASW----RRQIAWVPQN----PYLf 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 101 --SAEENVGLpllldnvSQKKATMTA-TRLLELVGLKGKEKHLP-----------AQLSGGQQQRVAIARAFANEPAIIL 166
Cdd:COG4988 424 agTIRENLRL-------GRPDASDEElEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALARALLRDAPLLL 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 872553587 167 ADEPTGALDSENSKNIIAALRNACDelGQTAVVVTHDPFVAAHADKVVFLLDGEVIHE--HAE 227
Cdd:COG4988 497 LDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQADRILVLDDGRIVEQgtHEE 557
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-223 |
2.02e-34 |
|
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: 123.99 E-value: 2.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLEKsfDIGDSKvkiLKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKelalfr 83
Cdd:cd03299 1 LKVENLSK--DWKEFK---LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 84 RHKIGFIFQQFNLIPVFSAEENV--GLPLLLDNVSQKKAtmtatRLLELVGLKGKEkHL----PAQLSGGQQQRVAIARA 157
Cdd:cd03299 70 KRDISYVPQNYALFPHMTVYKNIayGLKKRKVDKKEIER-----KVLEIAEMLGID-HLlnrkPETLSGGEQQRVAIARA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 872553587 158 FANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDpF--VAAHADKVVFLLDGEVIH 223
Cdd:cd03299 144 LVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHD-FeeAWALADKVAIMLNGKLIQ 210
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
28-222 |
4.63e-34 |
|
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: 122.22 E-value: 4.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 28 LQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKElalfrrHKIGFIFQQFNLIPVFSAEENVG 107
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD------RPVSMLFQENNLFAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 108 L---PLLLDNVSQKKATMTAtrlLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIA 184
Cdd:cd03298 93 LglsPGLKLTAEDRQAIEVA---LARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLD 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 872553587 185 ALRNACDELGQTAVVVTHDPFVAAH-ADKVVFLLDGEVI 222
Cdd:cd03298 170 LVLDLHAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIA 208
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-221 |
6.13e-34 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 125.83 E-value: 6.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 1 MNIIEIKRLEKSFDigdSKvKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKela 80
Cdd:PRK09452 12 SPLVELRGISKSFD---GK-EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 81 lfRRHkIGFIFQQFNLIPVFSAEENVGLPLLLDNVSQKKatmTATRLLE---LVGLKGKEKHLPAQLSGGQQQRVAIARA 157
Cdd:PRK09452 85 --NRH-VNTVFQSYALFPHMTVFENVAFGLRMQKTPAAE---ITPRVMEalrMVQLEEFAQRKPHQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 872553587 158 FANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVA-AHADKVVFLLDGEV 221
Cdd:PRK09452 159 VVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEAlTMSDRIVVMRDGRI 223
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-220 |
1.09e-33 |
|
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: 119.66 E-value: 1.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 5 EIKRLEKSFDigdsKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfrR 84
Cdd:cd00267 1 EIENLSFRYG----GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL----R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 85 HKIGFIFQqfnlipvfsaeenvglpllldnvsqkkatmtatrllelvglkgkekhlpaqLSGGQQQRVAIARAFANEPAI 164
Cdd:cd00267 73 RRIGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 872553587 165 ILADEPTGALDSENSKNIIAALRNACDElGQTAVVVTHDP-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 |
1.75e-33 |
|
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: 121.39 E-value: 1.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLEKSFDigdsKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELAlfr 83
Cdd:cd03219 1 LEVRGLTKRFG----GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 84 RHKIGFIFQQFNLIPVFSAEENV--------GLPLLLDNVSQKKATMT--ATRLLELVGLKGKEKHLPAQLSGGQQQRVA 153
Cdd:cd03219 74 RLGIGRTFQIPRLFPELTVLENVmvaaqartGSGLLLARARREEREARerAEELLERVGLADLADRPAGELSYGQQRRLE 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 872553587 154 IARAFANEPAIILADEPTGALDSENSKNIIAALRNACDElGQTAVVVTHD-PFVAAHADKVVFLLDGEVIHE 224
Cdd:cd03219 154 IARALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDmDVVMSLADRVTVLDQGRVIAE 224
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-229 |
4.91e-33 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 120.91 E-value: 4.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 3 IIEIKRLekSFDIGDSKVkiLKGINLQIQKGDFVCIMGASGSGKttllql--lggldIPSV---GSIRVDGTEISTlKEK 77
Cdd:COG1117 11 KIEVRNL--NVYYGDKQA--LKDINLDIPENKVTALIGPSGCGKstllrclnrmndlIPGArveGEILLDGEDIYD-PDV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 78 ELALFRRhKIGFIFQQFNLIPvFSAEENVGLPLLLDNVSqKKATMTAT--RLLELVGL----KGKEKHLPAQLSGGQQQR 151
Cdd:COG1117 86 DVVELRR-RVGMVFQKPNPFP-KSIYDNVAYGLRLHGIK-SKSELDEIveESLRKAALwdevKDRLKKSALGLSGGQQQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 152 VAIARAFANEPAIILADEPTGALDSENSKNIIAALRnacdELGQ--TAVVVTHDPFVAAH-ADKVVFLLDGEVIhEHAES 228
Cdd:COG1117 163 LCIARALAVEPEVLLMDEPTSALDPISTAKIEELIL----ELKKdyTIVIVTHNMQQAARvSDYTAFFYLGELV-EFGPT 237
|
.
gi 872553587 229 K 229
Cdd:COG1117 238 E 238
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-221 |
1.21e-32 |
|
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: 117.32 E-value: 1.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLekSFDIGDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKElalFR 83
Cdd:cd03246 1 LEVENV--SFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNE---LG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 84 RHkIGFIFQQFNLipvFSAEenvglplLLDNVsqkkatmtatrllelvglkgkekhlpaqLSGGQQQRVAIARAFANEPA 163
Cdd:cd03246 76 DH-VGYLPQDDEL---FSGS-------IAENI----------------------------LSGGQRQRLGLARALYGNPR 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 872553587 164 IILADEPTGALDSENSKNIIAALRNAcDELGQTAVVVTHDPFVAAHADKVVFLLDGEV 221
Cdd:cd03246 117 ILVLDEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
3-229 |
2.83e-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: 118.55 E-value: 2.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 3 IIEIKRLEKSFdiGDSKVkiLKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLD--IPSV---GSIRVDGTEISTLKEK 77
Cdd:TIGR00972 1 AIEIENLNLFY--GEKEA--LKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNdlVPGVrieGKVLFDGQDIYDKKID 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 78 ELALfrRHKIGFIFQQFNLIPvFSAEENVGLPLLLDNV-SQKKATMTATRLLELVGL----KGKEKHLPAQLSGGQQQRV 152
Cdd:TIGR00972 77 VVEL--RRRVGMVFQKPNPFP-MSIYDNIAYGPRLHGIkDKKELDEIVEESLKKAALwdevKDRLHDSALGLSGGQQQRL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 872553587 153 AIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELgqTAVVVTHDPFVAAH-ADKVVFLLDGEVIhEHAESK 229
Cdd:TIGR00972 154 CIARALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKKY--TIVIVTHNMQQAARiSDRTAFFYDGELV-EYGPTE 228
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-203 |
8.50e-32 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 120.33 E-value: 8.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 3 IIEIKRLEKSFDiGDSKVKilkGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEIStlkekELALF 82
Cdd:PRK11607 19 LLEIRNLTKSFD-GQHAVD---DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS-----HVPPY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 83 RRhKIGFIFQQFNLIPVFSAEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEP 162
Cdd:PRK11607 90 QR-PINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRP 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 872553587 163 AIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHD 203
Cdd:PRK11607 169 KLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHD 209
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-224 |
1.23e-31 |
|
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: 117.06 E-value: 1.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 1 MNIIEIKRLEKSFDigdsKVKILKGINLQIQKGDFVCIMGASGSGK---------TTLlqllggldiPSVGSIRVDGTEI 71
Cdd:COG0411 2 DPLLEVRGLTKRFG----GLVAVDDVSLEVERGEIVGLIGPNGAGKttlfnlitgFYR---------PTSGRILFDGRDI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 72 STLKEKELAlfrRHKIGFIFQQFNLIPVFSAEENV---------------GLPLLLDNVSQKKATMTATRLLELVGLKGK 136
Cdd:COG0411 69 TGLPPHRIA---RLGIARTFQNPRLFPELTVLENVlvaaharlgrgllaaLLRLPRARREEREARERAEELLERVGLADR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 137 EKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHD-PFVAAHADKVVF 215
Cdd:COG0411 146 ADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDmDLVMGLADRIVV 225
|
....*....
gi 872553587 216 LLDGEVIHE 224
Cdd:COG0411 226 LDFGRVIAE 234
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-224 |
1.56e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 116.94 E-value: 1.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 1 MNIIEIKRLEKSFdigdSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGG-----LDIPSVGSIRVDGTEISTLK 75
Cdd:PRK14247 1 MNKIEIRDLKVSF----GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRlielyPEARVSGEVYLDGQDIFKMD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 76 EKELalfrRHKIGFIFQQFNLIPVFSAEENVGLPLLLDNVSQKKATMTA--TRLLELVGLKGKEKH---LPA-QLSGGQQ 149
Cdd:PRK14247 77 VIEL----RRRVQMVFQIPNPIPNLSIFENVALGLKLNRLVKSKKELQErvRWALEKAQLWDEVKDrldAPAgKLSGGQQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 872553587 150 QRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELgqTAVVVTHDPFVAAH-ADKVVFLLDGEVIHE 224
Cdd:PRK14247 153 QRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARiSDYVAFLYKGQIVEW 226
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-221 |
6.60e-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: 112.88 E-value: 6.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLEKSFDigdsKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKelalfR 83
Cdd:cd03230 1 IEVRNLSKRYG----KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE-----V 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 84 RHKIGFIFQQFNLIPVFSAEENVglpllldnvsqkkatmtatrllelvglkgkekhlpaQLSGGQQQRVAIARAFANEPA 163
Cdd:cd03230 72 KRRIGYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 872553587 164 IILADEPTGALDSENSKNIIAALRNACDElGQTAVVVTHD-PFVAAHADKVVFLLDGEV 221
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHIlEEAERLCDRVAILNNGRI 173
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
3-203 |
1.19e-30 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 116.37 E-value: 1.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 3 IIEIKRLEKSFDIG-------DSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLK 75
Cdd:COG4608 7 LLEVRDLKKHFPVRgglfgrtVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 76 EKELALFRRhKIGFIFQ--QFNLIPVFSAEENVGLPLLLDNVSQKKATMTATR-LLELVGLKgkEKHL---PAQLSGGQQ 149
Cdd:COG4608 87 GRELRPLRR-RMQMVFQdpYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAeLLELVGLR--PEHAdryPHEFSGGQR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 872553587 150 QRVAIARAFANEPAIILADEPTGALD-SENSK--NIIAALRnacDELGQTAVVVTHD 203
Cdd:COG4608 164 QRIGIARALALNPKLIVCDEPVSALDvSIQAQvlNLLEDLQ---DELGLTYLFISHD 217
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
17-227 |
1.51e-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: 1.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 17 DSKVKILKGINLQIQKGDFVCIMGASGSGKttllqllggldiPSVGSIRVDGTEISTLKEKELalfrRHKIGFIFQQFNL 96
Cdd:COG1132 350 PGDRPVLKDISLTIPPGETVALVGPSGSGKstlvnlllrfydPTSGRILIDGVDIRDLTLESL----RRQIGVVPQDTFL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 97 ipvFSA--EENVGLpllldnvSQKKATMTA-TRLLELVGLKGKEKHLP-----------AQLSGGQQQRVAIARAFANEP 162
Cdd:COG1132 426 ---FSGtiRENIRY-------GRPDATDEEvEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARALLKDP 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 872553587 163 AIILADEPTGALDSENSKNIIAALRNACDelGQTAVVVTHDPFVAAHADKVVFLLDGEVIHE--HAE 227
Cdd:COG1132 496 PILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRNADRILVLDDGRIVEQgtHEE 560
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-213 |
2.54e-30 |
|
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: 112.19 E-value: 2.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLEKSFDigdsKVKILKGINLQIQKGDFVCIMGASGSGK----------TTllqllggldiPSVGSIRVDGTEIst 73
Cdd:COG4133 3 LEAENLSCRRG----ERLLFSGLSFTLAAGEALALTGPNGSGKttllrilaglLP----------PSAGEVLWNGEPI-- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 74 lkEKELALFRRHkIGFIFQQFNLIPVFSAEENVGLPLLLDNVSQkkATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVA 153
Cdd:COG4133 67 --RDAREDYRRR-LAYLGHADGLKPELTVRENLRFWAALYGLRA--DREAIDEALEAVGLAGLADLPVRQLSAGQKRRVA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 154 IARAFANEPAIILADEPTGALDSENSKNIIAALRNACDElGQTAVVVTHDPFVAAHADKV 213
Cdd:COG4133 142 LARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLAR-GGAVLLTTHQPLELAAARVL 200
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-222 |
2.96e-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: 118.25 E-value: 2.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 3 IIEIKRLEKSFDI-------GDSKVKILKGINLQIQKGDFVCIMGASGSGKttllqllggldIPSVGSIRVDGTEISTLK 75
Cdd:COG4172 275 LLEARDLKVWFPIkrglfrrTVGHVKAVDGVSLTLRRGETLGLVGESGSGKstlgl-allrlIPSEGEIRFDGQDLDGLS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 76 EKELALFRRHkIGFIFQ----QFNliPVFSAEENVGLPLLLDNVSQKKATMTA--TRLLELVGLKGKEKH-LPAQLSGGQ 148
Cdd:COG4172 354 RRALRPLRRR-MQVVFQdpfgSLS--PRMTVGQIIAEGLRVHGPGLSAAERRArvAEALEEVGLDPAARHrYPHEFSGGQ 430
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 872553587 149 QQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHD-PFVAAHADKVVFLLDGEVI 222
Cdd:COG4172 431 RQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDlAVVRALAHRVMVMKDGKVV 505
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
3-222 |
3.32e-30 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 115.56 E-value: 3.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 3 IIEIKRLEKsfdigDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLK-EKElal 81
Cdd:NF040840 1 MIRIENLSK-----DWKEFKLRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPpEKR--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 82 frrhKIGFIFQQFNLIPVFSAEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANE 161
Cdd:NF040840 73 ----GIAYVYQNYMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 872553587 162 PAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDpFVAA--HADKVVFLLDGEVI 222
Cdd:NF040840 149 PKLLLLDEPLSALDVQTRDELIREMKRWHREFGFTAIHVTHN-FEEAlsLADRVGIMLNGRLS 210
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
27-221 |
8.91e-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: 111.11 E-value: 8.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 27 NLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLkekelALFRRhKIGFIFQQFNLIPVFSAEENV 106
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGL-----APYQR-PVSMLFQENNLFAHLTVRQNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 107 GL---PLLLDNVSQKKATMTATRLlelVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNII 183
Cdd:TIGR01277 92 GLglhPGLKLNAEQQEKVVDAAQQ---VGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEML 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 872553587 184 AALRNACDELGQTAVVVTHDPF-VAAHADKVVFLLDGEV 221
Cdd:TIGR01277 169 ALVKQLCSERQRTLLMVTHHLSdARAIASQIAVVSQGKI 207
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
22-203 |
1.28e-29 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 111.72 E-value: 1.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 22 ILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKElalfrrhkiGFIFQQFNLIPVFS 101
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER---------GVVFQNEGLLPWRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 102 AEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKN 181
Cdd:PRK11248 87 VQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQ 166
|
170 180
....*....|....*....|..
gi 872553587 182 IIAALRNACDELGQTAVVVTHD 203
Cdd:PRK11248 167 MQTLLLKLWQETGKQVLLITHD 188
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
20-227 |
1.35e-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: 111.48 E-value: 1.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 20 VKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfrRHKIGFIFQQFNLIPV 99
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWL----RSQIGLVSQEPVLFDG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 100 fSAEENVGLPlllDNVSQKKATMTATRLLE--------------LVGLKGkekhlpAQLSGGQQQRVAIARAFANEPAII 165
Cdd:cd03249 92 -TIAENIRYG---KPDATDEEVEEAAKKANihdfimslpdgydtLVGERG------SQLSGGQKQRIAIARALLRNPKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 872553587 166 LADEPTGALDSENSKNIIAALRNACdeLGQTAVVVTHDPFVAAHADKVVFLLDGEVIHE--HAE 227
Cdd:cd03249 162 LLDEATSALDAESEKLVQEALDRAM--KGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQgtHDE 223
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-222 |
4.19e-29 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 112.51 E-value: 4.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 2 NIIEIKRLEKSFdiGDSKVkiLKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEI--STLKEKEl 79
Cdd:PRK11432 5 NFVVLKNITKRF--GSNTV--IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVthRSIQQRD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 80 alfrrhkIGFIFQQFNLIPVFSAEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFA 159
Cdd:PRK11432 80 -------ICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 872553587 160 NEPAIILADEPTGALDSenskNIIAALRNACDELGQ----TAVVVTHDPFVA-AHADKVVFLLDGEVI 222
Cdd:PRK11432 153 LKPKVLLFDEPLSNLDA----NLRRSMREKIRELQQqfniTSLYVTHDQSEAfAVSDTVIVMNKGKIM 216
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-224 |
4.48e-29 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 110.88 E-value: 4.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 2 NIIEIKRLekSFDIGDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTeisTLKEKELAL 81
Cdd:PRK13635 4 EIIRVEHI--SFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM---VLSEETVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 82 FRRhKIGFIFQ----QFNLIPV-----FSAEeNVGLP--LLLDNVSQKkatmtatrlLELVGLKGKEKHLPAQLSGGQQQ 150
Cdd:PRK13635 79 VRR-QVGMVFQnpdnQFVGATVqddvaFGLE-NIGVPreEMVERVDQA---------LRQVGMEDFLNREPHRLSGGQKQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 872553587 151 RVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVAAHADKVVFLLDGEVIHE 224
Cdd:PRK13635 148 RVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEE 221
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-221 |
5.27e-29 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 110.15 E-value: 5.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 6 IKRLEKSFdiGDSKVkiLKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKelalfrrh 85
Cdd:PRK11247 15 LNAVSKRY--GERTV--LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARED-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 86 kIGFIFQQFNLIPVFSAEENVGLPLlldnvsQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAII 165
Cdd:PRK11247 83 -TRLMFQDARLLPWKKVIDNVGLGL------KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 872553587 166 LADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVA-AHADKVVFLLDGEV 221
Cdd:PRK11247 156 LLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAvAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-221 |
8.88e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 110.21 E-value: 8.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 1 MNIIEIKRLEKSFDiGDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELa 80
Cdd:PRK13650 2 SNIIEVKNLTFKYK-EDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDI- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 81 lfrRHKIGFIFQ----QFNLIPVfsaEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIAR 156
Cdd:PRK13650 80 ---RHKIGMVFQnpdnQFVGATV---EDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 872553587 157 AFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVAAHADKVVFLLDGEV 221
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
4-222 |
1.12e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 109.70 E-value: 1.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLekSFDIGDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfr 83
Cdd:PRK13632 8 IKVENV--SFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEI---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 84 RHKIGFIFQ----QFNLIpvfSAEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFA 159
Cdd:PRK13632 82 RKKIGIIFQnpdnQFIGA---TVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 872553587 160 NEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVAAHADKVVFLLDGEVI 222
Cdd:PRK13632 159 LNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLI 221
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-224 |
1.52e-28 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 109.02 E-value: 1.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLEKSFdiGDSKVkiLKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELAlfr 83
Cdd:COG4604 2 IEIKNVSKRY--GGKVV--LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELA--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 84 rhKIGFIFQQFNLIPV-FSAEENVGL---PLlldnvSQ-------KKATMTATRLLELVGLKgkEKHLPaQLSGGQQQRV 152
Cdd:COG4604 75 --KRLAILRQENHINSrLTVRELVAFgrfPY-----SKgrltaedREIIDEAIAYLDLEDLA--DRYLD-ELSGGQRQRA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 872553587 153 AIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHD-PFVAAHADKVVFLLDGEVIHE 224
Cdd:COG4604 145 FIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDiNFASCYADHIVAMKDGRVVAQ 217
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
4-222 |
1.60e-28 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 108.06 E-value: 1.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLEKSFDigDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfR 83
Cdd:cd03245 3 IEFRNVSFSYP--NQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADL---R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 84 RHkIGFIFQQFNLipvFSAEenvglplLLDNVSQKKATMTATRLLELVGLKGKEKHLP--------------AQLSGGQQ 149
Cdd:cd03245 78 RN-IGYVPQDVTL---FYGT-------LRDNITLGAPLADDERILRAAELAGVTDFVNkhpngldlqigergRGLSGGQR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 872553587 150 QRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDelGQTAVVVTHDPFVAAHADKVVFLLDGEVI 222
Cdd:cd03245 147 QAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
25-224 |
1.85e-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: 108.22 E-value: 1.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 25 GINLQIQKGDFVCIMGASGSGKTTLLQLLG----GLDIPSVGSIRVDGTEISTLKekelalFRRHKIGFIFQQ----FNl 96
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSLTCLAILgllpPGLTQTSGEILLDGRPLLPLS------IRGRHIATIMQNprtaFN- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 97 iPVFSAEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHL---PAQLSGGQQQRVAIARAFANEPAIILADEPTGA 173
Cdd:TIGR02770 77 -PLFTMGNHAIETLRSLGKLSKQARALILEALEAVGLPDPEEVLkkyPFQLSGGMLQRVMIALALLLEPPFLIADEPTTD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 872553587 174 LDSENSKNIIAALRNACDELGQTAVVVTHDPFVAAH-ADKVVFLLDGEVIHE 224
Cdd:TIGR02770 156 LDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARiADEVAVMDDGRIVER 207
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
23-216 |
2.97e-28 |
|
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: 112.38 E-value: 2.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 23 LKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKelalFRRHKIGFIFQQFNLIPVfSA 102
Cdd:TIGR02857 338 LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADAD----SWRDQIAWVPQHPFLFAG-TI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 103 EENVGLpllldnvSQKKATMTAT-RLLELVGLKGKEKHLP-----------AQLSGGQQQRVAIARAFANEPAIILADEP 170
Cdd:TIGR02857 413 AENIRL-------ARPDASDAEIrEALERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLALARAFLRDAPLLLLDEP 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 872553587 171 TGALDSENSKNIIAALRNACDelGQTAVVVTHDPFVAAHADKVVFL 216
Cdd:TIGR02857 486 TAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALADRIVVL 529
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-222 |
3.06e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 108.73 E-value: 3.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 2 NIIEIKRLekSFDIGDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIP---SVGSIRVDGTeisTLKEKE 78
Cdd:PRK13640 4 NIVEFKHV--SFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGI---TLTAKT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 79 LALFRrHKIGFIFQ----QFNLIPVfsaEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAI 154
Cdd:PRK13640 79 VWDIR-EKVGIVFQnpdnQFVGATV---GDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 872553587 155 ARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVAAHADKVVFLLDGEVI 222
Cdd:PRK13640 155 AGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLL 222
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
17-227 |
3.17e-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: 107.70 E-value: 3.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 17 DSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKekeLALFRRHkIGFIFQQ--- 93
Cdd:cd03253 11 DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVT---LDSLRRA-IGVVPQDtvl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 94 FNL---------------IPVFSAEENVGLPLLLDNVSQKKATMTATRllelvGLKgkekhlpaqLSGGQQQRVAIARAF 158
Cdd:cd03253 87 FNDtigynirygrpdatdEEVIEAAKAAQIHDKIMRFPDGYDTIVGER-----GLK---------LSGGEKQRVAIARAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 872553587 159 ANEPAIILADEPTGALDSENSKNIIAALRNACDelGQTAVVVTHDPFVAAHADKVVFLLDGEVIHE--HAE 227
Cdd:cd03253 153 LKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVNADKIIVLKDGRIVERgtHEE 221
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
22-216 |
8.36e-28 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 106.03 E-value: 8.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 22 ILKGINLQIQKGDFVCIMGASGSGKT---TLLQLLGGLDIPSVGSIRVDGTEISTLKekelALFRRhkIGFIFQQFNLIP 98
Cdd:COG4136 16 LLAPLSLTVAPGEILTLMGPSGSGKStllAAIAGTLSPAFSASGEVLLNGRRLTALP----AEQRR--IGILFQDDLLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 99 VFSAEENV--GLPlllDNV--SQKKATMTATrlLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGAL 174
Cdd:COG4136 90 HLSVGENLafALP---PTIgrAQRRARVEQA--LEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 872553587 175 DSENSKNIIAALRNACDELGQTAVVVTHDPFVAAHADKVVFL 216
Cdd:COG4136 165 DAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAAGRVLDL 206
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
23-246 |
1.13e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 107.48 E-value: 1.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 23 LKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGteISTLKEKELALFRRhKIGFIFQQ-FNLIPVFS 101
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEENLWDIRN-KAGMVFQNpDNQIVATI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 102 AEENVGL-PLLLdNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSK 180
Cdd:PRK13633 103 VEEDVAFgPENL-GIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRR 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 872553587 181 NIIAALRNACDELGQTAVVVTHDPFVAAHADKVVFLLDGEVIHEHAEskgwkfRNIPQQVTHIQEI 246
Cdd:PRK13633 182 EVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTP------KEIFKEVEMMKKI 241
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
3-224 |
1.99e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 106.70 E-value: 1.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 3 IIEIKRLEKSFDIGDSkvkILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALf 82
Cdd:PRK13639 1 ILETRDLKYSYPDGTE---ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEV- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 83 rRHKIGFIFQQF-NLIPVFSAEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANE 161
Cdd:PRK13639 77 -RKTVGIVFQNPdDQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 872553587 162 PAIILADEPTGALDSENSKNIIAALRNACDElGQTAVVVTHD-PFVAAHADKVVFLLDGEVIHE 224
Cdd:PRK13639 156 PEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDvDLVPVYADKVYVMSDGKIIKE 218
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
12-227 |
2.12e-27 |
|
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: 105.39 E-value: 2.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 12 SFDIGDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfrRHKIGFIF 91
Cdd:cd03251 7 TFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASL----RRQIGLVS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 92 QQFNLipvFSA--EENV--GLPllldNVSQKKAtMTATRLLEL--------------VGLKGkekhlpAQLSGGQQQRVA 153
Cdd:cd03251 83 QDVFL---FNDtvAENIayGRP----GATREEV-EEAARAANAhefimelpegydtvIGERG------VKLSGGQRQRIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 872553587 154 IARAFANEPAIILADEPTGALDSENSKNIIAALrnacDEL--GQTAVVVTHDPFVAAHADKVVFLLDGEVIHE--HAE 227
Cdd:cd03251 149 IARALLKDPPILILDEATSALDTESERLVQAAL----ERLmkNRTTFVIAHRLSTIENADRIVVLEDGKIVERgtHEE 222
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-222 |
7.73e-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: 103.11 E-value: 7.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 5 EIKRLekSFDIGDSKvKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEIstlKEKElalfRR 84
Cdd:cd03226 1 RIENI--SFSYKKGT-EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKE----RR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 85 HKIGFIFQ----QFNLIPVFSaEENVGLPLLLDNVSQKKATMtatRLLELVGLKgkEKHlPAQLSGGQQQRVAIARAFAN 160
Cdd:cd03226 71 KSIGYVMQdvdyQLFTDSVRE-ELLLGLKELDAGNEQAETVL---KDLDLYALK--ERH-PLSLSGGQKQRLAIAAALLS 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 872553587 161 EPAIILADEPTGALDSENSKNIIAALRNACDElGQTAVVVTHDP-FVAAHADKVVFLLDGEVI 222
Cdd:cd03226 144 GKDLLIFDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYeFLAKVCDRVLLLANGAIV 205
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
18-221 |
8.02e-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: 108.68 E-value: 8.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 18 SKVKILKGINLQIQKGDFVCIMGASGSGK-----------TtllqllggldiPSVGSIRVDGTEISTLKEKELAlfrRHk 86
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKstlarllvgvwP-----------PTAGSVRLDGADLSQWDREELG---RH- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 87 IGFIFQQFNLipvFSA--EENVGLpllLDNVSQKKATMTATR--LLELVGlkgkekHLP-----------AQLSGGQQQR 151
Cdd:COG4618 408 IGYLPQDVEL---FDGtiAENIAR---FGDADPEKVVAAAKLagVHEMIL------RLPdgydtrigeggARLSGGQRQR 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 152 VAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDElGQTAVVVTHDPFVAAHADKVVFLLDGEV 221
Cdd:COG4618 476 IGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPSLLAAVDKLLVLRDGRV 544
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
22-222 |
9.47e-27 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 104.08 E-value: 9.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 22 ILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALFRrhkiGFIFQQFNLIPVFS 101
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRR----AVLPQHSSLSFPFT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 102 AEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFA------NEPAIILADEPTGALD 175
Cdd:PRK13548 93 VEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 872553587 176 SENSKNIIAALRNACDELGQTAVVVTHDPFVAAH-ADKVVFLLDGEVI 222
Cdd:PRK13548 173 LAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARyADRIVLLHQGRLV 220
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-224 |
9.65e-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: 103.22 E-value: 9.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 3 IIEIKRLEKSFDIGDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGteISTLKEKELAlf 82
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVKEPAEA-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 83 rRHKIGFIFQQFNLIPVFSAEENVGLPLLLDNVSQKKATmtaTRLLELVGLKGKEKHLP---AQLSGGQQQRVAIARAFA 159
Cdd:cd03266 77 -RRRLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELT---ARLEELADRLGMEELLDrrvGGFSTGMRQKVAIARALV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 872553587 160 NEPAIILADEPTGALDSENSKNIIAALRNACDElGQTAVVVTHD-PFVAAHADKVVFLLDGEVIHE 224
Cdd:cd03266 153 HDPPVLLLDEPTTGLDVMATRALREFIRQLRAL-GKCILFSTHImQEVERLCDRVVVLHRGRVVYE 217
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
16-238 |
1.17e-26 |
|
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: 103.72 E-value: 1.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 16 GDSKVkILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLkekELALFRRhKIGFIFQqfn 95
Cdd:cd03252 12 PDGPV-ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALA---DPAWLRR-QVGVVLQ--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 96 lipvfsaeENVGLP-LLLDNVSQKKATMTATRLLELVGLKGKEK---HLP-----------AQLSGGQQQRVAIARAFAN 160
Cdd:cd03252 84 --------ENVLFNrSIRDNIALADPGMSMERVIEAAKLAGAHDfisELPegydtivgeqgAGLSGGQRQRIAIARALIH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 161 EPAIILADEPTGALDSENSKNIIAALRNACDelGQTAVVVTHDPFVAAHADKVVFLLDGEVI----HEHAESKGWKFRNI 236
Cdd:cd03252 156 NPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKNADRIIVMEKGRIVeqgsHDELLAENGLYAYL 233
|
..
gi 872553587 237 PQ 238
Cdd:cd03252 234 YQ 235
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-249 |
1.19e-26 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 104.32 E-value: 1.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 3 IIEIKRLEKSFDigdsKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGgldipsvGSIRVDGTEISTLK------E 76
Cdd:PRK09984 4 IIRVEKLAKTFN----QHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLS-------GLITGDKSAGSHIEllgrtvQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 77 KELALFR-----RHKIGFIFQQFNLIPVFSAEENVGLPLL------------LDNVSQKKATMTATRllelVGLKGKEKH 139
Cdd:PRK09984 73 REGRLARdirksRANTGYIFQQFNLVNRLSVLENVLIGALgstpfwrtcfswFTREQKQRALQALTR----VGMVHFAHQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 140 LPAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHD-PFVAAHADKVVFLLD 218
Cdd:PRK09984 149 RVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQvDYALRYCERIVALRQ 228
|
250 260 270
....*....|....*....|....*....|.
gi 872553587 219 GEVIHEHAESkgwKFRNipQQVTHIQEIMNR 249
Cdd:PRK09984 229 GHVFYDGSSQ---QFDN--ERFDHLYRSINR 254
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
19-224 |
3.00e-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: 102.13 E-value: 3.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 19 KVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELAlfrRHKIGFIFQQFNLIP 98
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERA---RAGIGYVPEGRRIFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 99 VFSAEENVGLPLLLDNVSQKKATMtaTRLLELV-GLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSE 177
Cdd:cd03224 89 ELTVEENLLLGAYARRRAKRKARL--ERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPK 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 872553587 178 NSKNIIAALRNACDElGQTAVVVTHD-PFVAAHADKVVFLLDGEVIHE 224
Cdd:cd03224 167 IVEEIFEAIRELRDE-GVTILLVEQNaRFALEIADRAYVLERGRVVLE 213
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
4-224 |
3.71e-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: 101.92 E-value: 3.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLEKSFDigdSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfr 83
Cdd:cd03254 3 IEFENVNFSYD---EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSL---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 84 RHKIGFIFQQFNLIPVfSAEENVGLPLLLDNVSQKKATMTATRLLELVglkgkeKHLP-----------AQLSGGQQQRV 152
Cdd:cd03254 76 RSMIGVVLQDTFLFSG-TIMENIRLGRPNATDEEVIEAAKEAGAHDFI------MKLPngydtvlgengGNLSQGERQLL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 872553587 153 AIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDelGQTAVVVTHDPFVAAHADKVVFLLDGEVIHE 224
Cdd:cd03254 149 AIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKNADKILVLDDGKIIEE 218
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
26-221 |
4.76e-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: 104.42 E-value: 4.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 26 INLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTeisTLKEKELALF---RRHKIGFIFQQFNLIPVFSA 102
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGR---TLFDSRKGIFlppEKRRIGYVFQEARLFPHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 103 EENVGLPLLLDNVSQKKATMTatRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNI 182
Cdd:TIGR02142 93 RGNLRYGMKRARPSERRISFE--RVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEI 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 872553587 183 IAALRNACDELGQTAVVVTHDPFVAAH-ADKVVFLLDGEV 221
Cdd:TIGR02142 171 LPYLERLHAEFGIPILYVSHSLQEVLRlADRVVVLEDGRV 210
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
18-229 |
6.62e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 101.78 E-value: 6.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 18 SKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLD--IPSV---GSIRVDGTEISTLKEKELALfrRHKIGFIFQ 92
Cdd:PRK14239 16 NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNdlNPEVtitGSIVYNGHNIYSPRTDTVDL--RKEIGMVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 93 QFNLIPvFSAEENVGLPLLLDNVSQKKatmtatRLLELV--GLKG-------KEK-HLPA-QLSGGQQQRVAIARAFANE 161
Cdd:PRK14239 94 QPNPFP-MSIYENVVYGLRLKGIKDKQ------VLDEAVekSLKGasiwdevKDRlHDSAlGLSGGQQQRVCIARVLATS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 872553587 162 PAIILADEPTGALDSENSKNIIAALRNACDELgqTAVVVTHDPFVAAH-ADKVVFLLDGEVIhEHAESK 229
Cdd:PRK14239 167 PKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRiSDRTGFFLDGDLI-EYNDTK 232
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-224 |
1.05e-25 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 101.77 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 1 MNIIEIKRLekSFDIGDSKvkILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELA 80
Cdd:PRK11831 5 ANLVDMRGV--SFTRGNRC--IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 81 LFRRhKIGFIFQQFNLIPVFSAEENVGLPL-----LLDNVSQKKATMTatrlLELVGLKGKEKHLPAQLSGGQQQRVAIA 155
Cdd:PRK11831 81 TVRK-RMSMLFQSGALFTDMNVFDNVAYPLrehtqLPAPLLHSTVMMK----LEAVGLRGAAKLMPSELSGGMARRAALA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 156 RAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHD-PFVAAHADKVVFLLDGEVIHE 224
Cdd:PRK11831 156 RAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDvPEVLSIADHAYIVADKKIVAH 225
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-228 |
1.07e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 101.74 E-value: 1.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 2 NIIEIKRLEKSFDIGDskvKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELal 81
Cdd:PRK13647 3 NIIEVEDLHFRYKDGT---KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWV-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 82 frRHKIGFIFQQfnliP---VFSA--EENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIAR 156
Cdd:PRK13647 78 --RSKVGLVFQD----PddqVFSStvWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 872553587 157 AFANEPAIILADEPTGALDSENSKNIIAALrNACDELGQTAVVVTHD-PFVAAHADKVVFLLDGEVIHEHAES 228
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEIL-DRLHNQGKTVIVATHDvDLAAEWADQVIVLKEGRVLAEGDKS 223
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-224 |
1.25e-25 |
|
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: 104.88 E-value: 1.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLEKSFDigdsKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLD---------------IPSVGSIRV-- 66
Cdd:TIGR03269 1 IEVKNLTKKFD----GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyeptsgriiyhvalCEKCGYVERps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 67 -DGTEI----STLKEKEL-------ALFR--RHKIGFIFQQ-FNLIPVFSAEENVGLPLLLDNVSQKKATMTATRLLELV 131
Cdd:TIGR03269 77 kVGEPCpvcgGTLEPEEVdfwnlsdKLRRriRKRIAIMLQRtFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 132 GLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVAAH-A 210
Cdd:TIGR03269 157 QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDlS 236
|
250
....*....|....
gi 872553587 211 DKVVFLLDGEVIHE 224
Cdd:TIGR03269 237 DKAIWLENGEIKEE 250
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
4-222 |
2.12e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 101.25 E-value: 2.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLEKSFDIGDSKVKI-LKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEIS-TLKEKELAL 81
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFERRaLYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITaGKKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 82 FRRhKIGFIFqQFNLIPVFsaEENVglplLLD--------NVSQKKATMTATRLLELVGLkgKEKHL---PAQLSGGQQQ 150
Cdd:PRK13634 83 LRK-KVGIVF-QFPEHQLF--EETV----EKDicfgpmnfGVSEEDAKQKAREMIELVGL--PEELLarsPFELSGGQMR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 872553587 151 RVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTH---DpfVAAHADKVVFLLDGEVI 222
Cdd:PRK13634 153 RVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHsmeD--AARYADQIVVMHKGTVF 225
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
18-221 |
2.18e-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: 104.35 E-value: 2.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 18 SKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEIstlKEKELALFRRHkIGFIFQQFNLI 97
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADL---KQWDRETFGKH-IGYLPQDVELF 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 98 PVFSAEenvglpllldNVSQKKATMTATRLLELVGLKGKEK---HLP-----------AQLSGGQQQRVAIARAFANEPA 163
Cdd:TIGR01842 405 PGTVAE----------NIARFGENADPEKIIEAAKLAGVHElilRLPdgydtvigpggATLSGGQRQRIALARALYGDPK 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 872553587 164 IILADEPTGALDSENSkniiAALRNACDEL---GQTAVVVTHDPFVAAHADKVVFLLDGEV 221
Cdd:TIGR01842 475 LVVLDEPNSNLDEEGE----QALANAIKALkarGITVVVITHRPSLLGCVDKILVLQDGRI 531
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-223 |
2.27e-25 |
|
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: 99.50 E-value: 2.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLEKSFdiGDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKelalfR 83
Cdd:cd03263 1 LQIRNLTKTY--KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKA-----A 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 84 RHKIGFIFQQFNLIPVFSAEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPA 163
Cdd:cd03263 74 RQSLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 872553587 164 IILADEPTGALDSEnSKNIIAALRNACDElGQTAVVVTHDPFVAAH-ADKVVFLLDGEVIH 223
Cdd:cd03263 154 VLLLDEPTSGLDPA-SRRAIWDLILEVRK-GRSIILTTHSMDEAEAlCDRIAIMSDGKLRC 212
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
4-224 |
2.91e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 101.32 E-value: 2.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLEKSFDIG-DSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIR----------------- 65
Cdd:PRK13651 3 IKVKNIVKIFNKKlPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwifkdeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 66 -VDGTEISTLKEKELALFR--RHKIGFIFqQFNLIPVFSA--EENVGLPLLLDNVSQKKATMTATRLLELVGLkgKEKHL 140
Cdd:PRK13651 83 vLEKLVIQKTRFKKIKKIKeiRRRVGVVF-QFAEYQLFEQtiEKDIIFGPVSMGVSKEEAKKRAAKYIELVGL--DESYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 141 ---PAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDElGQTAVVVTHD-PFVAAHADKVVFL 216
Cdd:PRK13651 160 qrsPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDlDNVLEWTKRTIFF 238
|
....*...
gi 872553587 217 LDGEVIHE 224
Cdd:PRK13651 239 KDGKIIKD 246
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
23-246 |
1.22e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 99.05 E-value: 1.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 23 LKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEI-STLKEKELALFRRhKIGFIFqQFNLIPVFs 101
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItSTSKNKDIKQIRK-KVGLVF-QFPESQLF- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 102 aEENVglplLLD--------NVSQKKATMTATRLLELVGLKGK--EKHlPAQLSGGQQQRVAIARAFANEPAIILADEPT 171
Cdd:PRK13649 100 -EETV----LKDvafgpqnfGVSQEEAEALAREKLALVGISESlfEKN-PFELSGGQMRRVAIAGILAMEPKILVLDEPT 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 872553587 172 GALDSENSKNIIAALRNaCDELGQTAVVVTH---DpfVAAHADKVVFLLDGEVIhehaesKGWKFRNIPQQVTHIQEI 246
Cdd:PRK13649 174 AGLDPKGRKELMTLFKK-LHQSGMTIVLVTHlmdD--VANYADFVYVLEKGKLV------LSGKPKDIFQDVDFLEEK 242
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
23-223 |
3.33e-24 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 100.11 E-value: 3.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 23 LKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALFRRHKIGFIFQQFNLIPVFSA 102
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 103 EENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNI 182
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 872553587 183 IAALRNACDELGQTAVVVTHDPFVAAH-ADKVVFLLDGEVIH 223
Cdd:PRK10070 204 QDELVKLQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQ 245
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
22-224 |
3.52e-24 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 97.84 E-value: 3.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 22 ILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALFRRhKIGFIFQQ----FNli 97
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRR-DIQMVFQDsisaVN-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 98 PVFSAEENVGLPLL-LDNVSQKKATMTATRLLELVGLK-GKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGALD 175
Cdd:PRK10419 104 PRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 872553587 176 SENSKNIIAALRNACDELGQTAVVVTHD-PFVAAHADKVVFLLDGEVIHE 224
Cdd:PRK10419 184 LVLQAGVIRLLKKLQQQFGTACLFITHDlRLVERFCQRVMVMDNGQIVET 233
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
26-222 |
5.32e-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: 98.63 E-value: 5.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 26 INLQIQKGDF------------VC-IMGASGSGK----------TTllqllggldiPSVGSIRVDGTeisTLKEKELALF 82
Cdd:COG4148 5 VDFRLRRGGFtldvdftlpgrgVTaLFGPSGSGKttllraiaglER----------PDSGRIRLGGE---VLQDSARGIF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 83 ----RRHkIGFIFQQFNLIPVFSAEENvglplLLDNVSQKKATMTATRLLELVGLKGKEKHL---PAQLSGGQQQRVAIA 155
Cdd:COG4148 72 lpphRRR-IGYVFQEARLFPHLSVRGN-----LLYGRKRAPRAERRISFDEVVELLGIGHLLdrrPATLSGGERQRVAIG 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 872553587 156 RAFANEPAIILADEPTGALDsENSKN-IIAALRNACDELGQTAVVVTHDPF-VAAHADKVVFLLDGEVI 222
Cdd:COG4148 146 RALLSSPRLLLMDEPLAALD-LARKAeILPYLERLRDELDIPILYVSHSLDeVARLADHVVLLEQGRVV 213
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
12-224 |
6.81e-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: 94.69 E-value: 6.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 12 SFDIGDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKelalfRRHKIGFIF 91
Cdd:cd03247 7 SFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-----LSSLISVLN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 92 QQfnlipvfsaeenvglPLLLDnvsqkkatmtaTRLLELVGlkgkekhlpAQLSGGQQQRVAIARAFANEPAIILADEPT 171
Cdd:cd03247 82 QR---------------PYLFD-----------TTLRNNLG---------RRFSGGERQRLALARILLQDAPIVLLDEPT 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 872553587 172 GALDSENSKNIIAALRNACDElgQTAVVVTHDPFVAAHADKVVFLLDGEVIHE 224
Cdd:cd03247 127 VGLDPITERQLLSLIFEVLKD--KTLIWITHHLTGIEHMDKILFLENGKIIMQ 177
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
22-224 |
8.98e-24 |
|
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: 95.67 E-value: 8.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 22 ILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELAlfrRHKIGFIFQQFNLIPVFS 101
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERA---RAGIAYVPQGREIFPRLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 102 AEENVglpllldnvsqkkatmtatrLLELVGLKGKEKHLPAQ------------------LSGGQQQRVAIARAFANEPA 163
Cdd:TIGR03410 92 VEENL--------------------LTGLAALPRRSRKIPDEiyelfpvlkemlgrrggdLSGGQQQQLAIARALVTRPK 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 872553587 164 IILADEPTGALDSENSKNIIAALRNACDELGQTAVVV-THDPFVAAHADKVVFLLDGEVIHE 224
Cdd:TIGR03410 152 LLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVeQYLDFARELADRYYVMERGRVVAS 213
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
27-224 |
9.97e-24 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 95.80 E-value: 9.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 27 NLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDG-----TEIStlkekelalfrRHKIGFIFQQFNLIPVFS 101
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGqdhttTPPS-----------RRPVSMLFQENNLFSHLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 102 AEENVGL---PLLLDNVSQKKatmTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSEN 178
Cdd:PRK10771 88 VAQNIGLglnPGLKLNAAQRE---KLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPAL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 872553587 179 SKNIIAALRNACDELGQTAVVVTHDPFVAAH-ADKVVFLLDGEVIHE 224
Cdd:PRK10771 165 RQEMLTLVSQVCQERQLTLLMVSHSLEDAARiAPRSLVVADGRIAWD 211
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-222 |
1.55e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 95.68 E-value: 1.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 22 ILKGINLQIQKGDFVCIMGASGSGKTTLLQL-----LGGLDIPSVGSIRVDGTEISTLKEKELALfrRHKIGFIFQQFNL 96
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrllELNEEARVEGEVRLFGRNIYSPDVDPIEV--RREVGMVFQYPNP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 97 IPVFSAEENVGLPLLLDNVSQKKA--------TMTATRLLELVglKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILAD 168
Cdd:PRK14267 97 FPHLTIYDNVAIGVKLNGLVKSKKeldervewALKKAALWDEV--KDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 872553587 169 EPTGALDSENSKNIIAALRNACDELgqTAVVVTHDPFVAAH-ADKVVFLLDGEVI 222
Cdd:PRK14267 175 EPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARvSDYVAFLYLGKLI 227
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-222 |
1.75e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 95.50 E-value: 1.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 22 ILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKE--KELALFRRHKIGFIFQQFNLIPV 99
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDifQIDAIKLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 100 FSAEENVGLPLLLDNVSQKKATMT-ATRLLELVGLkGKEKH----LPA-QLSGGQQQRVAIARAFANEPAIILADEPTGA 173
Cdd:PRK14246 105 LSIYDNIAYPLKSHGIKEKREIKKiVEECLRKVGL-WKEVYdrlnSPAsQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 872553587 174 LDSENSKNIIAALRNACDELgqTAVVVTHDPFVAAH-ADKVVFLLDGEVI 222
Cdd:PRK14246 184 IDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARvADYVAFLYNGELV 231
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-226 |
2.96e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 98.17 E-value: 2.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 3 IIEIKRLEKSFdigdSKVKILKGINLQIQKGDFVCIMGASGSGK-----------TtllqllggldiPSVGSIRVDGTEI 71
Cdd:COG1129 4 LLEMRGISKSF----GGVKALDGVSLELRPGEVHALLGENGAGKstlmkilsgvyQ-----------PDSGEILLDGEPV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 72 STLKEKElAlfRRHKIGFIFQQFNLIPVFSAEENVGLPLLLDN---VSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQ 148
Cdd:COG1129 69 RFRSPRD-A--QAAGIAIIHQELNLVPNLSVAENIFLGREPRRgglIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 149 QQRVAIARAFANEPAIILADEPTGALDSENSKN---IIAALRnacdELGqTAVV-VTHD-PFVAAHADKVVFLLDGEVIH 223
Cdd:COG1129 146 QQLVEIARALSRDARVLILDEPTASLTEREVERlfrIIRRLK----AQG-VAIIyISHRlDEVFEIADRVTVLRDGRLVG 220
|
...
gi 872553587 224 EHA 226
Cdd:COG1129 221 TGP 223
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
21-222 |
4.18e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 95.19 E-value: 4.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 21 KILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRV-DGTEISTLKEKELALFRRhKIGFIFQ------- 92
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgDIVVSSTSKQKEIKPVRK-KVGVVFQfpesqlf 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 93 -QFNLIPVFSAEENVGlpllldnVSQKKATMTATRLLELVGLKGK--EKHlPAQLSGGQQQRVAIARAFANEPAIILADE 169
Cdd:PRK13643 99 eETVLKDVAFGPQNFG-------IPKEKAEKIAAEKLEMVGLADEfwEKS-PFELSGGQMRRVAIAGILAMEPEVLVLDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 872553587 170 PTGALDSENSKNIIaALRNACDELGQTAVVVTH--DPfVAAHADKVVFLLDGEVI 222
Cdd:PRK13643 171 PTAGLDPKARIEMM-QLFESIHQSGQTVVLVTHlmDD-VADYADYVYLLEKGHII 223
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
12-222 |
4.59e-23 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 97.86 E-value: 4.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 12 SFDIGDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKekeLALFRRHkIGFIF 91
Cdd:TIGR02203 337 TFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT---LASLRRQ-VALVS 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 92 QQFNLipvF--SAEENVGLPLLLDNVSQK-KATMTATRLLELVGLKGKEKHLP-----AQLSGGQQQRVAIARAFANEPA 163
Cdd:TIGR02203 413 QDVVL---FndTIANNIAYGRTEQADRAEiERALAAAYAQDFVDKLPLGLDTPigengVLLSGGQRQRLAIARALLKDAP 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 872553587 164 IILADEPTGALDSENSKNIIAALrnacDEL--GQTAVVVTHDPFVAAHADKVVFLLDGEVI 222
Cdd:TIGR02203 490 ILILDEATSALDNESERLVQAAL----ERLmqGRTTLVIAHRLSTIEKADRIVVMDDGRIV 546
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
23-216 |
7.37e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 92.30 E-value: 7.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 23 LKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEistlkekelalfrrhKIGFIFQQFNLIPVF-- 100
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGA---------------RVAYVPQRSEVPDSLpl 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 101 SAEENVGL----PLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGALDS 176
Cdd:NF040873 73 TVRDLVAMgrwaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 872553587 177 ENSKNIIAALRNACDElGQTAVVVTHDPFVAAHADKVVFL 216
Cdd:NF040873 153 ESRERIIALLAEEHAR-GATVVVVTHDLELVRRADPCVLL 191
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
12-222 |
1.19e-22 |
|
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: 96.86 E-value: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 12 SFDIGDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfrRHKIGFIF 91
Cdd:TIGR03375 470 SFAYPGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADL----RRNIGYVP 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 92 QQfnlIPVFSA--EENV--GLPLLLDNVSQKKATMTAtrLLELVGLKGKEKHLP-----AQLSGGQQQRVAIARAFANEP 162
Cdd:TIGR03375 546 QD---PRLFYGtlRDNIalGAPYADDEEILRAAELAG--VTEFVRRHPDGLDMQigergRSLSGGQRQAVALARALLRDP 620
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 163 AIILADEPTGALDSENSKNIIAALRNACdeLGQTAVVVTHDPFVAAHADKVVFLLDGEVI 222
Cdd:TIGR03375 621 PILLLDEPTSAMDNRSEERFKDRLKRWL--AGKTLVLVTHRTSLLDLVDRIIVMDNGRIV 678
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
23-251 |
1.20e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 94.13 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 23 LKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEI-STLKEKELALFRRhKIGFIFQqFNLIPVFs 101
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItPETGNKNLKKLRK-KVSLVFQ-FPEAQLF- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 102 aeENVGL------PLLLdNVSQKKATMTATRLLELVGLKGK-EKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGAL 174
Cdd:PRK13641 100 --ENTVLkdvefgPKNF-GFSEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 872553587 175 DSENSKNIIAALRNAcDELGQTAVVVTHD-PFVAAHADKVVFLLDGEVIhEHAEskgwkfrniPQQVTHIQEIMNRHF 251
Cdd:PRK13641 177 DPEGRKEMMQLFKDY-QKAGHTVILVTHNmDDVAEYADDVLVLEHGKLI-KHAS---------PKEIFSDKEWLKKHY 243
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
21-222 |
1.24e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 93.96 E-value: 1.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 21 KILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEIsTLKEKELALFRRhKIGFIFQ--QFNLIp 98
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDI-TDKKVKLSDIRK-KVGLVFQypEYQLF- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 99 vfsaEE-----------NVGLpllldnvSQKKATMTATRLLELVGLKG---KEKHlPAQLSGGQQQRVAIARAFANEPAI 164
Cdd:PRK13637 98 ----EEtiekdiafgpiNLGL-------SEEEIENRVKRAMNIVGLDYedyKDKS-PFELSGGQKRRVAIAGVVAMEPKI 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 872553587 165 ILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTH---DpfVAAHADKVVFLLDGEVI 222
Cdd:PRK13637 166 LILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHsmeD--VAKLADRIIVMNKGKCE 224
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-222 |
1.65e-22 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 92.98 E-value: 1.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 1 MNIIEIKRLEKSFDIGDS-----KVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLK 75
Cdd:COG4167 2 SALLEVRNLSKTFKYRTGlfrrqQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 76 EKelalFRRHKIGFIFQQFNliPVFSAEENVG----LPLLLD---NVSQKKATMTATrlLELVGLKGKEKHL-PAQLSGG 147
Cdd:COG4167 82 YK----YRCKHIRMIFQDPN--TSLNPRLNIGqileEPLRLNtdlTAEEREERIFAT--LRLVGLLPEHANFyPHMLSSG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 872553587 148 QQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVAAH-ADKVVFLLDGEVI 222
Cdd:COG4167 154 QKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHiSDKVLVMHQGEVV 229
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-222 |
1.92e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 96.05 E-value: 1.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLekSFDIGDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfr 83
Cdd:PRK11160 339 LTLNNV--SFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAL---- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 84 RHKIGFIFQQfnlIPVFSAEenvglplLLDNVSQKKATMTATRL---LELVGLkgkEKHLPA-------------QLSGG 147
Cdd:PRK11160 413 RQAISVVSQR---VHLFSAT-------LRDNLLLAAPNASDEALievLQQVGL---EKLLEDdkglnawlgeggrQLSGG 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 872553587 148 QQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDelGQTAVVVTHDPFVAAHADKVVFLLDGEVI 222
Cdd:PRK11160 480 EQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQFDRICVMDNGQII 552
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-224 |
2.12e-22 |
|
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: 90.18 E-value: 2.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLEKSFdigdSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKElAlfR 83
Cdd:cd03216 1 LELRGITKRF----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD-A--R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 84 RHKIGFIFQqfnlipvfsaeenvglpllldnvsqkkatmtatrllelvglkgkekhlpaqLSGGQQQRVAIARAFANEPA 163
Cdd:cd03216 74 RAGIAMVYQ---------------------------------------------------LSVGERQMVEIARALARNAR 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 872553587 164 IILADEPTGALDSENSKNIIAALRNACDElGQTAVVVTHD-PFVAAHADKVVFLLDGEVIHE 224
Cdd:cd03216 103 LLILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRlDEVFEIADRVTVLRDGRVVGT 163
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-224 |
2.13e-22 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 92.49 E-value: 2.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLekSFDIGdsKVKILKGINLQIQKGDFVCIMGASGSGK-----------TtllqllggldiPSVGSIRVDGTEIS 72
Cdd:COG4559 2 LEAENL--SVRLG--GRTLLDDVSLTLRPGELTAIIGPNGAGKstllklltgelT-----------PSSGEVRLNGRPLA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 73 TLKEKELALFR-----RHKIGFifqqfnliPvFSAEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGG 147
Cdd:COG4559 67 AWSPWELARRRavlpqHSSLAF--------P-FTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 148 QQQRVAIARAFA-------NEPAIILADEPTGALDSENSKNIIAALRNACDElGQTAVVVTHDPFVAAH-ADKVVFLLDG 219
Cdd:COG4559 138 EQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQyADRILLLHQG 216
|
....*
gi 872553587 220 EVIHE 224
Cdd:COG4559 217 RLVAQ 221
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
3-229 |
2.15e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 93.23 E-value: 2.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 3 IIEIKRLEKSFDiGDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalf 82
Cdd:PRK13642 4 ILEVENLVFKYE-KESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNL--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 83 rRHKIGFIFQQ-FNLIPVFSAEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANE 161
Cdd:PRK13642 80 -RRKIGMVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 872553587 162 PAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVAAHADKVVFLLDGEVIHEHAESK 229
Cdd:PRK13642 159 PEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSE 226
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
26-222 |
2.57e-22 |
|
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: 92.59 E-value: 2.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 26 INLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDG-----TEISTLKEKELALFRRHKIGFIFQQF--NLIP 98
Cdd:TIGR02323 22 VSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMrsgaeLELYQLSEAERRRLMRTEWGFVHQNPrdGLRM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 99 VFSAEENVGLPLLLDNVSQ-KKATMTATRLLELVGL-KGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGALDS 176
Cdd:TIGR02323 102 RVSAGANIGERLMAIGARHyGNIRATAQDWLEEVEIdPTRIDDLPRAFSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDV 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 872553587 177 ENSKNIIAALRNACDELGQTAVVVTHDPFVAA-HADKVVFLLDGEVI 222
Cdd:TIGR02323 182 SVQARLLDLLRGLVRDLGLAVIIVTHDLGVARlLAQRLLVMQQGRVV 228
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-221 |
3.17e-22 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 93.75 E-value: 3.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 1 MNIIEIKRLEKSFDigdSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKEla 80
Cdd:PRK11650 1 MAGLKLQAVRKSYD---GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 81 lfrrHKIGFIFQQFNLIPVFSAEENVGLPLLLDNVSqkKATMT-----ATRLLELvglkgkEKHL---PAQLSGGQQQRV 152
Cdd:PRK11650 76 ----RDIAMVFQNYALYPHMSVRENMAYGLKIRGMP--KAEIEervaeAARILEL------EPLLdrkPRELSGGQRQRV 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 872553587 153 AIARAFANEPAIILADEPTGALDsenskniiAALRNA-CDE-------LGQTAVVVTHDPfVAAH--ADKVVFLLDGEV 221
Cdd:PRK11650 144 AMGRAIVREPAVFLFDEPLSNLD--------AKLRVQmRLEiqrlhrrLKTTSLYVTHDQ-VEAMtlADRVVVMNGGVA 213
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
4-222 |
3.33e-22 |
|
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: 90.69 E-value: 3.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLEKSFDIGDSKVK--ILKGINLQIQKGDFVCIMGASGSGKTT-LLQLLGGLDIPSV-GSIRVDGTEIStlkekeL 79
Cdd:cd03213 4 LSFRNLTVTVKSSPSKSGkqLLKNVSGKAKPGELTAIMGPSGAGKSTlLNALAGRRTGLGVsGEVLINGRPLD------K 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 80 ALFRRHkIGFIFQQFNLIPVFSAEENVGlpllldnvsqkkatMTAtrllelvGLKGkekhlpaqLSGGQQQRVAIARAFA 159
Cdd:cd03213 78 RSFRKI-IGYVPQDDILHPTLTVRETLM--------------FAA-------KLRG--------LSGGERKRVSIALELV 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 872553587 160 NEPAIILADEPTGALDSENSKNIIAALRNACDElGQTAVVVTHDP--FVAAHADKVVFLLDGEVI 222
Cdd:cd03213 128 SNPSLLFLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHQPssEIFELFDKLLLLSQGRVI 191
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-203 |
5.29e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 91.69 E-value: 5.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 3 IIEIKRLEKSFDIG-DSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEkelal 81
Cdd:COG1101 1 MLELKNLSKTFNPGtVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPE----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 82 FRRHK-IGFIFQQ------FNLipvfSAEENvglpLLL-DNVSQKK----ATMTATR-----LLELVGLkGKEKHLPAQ- 143
Cdd:COG1101 76 YKRAKyIGRVFQDpmmgtaPSM----TIEEN----LALaYRRGKRRglrrGLTKKRRelfreLLATLGL-GLENRLDTKv 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 872553587 144 --LSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHD 203
Cdd:COG1101 147 glLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHN 208
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-219 |
6.08e-22 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 92.87 E-value: 6.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 1 MNIIEIKRLEKSFDIGDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPS---VGSIRVDGTEISTLKEK 77
Cdd:PRK09473 10 DALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 78 ELALFRRHKIGFIFQQ--FNLIPVFSAEENVGLPLLL-DNVSQKKATMTATRLLELVGLKGKEKHL---PAQLSGGQQQR 151
Cdd:PRK09473 90 ELNKLRAEQISMIFQDpmTSLNPYMRVGEQLMEVLMLhKGMSKAEAFEESVRMLDAVKMPEARKRMkmyPHEFSGGMRQR 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 872553587 152 VAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHD-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 |
6.21e-22 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 94.48 E-value: 6.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 3 IIEIKRLEKSF-DIGDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVD-GTEISTLKEKELA 80
Cdd:TIGR03269 279 IIKVRNVSKRYiSVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 81 LFRRHK--IGFIFQQFNLIPVFSAEENVGLPLLLDnVSQKKATMTATRLLELVGLKGKE-----KHLPAQLSGGQQQRVA 153
Cdd:TIGR03269 359 GRGRAKryIGILHQEYDLYPHRTVLDNLTEAIGLE-LPDELARMKAVITLKMVGFDEEKaeeilDKYPDELSEGERHRVA 437
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 154 IARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHD-PFVAAHADKVVFLLDGEVI 222
Cdd:TIGR03269 438 LAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDmDFVLDVCDRAALMRDGKIV 507
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-204 |
7.13e-22 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 94.35 E-value: 7.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLEKSFDiGDSKVkiLKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfr 83
Cdd:TIGR02868 335 LELRDLSAGYP-GAPPV--LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEV---- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 84 RHKIGFIFQQFNLipvFSAEenvglplLLDNVSQKKATMT---ATRLLELVGLKGKEKHLP-----------AQLSGGQQ 149
Cdd:TIGR02868 408 RRRVSVCAQDAHL---FDTT-------VRENLRLARPDATdeeLWAALERVGLADWLRALPdgldtvlgeggARLSGGER 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 872553587 150 QRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDelGQTAVVVTHDP 204
Cdd:TIGR02868 478 QRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALS--GRTVVLITHHL 530
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-224 |
7.42e-22 |
|
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: 90.51 E-value: 7.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLEKSFDigdsKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEIStlkeKELALFR 83
Cdd:cd03265 1 IEVENLVKKYG----DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV----REPREVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 84 RhKIGFIFQQFNLIPVFSAEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPA 163
Cdd:cd03265 73 R-RIGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 872553587 164 IILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVA-AHADKVVFLLDGEVIHE 224
Cdd:cd03265 152 VLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAE 213
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-222 |
1.45e-21 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 93.38 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 2 NIIEIKRLEKSFDIGDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDG----------TEI 71
Cdd:PRK10261 11 DVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 72 STLKEKELALFRRHKIGFIFQQ--FNLIPVFSAEENVGLPLLL-DNVSQKKATMTATRLLELVGLKGKEKHL---PAQLS 145
Cdd:PRK10261 91 SEQSAAQMRHVRGADMAMIFQEpmTSLNPVFTVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIPEAQTILsryPHQLS 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 872553587 146 GGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVAAH-ADKVVFLLDGEVI 222
Cdd:PRK10261 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEiADRVLVMYQGEAV 248
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
2-224 |
3.99e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 89.43 E-value: 3.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 2 NIIEIKRLekSFDIGDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELal 81
Cdd:PRK13648 6 SIIVFKNV--SFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKL-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 82 fRRHkIGFIFQ----QFnlipVFS-AEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIAR 156
Cdd:PRK13648 82 -RKH-IGIVFQnpdnQF----VGSiVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAG 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 872553587 157 AFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVAAHADKVVFLLDGEVIHE 224
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKE 223
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
17-222 |
5.62e-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: 5.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 17 DSKVKILKGINLQIQKGDFVCIMGASGSGK----TTLLQLLGGLDIPSvGSIRVDGTEISTlkekelALFRRHkIGFIFQ 92
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKttllDAISGRVEGGGTTS-GQILFNGQPRKP------DQFQKC-VAYVRQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 93 QFNLIPVFSAEENV--GLPLLLDNVSQK--KATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILAD 168
Cdd:cd03234 89 DDILLPGLTVRETLtyTAILRLPRKSSDaiRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 872553587 169 EPTGALDSENSKNIIAALRNACDElGQTAVVVTHDP----FvaAHADKVVFLLDGEVI 222
Cdd:cd03234 169 EPTSGLDSFTALNLVSTLSQLARR-NRIVILTIHQPrsdlF--RLFDRILLLSSGEIV 223
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-226 |
5.63e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 91.69 E-value: 5.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 1 MNIIEIKRLEKSFDIGDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLdIPS------VGSIRVDGTEISTL 74
Cdd:PRK15134 3 QPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRL-LPSppvvypSGDIRFHGESLLHA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 75 KEKELALFRRHKIGFIFQQ--FNLIPVFSAEENVGLPLLLDNVSQKKATMT-ATRLLELVGLKGKEKHL---PAQLSGGQ 148
Cdd:PRK15134 82 SEQTLRGVRGNKIAMIFQEpmVSLNPLHTLEKQLYEVLSLHRGMRREAARGeILNCLDRVGIRQAAKRLtdyPHQLSGGE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 872553587 149 QQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHD-PFVAAHADKVVFLLDGEVIHEHA 226
Cdd:PRK15134 162 RQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNlSIVRKLADRVAVMQNGRCVEQNR 240
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-221 |
9.10e-21 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 90.09 E-value: 9.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 1 MNIIEIKRLEKSFDigdsKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLG-GLDIPSvGSIRVDGTEISTLKEKEl 79
Cdd:PRK11000 1 MASVTLRNVTKAYG----DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAgLEDITS-GDLFIGEKRMNDVPPAE- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 80 alfrrHKIGFIFQQFNLIPVFSAEENVGLPLLLDNVSQ---KKATMTATRLLELVGLKGKEkhlPAQLSGGQQQRVAIAR 156
Cdd:PRK11000 75 -----RGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKeeiNQRVNQVAEVLQLAHLLDRK---PKALSGGQRQRVAIGR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 872553587 157 AFANEPAIILADEPTGALDsenskniiAALR--------NACDELGQTAVVVTHDPFVA-AHADKVVFLLDGEV 221
Cdd:PRK11000 147 TLVAEPSVFLLDEPLSNLD--------AALRvqmrieisRLHKRLGRTMIYVTHDQVEAmTLADKIVVLDAGRV 212
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
12-222 |
9.50e-21 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 91.18 E-value: 9.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 12 SFDIGDSKvKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfrRHKIGFIF 91
Cdd:PRK13657 341 SFSYDNSR-QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASL----RRNIAVVF 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 92 QQ---FNLipvfSAEEN--VGLPLLLD-NVSQKKATMTATRLLE--------LVGLKGKekhlpaQLSGGQQQRVAIARA 157
Cdd:PRK13657 416 QDaglFNR----SIEDNirVGRPDATDeEMRAAAERAQAHDFIErkpdgydtVVGERGR------QLSGGERQRLAIARA 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 872553587 158 FANEPAIILADEPTGALDSENSKNIIAALrnacDEL--GQTAVVVTHDPFVAAHADKVVFLLDGEVI 222
Cdd:PRK13657 486 LLKDPPILILDEATSALDVETEAKVKAAL----DELmkGRTTFIIAHRLSTVRNADRILVFDNGRVV 548
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-224 |
1.15e-20 |
|
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: 86.89 E-value: 1.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLEKSFdigdSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKelalfr 83
Cdd:cd03268 1 LKTNDLTKTY----GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 84 RHKIGFIFQQFNLIPVFSAEENVGLPLLLDNVSQKKatmtATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPA 163
Cdd:cd03268 71 LRRIGALIEAPGFYPNLTARENLRLLARLLGIRKKR----IDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 872553587 164 IILADEPTGALDSENskniIAALRNACDELGQTAVVVthdpFVAAH--------ADKVVFLLDGEVIHE 224
Cdd:cd03268 147 LLILDEPTNGLDPDG----IKELRELILSLRDQGITV----LISSHllseiqkvADRIGIINKGKLIEE 207
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
23-224 |
1.94e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 87.91 E-value: 1.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 23 LKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEI-STLKEKELALFRRhKIGFIFQqFNLIPVFs 101
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITItHKTKDKYIRPVRK-RIGMVFQ-FPESQLF- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 102 aEENVGLPLLLD----NVSQKKATMTATRLLELVGLKGKEKHL-PAQLSGGQQQRVAIARAFANEPAIILADEPTGALDS 176
Cdd:PRK13646 100 -EDTVEREIIFGpknfKMNLDEVKNYAHRLLMDLGFSRDVMSQsPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 872553587 177 ENSKNIIAALRNACDELGQTAVVVTHD-PFVAAHADKVVFLLDGEVIHE 224
Cdd:PRK13646 179 QSKRQVMRLLKSLQTDENKTIILVSHDmNEVARYADEVIVMKEGSIVSQ 227
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
2-224 |
3.00e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 87.60 E-value: 3.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 2 NIIEIKRLEKSFDIGdskVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELAL 81
Cdd:PRK13636 4 YILKVEELNYNYSDG---THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 82 frRHKIGFIFQQFNLiPVFSAE--ENVGLPLLLDNVSQKKATMTATRLLELVG---LKGKEKHLpaqLSGGQQQRVAIAR 156
Cdd:PRK13636 81 --RESVGMVFQDPDN-QLFSASvyQDVSFGAVNLKLPEDEVRKRVDNALKRTGiehLKDKPTHC---LSFGQKKRVAIAG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 872553587 157 AFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHD-PFVAAHADKVVFLLDGEVIHE 224
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDiDIVPLYCDNVFVMKEGRVILQ 223
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-222 |
3.76e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 89.38 E-value: 3.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 3 IIEIKRLEKSFDIGDSKVK-------ILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLdIPSVGSIRVDGTEISTLK 75
Cdd:PRK15134 275 LLDVEQLQVAFPIRKGILKrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRL-INSQGEIWFDGQPLHNLN 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 76 EKELALFRrHKIGFIFQQFN--LIPVFSAEENV--GLPLLLDNVSQKKATMTATRLLELVGLKGKEKH-LPAQLSGGQQQ 150
Cdd:PRK15134 354 RRQLLPVR-HRIQVVFQDPNssLNPRLNVLQIIeeGLRVHQPTLSAAQREQQVIAVMEEVGLDPETRHrYPAEFSGGQRQ 432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 872553587 151 RVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHD-PFVAAHADKVVFLLDGEVI 222
Cdd:PRK15134 433 RIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDlHVVRALCHQVIVLRQGEVV 505
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
16-213 |
1.13e-19 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 86.56 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 16 GDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALFRRhKIGFIFQqfN 95
Cdd:PRK11308 24 PERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQ-KIQIVFQ--N 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 96 ----LIPVFSAEENVGLPLLLD-NVSQKKATMTATRLLELVGLKGKE-KHLPAQLSGGQQQRVAIARAFANEPAIILADE 169
Cdd:PRK11308 101 pygsLNPRKKVGQILEEPLLINtSLSAAERREKALAMMAKVGLRPEHyDRYPHMFSGGQRQRIAIARALMLDPDVVVADE 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 872553587 170 PTGALD-SENSK--NIIAALRnacDELGQTAVVVTHDPFVAAH-ADKV 213
Cdd:PRK11308 181 PVSALDvSVQAQvlNLMMDLQ---QELGLSYVFISHDLSVVEHiADEV 225
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-224 |
1.55e-19 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 85.95 E-value: 1.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 1 MNIIEIKRLEKSFDIGDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLG-GLDIP---SVGSIRVDGTEISTLKE 76
Cdd:PRK11022 1 MALLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMgLIDYPgrvMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 77 KElalfRRHKIG----FIFQQ--FNLIPVFSaeenVGLPLL-----LDNVSQKKATMTATRLLELVGLKGKEKHL---PA 142
Cdd:PRK11022 81 KE----RRNLVGaevaMIFQDpmTSLNPCYT----VGFQIMeaikvHQGGNKKTRRQRAIDLLNQVGIPDPASRLdvyPH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 143 QLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHD-PFVAAHADKVVFLLDGEV 221
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDlALVAEAAHKIIVMYAGQV 232
|
...
gi 872553587 222 IHE 224
Cdd:PRK11022 233 VET 235
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-221 |
1.94e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 86.82 E-value: 1.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 1 MNIIEIKRLEKSFdiGDskVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELA 80
Cdd:PRK09536 1 MPMIDVSDLSVEF--GD--TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 81 lfRRhkIGFIFQQFNLIPVFSAEENVGL---PLLldnvsQKKATMTAT------RLLELVGLKGKEKHLPAQLSGGQQQR 151
Cdd:PRK09536 77 --RR--VASVPQDTSLSFEFDVRQVVEMgrtPHR-----SRFDTWTETdraaveRAMERTGVAQFADRPVTSLSGGERQR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 872553587 152 VAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDElGQTAVVVTHDPFVAA-HADKVVFLLDGEV 221
Cdd:PRK09536 148 VLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAArYCDELVLLADGRV 217
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
21-223 |
2.87e-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: 83.98 E-value: 2.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 21 KILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVG-SIRV-----DGTEISTLkekelalfrRHKIGFI---F 91
Cdd:COG1119 17 TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLfgerrGGEDVWEL---------RKRIGLVspaL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 92 QQFnlipvFSAEENV------------GLPlllDNVSQkKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFA 159
Cdd:COG1119 88 QLR-----FPRDETVldvvlsgffdsiGLY---REPTD-EQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 872553587 160 NEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHD-----PFVaahaDKVVFLLDGEVIH 223
Cdd:COG1119 159 KDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHveeipPGI----THVLLLKDGRVVA 223
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
21-227 |
5.22e-19 |
|
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: 86.03 E-value: 5.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 21 KILKGINLQIQKGDFVCIMGASGSGKTTllqllggldI---------PSVGSIRVDGTEISTLKEKELalfrRHKIGFIF 91
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKST---------LarllfrfydVTSGRILIDGQDIRDVTQASL----RAAIGIVP 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 92 Q---------QFNLI---PVFSAEENV-------------GLPllldnvsQKKATMTATRllelvGLKgkekhlpaqLSG 146
Cdd:COG5265 439 QdtvlfndtiAYNIAygrPDASEEEVEaaaraaqihdfieSLP-------DGYDTRVGER-----GLK---------LSG 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 147 GQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNAcdELGQTAVVVTHDPFVAAHADKVVFLLDGEVIHE-- 224
Cdd:COG5265 498 GEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREV--ARGRTTLVIAHRLSTIVDADEILVLEAGRIVERgt 575
|
...
gi 872553587 225 HAE 227
Cdd:COG5265 576 HAE 578
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
25-222 |
7.21e-19 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 83.05 E-value: 7.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 25 GINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDG-----TEISTLKEKELALFRRHKIGFIFQ--QFNLI 97
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYALSEAERRRLLRTEWGFVHQhpRDGLR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 98 PVFSAEENVGLPLLldNVSQK---KATMTATRLLELVGLKGKE-KHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGA 173
Cdd:PRK11701 104 MQVSAGGNIGERLM--AVGARhygDIRATAGDWLERVEIDAARiDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGG 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 872553587 174 LDSENSKNIIAALRNACDELGQTAVVVTHDPFVAA-HADKVVFLLDGEVI 222
Cdd:PRK11701 182 LDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARlLAHRLLVMKQGRVV 231
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
20-221 |
8.65e-19 |
|
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: 82.13 E-value: 8.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 20 VKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfrRHKIGFIFQQfnliPV 99
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYL----HSKVSLVGQE----PV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 100 FSA---EENV--GLPLL-LDNV---SQKKATMTATRLLEL-----VGLKGkekhlpAQLSGGQQQRVAIARAFANEPAII 165
Cdd:cd03248 99 LFArslQDNIayGLQSCsFECVkeaAQKAHAHSFISELASgydteVGEKG------SQLSGGQKQRVAIARALIRNPQVL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 872553587 166 LADEPTGALDSENSKNIIAALRnaCDELGQTAVVVTHDPFVAAHADKVVFLLDGEV 221
Cdd:cd03248 173 ILDEATSALDAESEQQVQQALY--DWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
4-222 |
1.79e-18 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 81.61 E-value: 1.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLEKSFDI--------GDSK---------VKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRV 66
Cdd:cd03267 1 IEVSNLSKSYRVyskepgliGSLKslfkrkyreVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 67 DGTEISTLKEKELalfrrHKIGFIFQQFN-LIPVFSAEEnvGLPLLLD--NVSQKKATMTATRLLELVGLkGKEKHLPA- 142
Cdd:cd03267 81 AGLVPWKRRKKFL-----RRIGVVFGQKTqLWWDLPVID--SFYLLAAiyDLPPARFKKRLDELSELLDL-EELLDTPVr 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 143 QLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHD-PFVAAHADKVVFLLDGEV 221
Cdd:cd03267 153 QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYmKDIEALARRVLVIDKGRL 232
|
.
gi 872553587 222 I 222
Cdd:cd03267 233 L 233
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
5-224 |
1.97e-18 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 81.16 E-value: 1.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 5 EIKRLEKSFDIGDSKVK--ILKGINLQIQKGDFVCIMGASGSGKttllqllggldipsvgsirvdgteiSTLKEkelALF 82
Cdd:COG2401 26 RVAIVLEAFGVELRVVEryVLRDLNLEIEPGEIVLIVGASGSGK-------------------------STLLR---LLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 83 RRHKIGFIFQQFNLIPVFSAEENVglplLLDNVSQKKATMTATRLLELVGLKGKEKHL--PAQLSGGQQQRVAIARAFAN 160
Cdd:COG2401 78 GALKGTPVAGCVDVPDNQFGREAS----LIDAIGRKGDFKDAVELLNAVGLSDAVLWLrrFKELSTGQKFRFRLALLLAE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 872553587 161 EPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVAA--HADKVVFLLDGEVIHE 224
Cdd:COG2401 154 RPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDVIDdlQPDLLIFVGYGGVPEE 219
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
18-221 |
2.66e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 84.00 E-value: 2.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 18 SKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfrRHKIGFIFQQfnli 97
Cdd:TIGR00958 492 PDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYL----HRQVALVGQE---- 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 98 PVF---SAEENVGLPL------LLDNVSQKK------ATMTATRLLElVGLKGkekhlpAQLSGGQQQRVAIARAFANEP 162
Cdd:TIGR00958 564 PVLfsgSVRENIAYGLtdtpdeEIMAAAKAAnahdfiMEFPNGYDTE-VGEKG------SQLSGGQKQRIAIARALVRKP 636
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 872553587 163 AIILADEPTGALDSEnsknIIAALRNACDELGQTAVVVTHDPFVAAHADKVVFLLDGEV 221
Cdd:TIGR00958 637 RVLILDEATSALDAE----CEQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSV 691
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-224 |
3.32e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 81.77 E-value: 3.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 1 MNIIEIKRLEKSFDigdSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELa 80
Cdd:PRK13652 1 MHLIETRDLCYSYS---GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREV- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 81 lfrRHKIGFIFQQFNlIPVFS--AEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAF 158
Cdd:PRK13652 77 ---RKFVGLVFQNPD-DQIFSptVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 872553587 159 ANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHD-PFVAAHADKVVFLLDGEVIHE 224
Cdd:PRK13652 153 AMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQlDLVPEMADYIYVMDKGRIVAY 219
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
21-222 |
4.15e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 83.36 E-value: 4.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 21 KILKG-INLQIQKGDFVCIMGASGSGKTTLLQLLGGLdIPSVGSIRVDGTEistLKEKELALFRRHkIGFIFQqfnlipv 99
Cdd:PRK11174 363 KTLAGpLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIE---LRELDPESWRKH-LSWVGQ------- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 100 fsaeeNVGLPL--LLDNVSQKKATMTATRL---LELVGLKGKEKHLP-----------AQLSGGQQQRVAIARAFANEPA 163
Cdd:PRK11174 431 -----NPQLPHgtLRDNVLLGNPDASDEQLqqaLENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQ 505
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 872553587 164 IILADEPTGALDSENSKNIIAALRNAcdELGQTAVVVTH--DPFvaAHADKVVFLLDGEVI 222
Cdd:PRK11174 506 LLLLDEPTASLDAHSEQLVMQALNAA--SRRQTTLMVTHqlEDL--AQWDQIWVMQDGQIV 562
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
19-224 |
8.85e-18 |
|
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: 79.64 E-value: 8.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 19 KVKILKGINLQIQKGDFVCIMGASGSGKttllqllggldiPSVGSIRVDGTEISTLKEKELAlfrRHKIGFIFQQFNLIP 98
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKttllkaisgllpPRSGSIRFDGEDITGLPPHRIA---RLGIGYVPEGRRIFP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 99 VFSAEEN--VGLPLLLDnvsQKKATMTATRLLEL--VgLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGAL 174
Cdd:COG0410 92 SLTVEENllLGAYARRD---RAEVRADLERVYELfpR-LKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 872553587 175 dsenS----KNIIAALRNACDElGQTAVVVTHD-PFVAAHADKVVFLLDGEVIHE 224
Cdd:COG0410 168 ----AplivEEIFEIIRRLNRE-GVTILLVEQNaRFALEIADRAYVLERGRIVLE 217
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
22-219 |
1.50e-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: 1.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 22 ILKGINLQIQKGDFVCIMGASGSGKttllqllggldipsvgsirvdgteiSTLkekelalFR-----------------R 84
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGK-------------------------STL-------LRaiaglwpygsgriarpaG 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 85 HKIGFIFQQfNLIPVFSAEENVGLPLLLDNVSQK--KATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEP 162
Cdd:COG4178 426 ARVLFLPQR-PYLPLGTLREALLYPATAEAFSDAelREALEAVGLGHLAERLDEEADWDQVLSLGEQQRLAFARLLLHKP 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 872553587 163 AIILADEPTGALDSENSKNIIAALRnacDELGQTAVV-VTHDPFVAAHADKVVFLLDG 219
Cdd:COG4178 505 DWLFLDEATSALDEENEAALYQLLR---EELPGTTVIsVGHRSTLAAFHDRVLELTGD 559
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-222 |
1.62e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 80.28 E-value: 1.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 3 IIEIKRLEKSFDIGDS-KVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRV----------DGTEI 71
Cdd:PRK13631 21 ILRVKNLYCVFDEKQEnELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 72 STLKEKELALFR--RHKIGFIFQqFNLIPVF--SAEENVGL-PLLLdNVSQKKATMTATRLLELVGLKgkEKHL---PAQ 143
Cdd:PRK13631 101 TNPYSKKIKNFKelRRRVSMVFQ-FPEYQLFkdTIEKDIMFgPVAL-GVKKSEAKKLAKFYLNKMGLD--DSYLersPFG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 144 LSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDElGQTAVVVTHD-PFVAAHADKVVFLLDGEVI 222
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTmEHVLEVADEVIVMDKGKIL 255
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
13-216 |
2.00e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 78.60 E-value: 2.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 13 FDIGDSKvkILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfrRHKIGFIFQ 92
Cdd:PRK10247 15 YLAGDAK--ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIY----RQQVSYCAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 93 QfnliPVFSAE---ENVGLPLLLDNVSQKKATMTATrlLELVGLKGK--EKHLpAQLSGGQQQRVAIARAFANEPAIILA 167
Cdd:PRK10247 89 T----PTLFGDtvyDNLIFPWQIRNQQPDPAIFLDD--LERFALPDTilTKNI-AELSGGEKQRISLIRNLQFMPKVLLL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 872553587 168 DEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVAAHADKVVFL 216
Cdd:PRK10247 162 DEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITL 210
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
21-222 |
3.99e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 78.90 E-value: 3.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 21 KILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEI-STLKE-KELALFRRhKIGFIFQqFNLIP 98
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpANLKKiKEVKRLRK-EIGLVFQ-FPEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 99 VF--SAEENVGLPLLLDNVSQKKATMTATRLLELVGL-KGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGALD 175
Cdd:PRK13645 103 LFqeTIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 872553587 176 SENSKNIIAALRNACDELGQTAVVVTHD-PFVAAHADKVVFLLDGEVI 222
Cdd:PRK13645 183 PKGEEDFINLFERLNKEYKKRIIMVTHNmDQVLRIADEVIVMHEGKVI 230
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-202 |
4.05e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 79.08 E-value: 4.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 3 IIEIKRLEKSFdiGDSKVkiLKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEIStlkekELALF 82
Cdd:PRK13537 7 PIDFRNVEKRY--GDKLV--VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVP-----SRARH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 83 RRHKIGFIFQQFNLIPVFSAEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEP 162
Cdd:PRK13537 78 ARQRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 872553587 163 AIILADEPTGALDSENSKNIIAALRNACDElGQTAVVVTH 202
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTH 196
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
14-224 |
6.71e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 77.75 E-value: 6.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 14 DIGDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELAlfrRHkIGFIFQQ 93
Cdd:PRK11231 9 TVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA---RR-LALLPQH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 94 fNLIPV-FSAEENVGL---PLL-----LDNVSQKKAT--MTATRLLELVglkgkeKHLPAQLSGGQQQRVAIARAFANEP 162
Cdd:PRK11231 85 -HLTPEgITVRELVAYgrsPWLslwgrLSAEDNARVNqaMEQTRINHLA------DRRLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 872553587 163 AIILADEPTGALDSENSKNIIAALRNACDElGQTAVVVTHDPFVAA-HADKVVFLLDGEVIHE 224
Cdd:PRK11231 158 PVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASrYCDHLVVLANGHVMAQ 219
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-223 |
7.90e-17 |
|
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: 76.55 E-value: 7.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLEKSFdigdSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKekelalfr 83
Cdd:cd03269 1 LEVENVTKRF----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 84 RHKIGFIFQQFNLIPVFSAEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPA 163
Cdd:cd03269 69 RNRIGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 872553587 164 IILADEPTGALDSENS---KNIIAALRNAcdelGQTAVVVTHD-PFVAAHADKVVFLLDGEVIH 223
Cdd:cd03269 149 LLILDEPFSGLDPVNVellKDVIRELARA----GKTVILSTHQmELVEELCDRVLLLNKGRAVL 208
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
11-226 |
1.06e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 77.33 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 11 KSFDIGDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELAlfRRhkIGFI 90
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA--RR--IGLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 91 FQQFNLIPVFSAEENVG------LPLLldNVSQKKATMTATRLLELVGLKgkekHLPAQ----LSGGQQQRVAIARAFAN 160
Cdd:PRK10253 87 AQNATTPGDITVQELVArgryphQPLF--TRWRKEDEEAVTKAMQATGIT----HLADQsvdtLSGGQRQRAWIAMVLAQ 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 872553587 161 EPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVAA-HADKVVFLLDGEVIHEHA 226
Cdd:PRK10253 161 ETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACrYASHLIALREGKIVAQGA 227
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-203 |
1.16e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 79.13 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 19 KVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALFRRhKIGFIFQQ--FNL 96
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRR-DIQFIFQDpyASL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 97 IPVFSAEENVGLPLLLDNVSQ-KKATMTATRLLELVGLKGKEK-HLPAQLSGGQQQRVAIARAFANEPAIILADEPTGAL 174
Cdd:PRK10261 415 DPRQTVGDSIMEPLRVHGLLPgKAAAARVAWLLERVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
|
170 180
....*....|....*....|....*....
gi 872553587 175 DSENSKNIIAALRNACDELGQTAVVVTHD 203
Cdd:PRK10261 495 DVSIRGQIINLLLDLQRDFGIAYLFISHD 523
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-220 |
1.33e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 77.00 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLEKSFDIGdskvKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDiPSVGSIRVDG-TEI--STLKEKELA 80
Cdd:PRK14258 8 IKVNNLSFYYDTQ----KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMN-ELESEVRVEGrVEFfnQNIYERRVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 81 LFR-RHKIGFIFQQFNLIPVfSAEENV--GLPLL-------LDNVSQkkATMTATRLLELVglKGKEKHLPAQLSGGQQQ 150
Cdd:PRK14258 83 LNRlRRQVSMVHPKPNLFPM-SVYDNVayGVKIVgwrpkleIDDIVE--SALKDADLWDEI--KHKIHKSALDLSGGQQQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 872553587 151 RVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHD-PFVAAHADKVVFLLDGE 220
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNlHQVSRLSDFTAFFKGNE 228
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-188 |
1.49e-16 |
|
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: 76.43 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLEKSFdigdSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELAlfr 83
Cdd:cd03218 1 LRAENLSKRY----GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 84 RHKIGFIFQQFNLIPVFSAEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPA 163
Cdd:cd03218 74 RLGIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPK 153
|
170 180
....*....|....*....|....*...
gi 872553587 164 IILADEPTGALDS---ENSKNIIAALRN 188
Cdd:cd03218 154 FLLLDEPFAGVDPiavQDIQKIIKILKD 181
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
3-213 |
1.76e-16 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 77.44 E-value: 1.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 3 IIEIKRLEKSFDIGDSK---------VKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEIST 73
Cdd:PRK15079 8 LLEVADLKVHFDIKDGKqwfwqppktLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 74 LKEKELALFRRhKIGFIFQQ--FNLIPVFSAEENVGLPLLL-------DNVSQK-KATMTATRLLE-LVglkgkeKHLPA 142
Cdd:PRK15079 88 MKDDEWRAVRS-DIQMIFQDplASLNPRMTIGEIIAEPLRTyhpklsrQEVKDRvKAMMLKVGLLPnLI------NRYPH 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 872553587 143 QLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVAAH-ADKV 213
Cdd:PRK15079 161 EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHiSDRV 232
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-222 |
2.19e-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: 75.61 E-value: 2.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLEKSFDIGDSKVkiLKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfr 83
Cdd:cd03244 3 IEFKNVSLRYRPNLPPV--LKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 84 RHKIGFIFQ---------QFNLIP--VFSAEEnvgLPLLLDNVSQKKATMTatrllELVGLKGKEKHLPAQLSGGQQQRV 152
Cdd:cd03244 77 RSRISIIPQdpvlfsgtiRSNLDPfgEYSDEE---LWQALERVGLKEFVES-----LPGGLDTVVEEGGENLSVGQRQLL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 153 AIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDelGQTAVVVTHDPFVAAHADKVVFLLDGEVI 222
Cdd:cd03244 149 CLARALLRKSKILVLDEATASVDPETDALIQKTIREAFK--DCTVLTIAHRLDTIIDSDRILVLDKGRVV 216
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
23-221 |
2.39e-16 |
|
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: 74.78 E-value: 2.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 23 LKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKElalFRRHKIGFI---FQQFNLIPV 99
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRD---AIRAGIAYVpedRKREGLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 100 FSAEENVGLPLLLdnvsqkkatmtatrllelvglkgkekhlpaqlSGGQQQRVAIARAFANEPAIILADEPTGALDSENS 179
Cdd:cd03215 93 LSVAENIALSSLL--------------------------------SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAK 140
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 872553587 180 KNIIAALRNACDElGQTAVVVTHD-PFVAAHADKVVFLLDGEV 221
Cdd:cd03215 141 AEIYRLIRELADA-GKAVLLISSElDELLGLCDRILVMYEGRI 182
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
8-224 |
2.78e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 76.18 E-value: 2.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 8 RLEK-SFDIGDSkVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGteISTLKEKELALFRRhK 86
Cdd:PRK13644 3 RLENvSYSYPDG-TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG--IDTGDFSKLQGIRK-L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 87 IGFIFQ----QFNLIPVfsaEENVGL---PLLLDNVSQKKatmTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFA 159
Cdd:PRK13644 79 VGIVFQnpetQFVGRTV---EEDLAFgpeNLCLPPIEIRK---RVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 872553587 160 NEPAIILADEPTGALDSENSKNIIAALRNaCDELGQTAVVVTHDPFVAAHADKVVFLLDGEVIHE 224
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKK-LHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLE 216
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
38-224 |
5.68e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 75.52 E-value: 5.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 38 IMGASGSGKTTLLQLLGGLDiPSVGSIRVDGTEI----STLKEKELALFRRhKIGFIFQQFNLIPVfSAEENVGLPLLLD 113
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMN-DKVSGYRYSGDVLlggrSIFNYRDVLEFRR-RVGMLFQRPNPFPM-SIMDNVLAGVRAH 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 114 N-VSQKKATMTATRLLELVGL----KGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRN 188
Cdd:PRK14271 129 KlVPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRS 208
|
170 180 190
....*....|....*....|....*....|....*..
gi 872553587 189 ACDELgqTAVVVTHDPFVAAH-ADKVVFLLDGEVIHE 224
Cdd:PRK14271 209 LADRL--TVIIVTHNLAQAARiSDRAALFFDGRLVEE 243
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
22-222 |
7.16e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 76.62 E-value: 7.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 22 ILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSV---GSIRVDGTEISTLKEKELAlfrrhkiGFIFQQFNLIP 98
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVkgsGSVLLNGMPIDAKEMRAIS-------AYVQQDDLFIP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 99 VFSAEENVGLPLLL---DNVSQK------KATMTATRLLE----LVGLKGKEKhlpaQLSGGQQQRVAIARAFANEPAII 165
Cdd:TIGR00955 113 TLTVREHLMFQAHLrmpRRVTKKekrervDEVLQALGLRKcantRIGVPGRVK----GLSGGERKRLAFASELLTDPPLL 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 872553587 166 LADEPTGALDSENSKNIIAALRNACDElGQTAVVVTHDPfvAAHA----DKVVFLLDGEVI 222
Cdd:TIGR00955 189 FCDEPTSGLDSFMAYSVVQVLKGLAQK-GKTIICTIHQP--SSELfelfDKIILMAEGRVA 246
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
25-202 |
9.82e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 73.30 E-value: 9.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 25 GINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELA--LFRRHKIGfifqqfnLIPVFSA 102
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQdlLYLGHQPG-------IKTELTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 103 EENVGLPLLLDNVSQKKATMTAtrlLELVGLKGKEkHLPA-QLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKN 181
Cdd:PRK13538 92 LENLRFYQRLHGPGDDEALWEA---LAQVGLAGFE-DVPVrQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVAR 167
|
170 180
....*....|....*....|.
gi 872553587 182 IIAALRNACDElGQTAVVVTH 202
Cdd:PRK13538 168 LEALLAQHAEQ-GGMVILTTH 187
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-188 |
1.13e-15 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 73.91 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 1 MNIIEIKRLEKSFdigdSKVKILKGINLQIQKGDFVCIMGASGSGK-----------TtllqllggldiPSVGSIRVDGT 69
Cdd:COG1137 1 MMTLEAENLVKSY----GKRTVVKDVSLEVNQGEIVGLLGPNGAGKtttfymivglvK-----------PDSGRIFLDGE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 70 EISTLkekelALFRRHK--IGF------IFQqfNLipvfSAEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLP 141
Cdd:COG1137 66 DITHL-----PMHKRARlgIGYlpqeasIFR--KL----TVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKA 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 872553587 142 AQLSGGQQQRVAIARAFANEPAIILADEPTGALDS---ENSKNIIAALRN 188
Cdd:COG1137 135 YSLSGGERRRVEIARALATNPKFILLDEPFAGVDPiavADIQKIIRHLKE 184
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-225 |
1.87e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 75.45 E-value: 1.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 3 IIEIKRLEKSFDigdsKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQllggldI------PSVGSIRVDGTE--ISTL 74
Cdd:COG3845 5 ALELRGITKRFG----GVVANDDVSLTVRPGEIHALLGENGAGKSTLMK------IlyglyqPDSGEILIDGKPvrIRSP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 75 KEkelAlfRRHKIGFIFQQFNLIPVFSAEENVGL---PLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQR 151
Cdd:COG3845 75 RD---A--IALGIGMVHQHFMLVPNLTVAENIVLglePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 872553587 152 VAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDElGQTAVVVTHD-PFVAAHADKVVFLLDGEVIHEH 225
Cdd:COG3845 150 VEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAE-GKSIIFITHKlREVMAIADRVTVLRRGKVVGTV 223
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
22-212 |
2.63e-15 |
|
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: 72.39 E-value: 2.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 22 ILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKelalfRRHKIGFIFQQFNLIPVFS 101
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDE-----PHENILYLGHLPGLKPELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 102 AEENvglpLLLDNVSQKKATMTATRLLELVGLKGKEkHLPA-QLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSK 180
Cdd:TIGR01189 90 ALEN----LHFWAAIHGGAQRTIEDALAAVGLTGFE-DLPAaQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVA 164
|
170 180 190
....*....|....*....|....*....|..
gi 872553587 181 NIIAALRNACdELGQTAVVVTHDPFVAAHADK 212
Cdd:TIGR01189 165 LLAGLLRAHL-ARGGIVLLTTHQDLGLVEARE 195
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-202 |
3.00e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 74.10 E-value: 3.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLEKSFdiGDSKVkiLKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTlkEKELAlfr 83
Cdd:PRK13536 42 IDLAGVSKSY--GDKAV--VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA--RARLA--- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 84 RHKIGFIFQQFNLIPVFSAEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPA 163
Cdd:PRK13536 113 RARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQ 192
|
170 180 190
....*....|....*....|....*....|....*....
gi 872553587 164 IILADEPTGALDSENSKNIIAALRnACDELGQTAVVVTH 202
Cdd:PRK13536 193 LLILDEPTTGLDPHARHLIWERLR-SLLARGKTILLTTH 230
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
23-222 |
4.51e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 72.57 E-value: 4.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 23 LKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLdIPSVGSIRVDGTEISTLKEKELALFRrhkiGFIFQQ----FnLIP 98
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAELARHR----AYLSQQqsppF-AMP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 99 VFSAeenvgLPLLL-DNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAF------AN-EPAIILADEP 170
Cdd:COG4138 86 VFQY-----LALHQpAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwptINpEGQLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 872553587 171 TGALDsenskniIA------ALRNACDELGQTAVVVTHD-PFVAAHADKVVFLLDGEVI 222
Cdd:COG4138 161 MNSLD-------VAqqaaldRLLRELCQQGITVVMSSHDlNHTLRHADRVWLLKQGKLV 212
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
22-227 |
4.94e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 72.42 E-value: 4.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 22 ILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSV----GSIRVDGTEIStlkekeLALFRRHKIGFIFQQ---- 93
Cdd:PRK10418 18 LVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGVrqtaGRVLLDGKPVA------PCALRGRKIATIMQNprsa 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 94 FNliPVFSAEENVGLPLLLDNVSQKKATMTATrlLELVGLKGKEKHL---PAQLSGGQQQRVAIARAFANEPAIILADEP 170
Cdd:PRK10418 92 FN--PLHTMHTHARETCLALGKPADDATLTAA--LEAVGLENAARVLklyPFEMSGGMLQRMMIALALLCEAPFIIADEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 872553587 171 TGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVAAH-ADKVVFLLDGEVIhEHAE 227
Cdd:PRK10418 168 TTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARlADDVAVMSHGRIV-EQGD 224
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
23-227 |
5.20e-15 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 74.28 E-value: 5.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 23 LKGINLQIQKGDFVCIMGASGSGKTTLLQLLGG-LDIPSvGSIRVDGTEistLKEKELALFRRHkIGFIFQQFNLI---- 97
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRfYDIDE-GEILLDGHD---LRDYTLASLRNQ-VALVSQNVHLFndti 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 98 ---------PVFSAEEnvglpllldnvSQKKATMT-ATRLLE--------LVGLKGkekhlpAQLSGGQQQRVAIARA-F 158
Cdd:PRK11176 434 anniayartEQYSREQ-----------IEEAARMAyAMDFINkmdngldtVIGENG------VLLSGGQRQRIAIARAlL 496
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 872553587 159 ANEPAIILaDEPTGALDSENSKNIIAALrnacDEL--GQTAVVVTHDPFVAAHADKVVFLLDGEVIH--EHAE 227
Cdd:PRK11176 497 RDSPILIL-DEATSALDTESERAIQAAL----DELqkNRTSLVIAHRLSTIEKADEILVVEDGEIVErgTHAE 564
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-202 |
5.75e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 74.05 E-value: 5.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLEKSFdigdSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELAlfr 83
Cdd:PRK09700 6 ISMAGIGKSF----GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAA--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 84 RHKIGFIFQQFNLIPVFSAEENVGLPLLL-------DNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIAR 156
Cdd:PRK09700 79 QLGIGIIYQELSVIDELTVLENLYIGRHLtkkvcgvNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAK 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 872553587 157 AFANEPAIILADEPTGALDSENSKNIIAALRNACDElGQTAVVVTH 202
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISH 203
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
22-220 |
1.03e-14 |
|
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: 70.58 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 22 ILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTeistlkekelalfrrhkIGFIFQQfnliP-VF 100
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-----------------IAYVSQE----PwIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 101 SA--EENV--GLPL-------------L---LDNVSQKKATMtatrllelVGLKGkekhlpAQLSGGQQQRVAIARAFAN 160
Cdd:cd03250 79 NGtiRENIlfGKPFdeeryekvikacaLepdLEILPDGDLTE--------IGEKG------INLSGGQKQRISLARAVYS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 872553587 161 EPAIILADEPTGALDSENSKNII-----AALRNacdelGQTAVVVTHDPFVAAHADKVVFLLDGE 220
Cdd:cd03250 145 DADIYLLDDPLSAVDAHVGRHIFencilGLLLN-----NKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-223 |
1.68e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 72.79 E-value: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 3 IIEIKRLEKSFDigdsKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVdGTEIstlkekelalf 82
Cdd:COG0488 315 VLELEGLSKSYG----DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 83 rrhKIGFiFQQFNLipVFSAEENVglpllLDNVSQ---KKATMTATRLLELVGLKGKEKHLP-AQLSGGQQQRVAIARAF 158
Cdd:COG0488 379 ---KIGY-FDQHQE--ELDPDKTV-----LDELRDgapGGTEQEVRGYLGRFLFSGDDAFKPvGVLSGGEKARLALAKLL 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 872553587 159 ANEPAIILADEPTGALDSENskniIAALRNACDELGQTAVVVTHDP-FVAAHADKVVFLLDGEVIH 223
Cdd:COG0488 448 LSPPNVLLLDEPTNHLDIET----LEALEEALDDFPGTVLLVSHDRyFLDRVATRILEFEDGGVRE 509
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-226 |
1.95e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 72.34 E-value: 1.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 3 IIEIKRLEKSFdigdSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEIS--TLKEKELA 80
Cdd:PRK10762 4 LLQLKGIDKAF----PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfnGPKSSQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 81 lfrrhKIGFIFQQFNLIPVFSAEENVGLPLLLDN----VSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIAR 156
Cdd:PRK10762 80 -----GIGIIHQELNLIPQLTIAENIFLGREFVNrfgrIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 872553587 157 AFANEPAIILADEPTGAL-DSENskniiAALRNACDEL---GQTAVVVTH---DPFVAahADKVVFLLDGEVIHEHA 226
Cdd:PRK10762 155 VLSFESKVIIMDEPTDALtDTET-----ESLFRVIRELksqGRGIVYISHrlkEIFEI--CDDVTVFRDGQFIAERE 224
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
23-215 |
3.08e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 70.58 E-value: 3.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 23 LKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLD--IPSV---GSIRVDGTEISTLKEKELALFRRhkIGFIFQQFNLI 97
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNdlIPGFrveGKVTFHGKNLYAPDVDPVEVRRR--IGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 98 PVfSAEENV-------GLPLLLDNVSQKKATMTAtrLLELVglKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEP 170
Cdd:PRK14243 104 PK-SIYDNIaygarinGYKGDMDELVERSLRQAA--LWDEV--KDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 872553587 171 TGALDSenskniIAALR--NACDELGQ--TAVVVTHDPFVAAH-ADKVVF 215
Cdd:PRK14243 179 CSALDP------ISTLRieELMHELKEqyTIIIVTHNMQQAARvSDMTAF 222
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-220 |
5.04e-14 |
|
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: 67.47 E-value: 5.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLEKSFDigdsKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEistlkekelalfr 83
Cdd:cd03221 1 IELENLSKTYG----GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 84 rhKIGFIfqqfnlipvfsaeenvglpllldnvsqkkatmtatrllelvglkgkekhlpAQLSGGQQQRVAIARAFANEPA 163
Cdd:cd03221 64 --KIGYF---------------------------------------------------EQLSGGEKMRLALAKLLLENPN 90
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 872553587 164 IILADEPTGALDSENskniIAALRNACDELGQTAVVVTHDP-FVAAHADKVVFLLDGE 220
Cdd:cd03221 91 LLLLDEPTNHLDLES----IEALEEALKEYPGTVILVSHDRyFLDQVATKIIELEDGK 144
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-222 |
9.85e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 70.52 E-value: 9.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLekSFDIGDSKVkILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfr 83
Cdd:PRK10790 341 IDIDNV--SFAYRDDNL-VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL---- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 84 RHKIGFIFQQfnliPVFSAE---ENVGLPlllDNVSQKK--ATMTATRLLELV-GL-KGKEKHLPAQ---LSGGQQQRVA 153
Cdd:PRK10790 414 RQGVAMVQQD----PVVLADtflANVTLG---RDISEEQvwQALETVQLAELArSLpDGLYTPLGEQgnnLSVGQKQLLA 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 872553587 154 IARAFANEPAIILADEPTGALDSENSKNIIAALRNACDElgQTAVVVTHDPFVAAHADKVVFLLDGEVI 222
Cdd:PRK10790 487 LARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAHRLSTIVEADTILVLHRGQAV 553
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
21-222 |
1.72e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 68.50 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 21 KILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALfrRHKIGFIFQQFNLiPVF 100
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLAL--RQQVATVFQDPEQ-QIF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 101 SAEENVGLPLLLDN--VSQKKATMTATRLLELVGLKGKeKHLPAQ-LSGGQQQRVAIARAFANEPAIILADEPTGALDSE 177
Cdd:PRK13638 92 YTDIDSDIAFSLRNlgVPEAEITRRVDEALTLVDAQHF-RHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 872553587 178 NSKNIIAALRNACDElGQTAVVVTHD-PFVAAHADKVVFLLDGEVI 222
Cdd:PRK13638 171 GRTQMIAIIRRIVAQ-GNHVIISSHDiDLIYEISDAVYVLRQGQIL 215
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
26-222 |
1.95e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 69.13 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 26 INLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTeisTLKEKELALF----RRHkIGFIFQQFNLIPVFS 101
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGR---VLFDAEKGIClppeKRR-IGYVFQDARLFPHYK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 102 AEENV--GLpllldnvsqkKATMTAtRLLELVGLKGKEKHL---PAQLSGGQQQRVAIARAFANEPAIILADEPTGALDS 176
Cdd:PRK11144 93 VRGNLryGM----------AKSMVA-QFDKIVALLGIEPLLdryPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 872553587 177 ENSKNIIAALRNACDELGQTAVVVTH--DPFVAAhADKVVFLLDGEVI 222
Cdd:PRK11144 162 PRKRELLPYLERLAREINIPILYVSHslDEILRL-ADRVVVLEQGKVK 208
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
21-189 |
2.51e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 67.61 E-value: 2.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 21 KILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELAlfrRHKIGFIFQQFNLIPVF 100
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARA---RRGIGYLPQEASIFRRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 101 SAEENVGLPL-LLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGALDS--- 176
Cdd:PRK10895 94 SVYDNLMAVLqIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPisv 173
|
170
....*....|...
gi 872553587 177 ENSKNIIAALRNA 189
Cdd:PRK10895 174 IDIKRIIEHLRDS 186
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
2-222 |
4.11e-13 |
|
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: 66.13 E-value: 4.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 2 NIIEIKRLeksfdiGDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSV---GSIRVDGTEIstlkeKE 78
Cdd:cd03233 8 NISFTTGK------GRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPY-----KE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 79 LALFRRHKIgfifqqfnlipVFSAEENVGLPllldnvsqkkaTMTATRLLELVG-LKGKEkhLPAQLSGGQQQRVAIARA 157
Cdd:cd03233 77 FAEKYPGEI-----------IYVSEEDVHFP-----------TLTVRETLDFALrCKGNE--FVRGISGGERKRVSIAEA 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 872553587 158 FANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVAAHA--DKVVFLLDGEVI 222
Cdd:cd03233 133 LVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASDEIYDlfDKVLVLYEGRQI 199
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-224 |
5.62e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 67.06 E-value: 5.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 3 IIEIKRLEKSFDigdsKVKILKGINLQIQKGDFVCIMGASGSGKttllqllgglDI--PSVGSIRVDGTEISTLKekela 80
Cdd:COG4152 1 MLELKGLTKRFG----DKTAVDDVSFTVPKGEIFGLLGPNGAGKttti--riilGIlaPDSGEVLWDGEPLDPED----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 81 lfrRHKIGFIfqqfnliPvfsaEE-------NVGLPLL----LDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQ 149
Cdd:COG4152 70 ---RRRIGYL-------P----EErglypkmKVGEQLVylarLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQ 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 872553587 150 QRVAIARAFANEPAIILADEPTGALDSENS---KNIIAALRNAcdelGQTAVVVTHD-PFVAAHADKVVFLLDGEVIHE 224
Cdd:COG4152 136 QKVQLIAALLHDPELLILDEPFSGLDPVNVellKDVIRELAAK----GTTVIFSSHQmELVEELCDRIVIINKGRKVLS 210
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
18-224 |
7.05e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 67.74 E-value: 7.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 18 SKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKElALfrRHKIGFI---FQQF 94
Cdd:COG1129 263 SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRD-AI--RAGIAYVpedRKGE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 95 NLIPVFSAEENVGLPLLLDN-----VSQKKATMTATRLLELVGLKGKEKHLPAQ-LSGGQQQRVAIARAFANEPAIILAD 168
Cdd:COG1129 340 GLVLDLSIRENITLASLDRLsrgglLDRRRERALAEEYIKRLRIKTPSPEQPVGnLSGGNQQKVVLAKWLATDPKVLILD 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 872553587 169 EPT-----GAldsensKN-IIAALRNACDElGQTAVVVTHD-PFVAAHADKVVFLLDGEVIHE 224
Cdd:COG1129 420 EPTrgidvGA------KAeIYRLIRELAAE-GKAVIVISSElPELLGLSDRILVMREGRIVGE 475
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
16-200 |
1.07e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 67.36 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 16 GDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKElalFRRHKIGFI---FQ 92
Cdd:COG3845 267 DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRE---RRRLGVAYIpedRL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 93 QFNLIPVFSAEENvglpLLLDN-----------VSQKKATMTATRLLELVGLKGKEKHLPA-QLSGGQQQRVAIARAFAN 160
Cdd:COG3845 344 GRGLVPDMSVAEN----LILGRyrrppfsrggfLDRKAIRAFAEELIEEFDVRTPGPDTPArSLSGGNQQKVILARELSR 419
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 872553587 161 EPAIILADEPTGALDSENSKNIIAALRNACDElGqTAVVV 200
Cdd:COG3845 420 DPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-G-AAVLL 457
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-203 |
2.76e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 65.70 E-value: 2.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 1 MNIIEIKRLEKSFDIGDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLggldipsVGSI-----------RVDGT 69
Cdd:COG4170 1 MPLLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAI-------CGITkdnwhvtadrfRWNGI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 70 EISTLKEKELALFRRHKIGFIFQ--QFNLIPvfsaEENVGlPLLLDNVSQKKAT-----------MTATRLLELVGLKGK 136
Cdd:COG4170 74 DLLKLSPRERRKIIGREIAMIFQepSSCLDP----SAKIG-DQLIEAIPSWTFKgkwwqrfkwrkKRAIELLHRVGIKDH 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 872553587 137 EKHL---PAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSeNSKNIIAALRNACDELGQTAVV-VTHD 203
Cdd:COG4170 149 KDIMnsyPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMES-TTQAQIFRLLARLNQLQGTSILlISHD 218
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
22-222 |
3.30e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 64.85 E-value: 3.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 22 ILKGINLQIQKGDFVCIMGASGSGKtTLLQLLGGLDIPS---------VGSIRVDGTEISTLKEKELALFRrhkiGFIFQ 92
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGK-STLLKALAGDLTGggaprgarvTGDVTLNGEPLAAIDAPRLARLR----AVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 93 QFNLIPVFSAEENVGL---PllldNVSQKKATMTATR-----LLELVGLKGKEKHLPAQLSGGQQQRVAIARAFAN---- 160
Cdd:PRK13547 91 AAQPAFAFSAREIVLLgryP----HARRAGALTHRDGeiawqALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpp 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 872553587 161 -----EPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVAA-HADKVVFLLDGEVI 222
Cdd:PRK13547 167 hdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAArHADRIAMLADGAIV 234
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
3-222 |
4.04e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 64.43 E-value: 4.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 3 IIEIKRLEKSFD-----IGDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEK 77
Cdd:PRK15112 4 LLEVRNLSKTFRyrtgwFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 78 elalFRRHKIGFIFQ--QFNLIPVFSAEENVGLPLLLD---NVSQKKATMTATrlLELVGLKGKE-KHLPAQLSGGQQQR 151
Cdd:PRK15112 84 ----YRSQRIRMIFQdpSTSLNPRQRISQILDFPLRLNtdlEPEQREKQIIET--LRQVGLLPDHaSYYPHMLAPGQKQR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 872553587 152 VAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVAAH-ADKVVFLLDGEVI 222
Cdd:PRK15112 158 LGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVV 229
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-222 |
4.37e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 65.34 E-value: 4.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 3 IIEIKRLEKSFDigdsKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQllggldIPS--------VGSIRVDGTEI--S 72
Cdd:PRK13549 5 LLEMKNITKTFG----GVKALDNVSLKVRAGEIVSLCGENGAGKSTLMK------VLSgvyphgtyEGEIIFEGEELqaS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 73 TLKEKElalfrRHKIGFIFQQFNLIPVFSAEENVGL---PLLLDNVSQKKATMTATRLLELVGLkGKEKHLP-AQLSGGQ 148
Cdd:PRK13549 75 NIRDTE-----RAGIAIIHQELALVKELSVLENIFLgneITPGGIMDYDAMYLRAQKLLAQLKL-DINPATPvGNLGLGQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 872553587 149 QQRVAIARAFANEPAIILADEPTGAL-DSENS--KNIIAALRNAcdelGQTAVVVTHD-PFVAAHADKVVFLLDGEVI 222
Cdd:PRK13549 149 QQLVEIAKALNKQARLLILDEPTASLtESETAvlLDIIRDLKAH----GIACIYISHKlNEVKAISDTICVIRDGRHI 222
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
22-224 |
5.00e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 64.04 E-value: 5.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 22 ILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELAlfrrHKIGFIFQQFNLIPVFS 101
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFA----RKVAYLPQQLPAAEGMT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 102 AEENVGL-------PLLLDNVSQKKATMTAtrlLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGAL 174
Cdd:PRK10575 102 VRELVAIgrypwhgALGRFGAADREKVEEA---ISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSAL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 872553587 175 DSENSKNIIAALRNACDELGQTAVVVTHDPFVAA-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 ... |
19-222 |
5.02e-12 |
|
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: 63.31 E-value: 5.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 19 KVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSV--GSIRVDGTEISTLKEKELAlfrRHKIGFIFQqfnl 96
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVteGEILFKGEDITDLPPEERA---RLGIFLAFQ---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 97 IPVfsAEENVGLPLLLDNVSqkkatmtatrllelVGlkgkekhlpaqLSGGQQQRVAIARAFANEPAIILADEPTGALDS 176
Cdd:cd03217 85 YPP--EIPGVKNADFLRYVN--------------EG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 872553587 177 ENSKNI---IAALRNAcdelGQTAVVVTHDPFVAAH--ADKVVFLLDGEVI 222
Cdd:cd03217 138 DALRLVaevINKLREE----GKSVLIITHYQRLLDYikPDRVHVLYDGRIV 184
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-202 |
5.20e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 65.32 E-value: 5.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 20 VKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKElALfrRHKIGFIFQQFNLIPV 99
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTA-AL--AAGVAIIYQELHLVPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 100 FSAEENV---GLPLLLDNVSQKKATMTATRLLELVGLK----GKEKHlpaqLSGGQQQRVAIARAFANEPAIILADEPTG 172
Cdd:PRK11288 94 MTVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDidpdTPLKY----LSIGQRQMVEIAKALARNARVIAFDEPTS 169
|
170 180 190
....*....|....*....|....*....|...
gi 872553587 173 AL---DSENSKNIIAALRnacDElGQTAVVVTH 202
Cdd:PRK11288 170 SLsarEIEQLFRVIRELR---AE-GRVILYVSH 198
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-229 |
7.67e-12 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 64.05 E-value: 7.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 1 MNIIEIKRLEKSFDIGDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLL--GGLDIPSVGS--IRVDGTEISTLKE 76
Cdd:PRK15093 1 MPLLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAIcgVTKDNWRVTAdrMRFDDIDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 77 KELALFRRHKIGFIFQ--QFNLIPvfsaEENVGLPLL------------LDNVSQKKATmtATRLLELVGLKGKE---KH 139
Cdd:PRK15093 81 RERRKLVGHNVSMIFQepQSCLDP----SERVGRQLMqnipgwtykgrwWQRFGWRKRR--AIELLHRVGIKDHKdamRS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 140 LPAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVAAH-ADKVVFLLD 218
Cdd:PRK15093 155 FPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQwADKINVLYC 234
|
250
....*....|.
gi 872553587 219 GEVIhEHAESK 229
Cdd:PRK15093 235 GQTV-ETAPSK 244
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
7-224 |
8.34e-12 |
|
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: 62.94 E-value: 8.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 7 KRLEKSFDIGDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLkekELALFrrhk 86
Cdd:cd03220 22 KLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLL---GLGGG---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 87 igfifqqFNliPVFSAEENVGLPLLLDNVSQKKATMTATRLLELVGLkGKEKHLP-AQLSGGQQQRVAIARAFANEPAII 165
Cdd:cd03220 95 -------FN--PELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSEL-GDFIDLPvKTYSSGMKARLAFAIATALEPDIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 166 LADEPTGALDSENSKNIIAALRNACDElGQTAVVVTHDP-FVAAHADKVVFLLDGEVIHE 224
Cdd:cd03220 165 LIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPsSIKRLCDRALVLEKGKIRFD 223
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-221 |
2.09e-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: 63.81 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 22 ILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfrRHKIGFIFQQfnliPV-F 100
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDL----RFKITIIPQD----PVlF 1372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 101 SAEenvgLPLLLDNVSQKKATMTATRlLELVGLKGKEKHLPAQ-----------LSGGQQQRVAIARAFANEPAIILADE 169
Cdd:TIGR00957 1373 SGS----LRMNLDPFSQYSDEEVWWA-LELAHLKTFVSALPDKldhecaeggenLSVGQRQLVCLARALLRKTKILVLDE 1447
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 872553587 170 PTGALDSENSKNIIAALRNACDELgqTAVVVTHDPFVAAHADKVVFLLDGEV 221
Cdd:TIGR00957 1448 ATAAVDLETDNLIQSTIRTQFEDC--TVLTIAHRLNTIMDYTRVIVLDKGEV 1497
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
144-220 |
2.18e-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: 2.18e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 872553587 144 LSGGQQQRVAIARAFANEPAIILADEPTGALDSENSkniiAALRNACDELGQTAVVVTHDPFVAAHADKVVfLLDGE 220
Cdd:cd03223 92 LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESE----DRLYQLLKELGITVISVGHRPSLWKFHDRVL-DLDGE 163
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
21-226 |
2.20e-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: 2.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 21 KILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfrRHKIGFIFQQFNLipvF 100
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL----RSSLTIIPQDPTL---F 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 101 SAeeNVGLPLLLDNVSQKKATMTATRLLElvglkGKEkhlpaQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSK 180
Cdd:cd03369 95 SG--TIRSNLDPFDEYSDEEIYGALRVSE-----GGL-----NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 872553587 181 NIIAALRNACDelGQTAVVVTHDPFVAAHADKVVFLLDGEVIhEHA 226
Cdd:cd03369 163 LIQKTIREEFT--NSTILTIAHRLRTIIDYDKILVMDAGEVK-EYD 205
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
3-222 |
2.74e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 62.88 E-value: 2.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 3 IIEIKRLEKSFdigdSKVKILKGINLQIQKGDFVCIMGASGSGKttllqllggldipSV---------------GSIRVD 67
Cdd:NF040905 1 ILEMRGITKTF----PGVKALDDVNLSVREGEIHALCGENGAGK-------------STlmkvlsgvyphgsyeGEILFD 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 68 GTEI--STLKEKElalfrRHKIGFIFQQFNLIPVFSAEENvglpLLLDNVSQKK-------ATMTATRLLELVGLKGKEK 138
Cdd:NF040905 64 GEVCrfKDIRDSE-----ALGIVIIHQELALIPYLSIAEN----IFLGNERAKRgvidwneTNRRARELLAKVGLDESPD 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 139 HLPAQLSGGQQQRVAIARAFANEPAIILADEPTGAL---DSENSKNIIAALRnacdELGQTAVVVTHD-PFVAAHADKVV 214
Cdd:NF040905 135 TLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALneeDSAALLDLLLELK----AQGITSIIISHKlNEIRRVADSIT 210
|
....*...
gi 872553587 215 FLLDGEVI 222
Cdd:NF040905 211 VLRDGRTI 218
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
22-204 |
3.10e-11 |
|
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: 60.97 E-value: 3.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 22 ILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTeisTLKEKELALFRrhKIGFIFQQFNLIPVFS 101
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGG---PLDFQRDSIAR--GLLYLGHAPGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 102 AEENvglpllLDNVSQKKATMTATRLLELVGLKGKEkHLP-AQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSK 180
Cdd:cd03231 90 VLEN------LRFWHADHSDEQVEEALARVGLNGFE-DRPvAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVA 162
|
170 180
....*....|....*....|....
gi 872553587 181 NIIAALRNACdELGQTAVVVTHDP 204
Cdd:cd03231 163 RFAEAMAGHC-ARGGMVVLTTHQD 185
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
131-214 |
3.93e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 63.12 E-value: 3.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 131 VGLKGKekhlpaQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVAAHA 210
Cdd:PTZ00265 1352 VGPYGK------SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRS 1425
|
....
gi 872553587 211 DKVV 214
Cdd:PTZ00265 1426 DKIV 1429
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
23-203 |
4.57e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 61.44 E-value: 4.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 23 LKGINLQIQKGDFVCIMGASGSGKTTLLQLLggldipsVGSIRVDGTEISTLKEKELALFRRHKIGFIFQqfnlipvfSA 102
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKAL-------MGFVRLASGKISILGQPTRQALQKNLVAYVPQ--------SE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 103 EENVGLPLLLDNV--------------SQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILAD 168
Cdd:PRK15056 88 EVDWSFPVLVEDVvmmgryghmgwlrrAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLD 167
|
170 180 190
....*....|....*....|....*....|....*
gi 872553587 169 EPTGALDSENSKNIIAALRNACDElGQTAVVVTHD 203
Cdd:PRK15056 168 EPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHN 201
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-203 |
6.44e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 62.00 E-value: 6.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 6 IKRLEKSFDigdsKVKILKGINLQIQKGDFVCIMGASGSGKttllqllggldipS------VGSIRVDGTEISTLKEKel 79
Cdd:COG0488 1 LENLSKSFG----GRPLLDDVSLSINPGDRIGLVGRNGAGK-------------StllkilAGELEPDSGEVSIPKGL-- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 80 alfrrhKIGFIFQQFNLIPVFSAEENV--GLPLLLDNVSQKKATMT------------------------------ATRL 127
Cdd:COG0488 62 ------RIGYLPQEPPLDDDLTVLDTVldGDAELRALEAELEELEAklaepdedlerlaelqeefealggweaearAEEI 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 872553587 128 LELVGLKGKEKHLP-AQLSGGQQQRVAIARAFANEPAIILADEPTGALDSEnsknIIAALRNACDELGQTAVVVTHD 203
Cdd:COG0488 136 LSGLGFPEEDLDRPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLE----SIEWLEEFLKNYPGTVLVVSHD 208
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
25-203 |
7.96e-11 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 60.77 E-value: 7.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 25 GINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELAlfrRHKIGFIFQQFNLIPVFSAEE 104
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIA---RMGVVRTFQHVRLFREMTVIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 105 NV-----------GLPLLLDNV----SQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADE 169
Cdd:PRK11300 100 NLlvaqhqqlktgLFSGLLKTPafrrAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDE 179
|
170 180 190
....*....|....*....|....*....|....*..
gi 872553587 170 PTGAL---DSENSKNIIAALRnacDELGQTAVVVTHD 203
Cdd:PRK11300 180 PAAGLnpkETKELDELIAELR---NEHNVTVLLIEHD 213
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
26-222 |
1.16e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 59.95 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 26 INLQIQKGDFVCIMGASGSGKTTLLQLLGGLdIPSVGSIRVDGTEISTLKEKELALFRrhkiGFIFQQFN---LIPVFSA 102
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELARHR----AYLSQQQTppfAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 103 eenvgLPLLLDNVSQKKATMTA-TRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAF-----ANEPA--IILADEPTGAL 174
Cdd:PRK03695 90 -----LTLHQPDKTRTEAVASAlNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPAgqLLLLDEPMNSL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 872553587 175 DSENsKNIIAALRNACDELGQTAVVVTHD-PFVAAHADKVVFLLDGEVI 222
Cdd:PRK03695 165 DVAQ-QAALDRLLSELCQQGIAVVMSSHDlNHTLRHADRVWLLKQGKLL 212
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
3-204 |
2.14e-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: 58.41 E-value: 2.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 3 IIEIKRLEKSFDIGDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSV--GSIRVDGteistlKEKELA 80
Cdd:cd03232 3 VLTWKNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGVitGEILING------RPLDKN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 81 LFRRhkIGFIFQQfnliPVFSAEENVGLPLLLDNVsqkkatmtatrllelvgLKGkekhlpaqLSGGQQQRVAIARAFAN 160
Cdd:cd03232 77 FQRS--TGYVEQQ----DVHSPNLTVREALRFSAL-----------------LRG--------LSVEQRKRLTIGVELAA 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 872553587 161 EPAIILADEPTGALDSENSKNIIAALRNACDElGQTAVVVTHDP 204
Cdd:cd03232 126 KPSILFLDEPTSGLDSQAAYNIVRFLKKLADS-GQAILCTIHQP 168
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-222 |
2.54e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 60.22 E-value: 2.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 3 IIEIKRLEKSFDigdsKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSV--GSIRVDGTEI--STLKEKE 78
Cdd:TIGR02633 1 LLEMKGIVKTFG----GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLkaSNIRDTE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 79 lalfrRHKIGFIFQQFNLIPVFSAEENV--GLPLLLDNVSQKKATMT--ATRLLELVGLKGKEKHLP-AQLSGGQQQRVA 153
Cdd:TIGR02633 77 -----RAGIVIIHQELTLVPELSVAENIflGNEITLPGGRMAYNAMYlrAKNLLRELQLDADNVTRPvGDYGGGQQQLVE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 154 IARAFANEPAIILADEPTGALDSENSKNIIAALRNaCDELGQTAVVVTHD-PFVAAHADKVVFLLDGEVI 222
Cdd:TIGR02633 152 IAKALNKQARLLILDEPSSSLTEKETEILLDIIRD-LKAHGVACVYISHKlNEVKAVCDTICVIRDGQHV 220
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
2-222 |
2.58e-10 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 58.94 E-value: 2.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 2 NIIEIKRLEKSFDIGDSK------------------VKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGS 63
Cdd:COG1134 3 SMIEVENVSKSYRLYHEPsrslkelllrrrrtrreeFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 64 IRVDGTeISTLkekeLALfrrhkiGFIFQqfnliPVFSAEENVGLPLLLDNVSQKKatmTATRL---LELVGLkGKEKHL 140
Cdd:COG1134 83 VEVNGR-VSAL----LEL------GAGFH-----PELTGRENIYLNGRLLGLSRKE---IDEKFdeiVEFAEL-GDFIDQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 141 PAQ-LSGGQQQRVAIARAFANEPAIILADEPTGALDS---ENSKNIIAALRNAcdelGQTAVVVTHDP-FVAAHADKVVF 215
Cdd:COG1134 143 PVKtYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAafqKKCLARIRELRES----GRTVIFVSHSMgAVRRLCDRAIW 218
|
....*..
gi 872553587 216 LLDGEVI 222
Cdd:COG1134 219 LEKGRLV 225
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
23-229 |
2.62e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 60.37 E-value: 2.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 23 LKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEIStlkEKELALFRRHkIGFIFQQFNLipvFSA 102
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT---AEQPEDYRKL-FSAVFTDFHL---FDQ 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 103 eenvglplLLDNVSQKKATMTATRLLELVGLKGKEKH-----LPAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSE 177
Cdd:PRK10522 412 --------LLGPEGKPANPALVEKWLERLKMAHKLELedgriSNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPH 483
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 872553587 178 NSKNIIAALRNACDELGQTAVVVTHDPFVAAHADKVVFLLDGEVIHEHAESK 229
Cdd:PRK10522 484 FRREFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSELTGEER 535
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
19-174 |
3.41e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 58.74 E-value: 3.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 19 KVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEIStlkEKELALFRRHKIGFIFQQFNLIP 98
Cdd:PRK11614 17 KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDIT---DWQTAKIMREAVAIVPEGRRVFS 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 872553587 99 VFSAEENVGLPLLLDNVSQKKATMtaTRLLELVGLKGKEKHLPA-QLSGGQQQRVAIARAFANEPAIILADEPTGAL 174
Cdd:PRK11614 94 RMTVEENLAMGGFFAERDQFQERI--KWVYELFPRLHERRIQRAgTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL 168
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
18-220 |
4.06e-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: 4.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 18 SKVKILKGINLQIQKGDF-----VCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALFR---RHKIGF 89
Cdd:cd03237 5 TMKKTLGEFTLEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKADYEgtvRDLLSS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 90 IFQQFNLIPVFSAEenVGLPLLLDnvsqkkatmtatRLLElvglkgkeKHLPaQLSGGQQQRVAIARAFANEPAIILADE 169
Cdd:cd03237 85 ITKDFYTHPYFKTE--IAKPLQIE------------QILD--------REVP-ELSGGELQRVAIAACLSKDADIYLLDE 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 872553587 170 PTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVAAH-ADKV-VFllDGE 220
Cdd:cd03237 142 PSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYlADRLiVF--EGE 192
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-223 |
4.46e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 58.95 E-value: 4.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 3 IIEIKRLEKSFDIGDSK-----------------VKILKGINLQIQKGDFVCIMGASGSGKTTLlqllggldI------- 58
Cdd:COG4586 1 IIEVENLSKTYRVYEKEpglkgalkglfrreyreVEAVDDISFTIEPGEIVGFIGPNGAGKSTT--------Ikmltgil 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 59 -PSVGSIRVDGtEISTLKEKELAlfrrHKIGFIFQQ-----FNLIPVFSaeenvgLPLLLD--NVSQKKATMTATRLLEL 130
Cdd:COG4586 73 vPTSGEVRVLG-YVPFKRRKEFA----RRIGVVFGQrsqlwWDLPAIDS------FRLLKAiyRIPDAEYKKRLDELVEL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 131 VGLKGKeKHLPA-QLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPF-VAA 208
Cdd:COG4586 142 LDLGEL-LDTPVrQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDdIEA 220
|
250
....*....|....*
gi 872553587 209 HADKVVFLLDGEVIH 223
Cdd:COG4586 221 LCDRVIVIDHGRIIY 235
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
18-219 |
8.25e-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: 57.34 E-value: 8.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 18 SKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALFRRHKIGFIFQQFNLI 97
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 98 PVfSAEENV--GLPLlldNVSQKKATMTATRLLELVGL--KGKEKHLPAQ---LSGGQQQRVAIARAFANEPAIILADEP 170
Cdd:cd03290 92 NA-TVEENItfGSPF---NKQRYKAVTDACSLQPDIDLlpFGDQTEIGERginLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 872553587 171 TGALDSENSKNII-AALRNACDELGQTAVVVTHDPFVAAHADKVVFLLDG 219
Cdd:cd03290 168 FSALDIHLSDHLMqEGILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-221 |
8.43e-10 |
|
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: 59.19 E-value: 8.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 23 LKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTeistlkekelalfrrhkIGFIFQQfNLIPVFSA 102
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-----------------VAYVPQQ-AWIQNDSL 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 103 EENV--GLPLlldNVSQKKATMTATRLL---EL--------VGLKGkekhlpAQLSGGQQQRVAIARAFANEPAIILADE 169
Cdd:TIGR00957 716 RENIlfGKAL---NEKYYQQVLEACALLpdlEIlpsgdrteIGEKG------VNLSGGQKQRVSLARAVYSNADIYLFDD 786
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 872553587 170 PTGALDSENSKNIIAALRNACDEL-GQTAVVVTHDPFVAAHADKVVFLLDGEV 221
Cdd:TIGR00957 787 PLSAVDAHVGKHIFEHVIGPEGVLkNKTRILVTHGISYLPQVDVIIVMSGGKI 839
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-216 |
8.46e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 57.43 E-value: 8.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 1 MNIIEIKRLEKSFdiGDSKVkiLKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIrvdgteistlkEKELA 80
Cdd:PRK09544 2 TSLVSLENVSVSF--GQRRV--LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRNGK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 81 LfrrhKIGFIFQQFNLIPVfsaeenvgLPLlldnvsqkkatmTATRLLELVGLKGKEKHLPA---------------QLS 145
Cdd:PRK09544 67 L----RIGYVPQKLYLDTT--------LPL------------TVNRFLRLRPGTKKEDILPAlkrvqaghlidapmqKLS 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 872553587 146 GGQQQRVAIARAFANEPAIILADEPTGALDSENS---KNIIAALRNacdELGQTAVVVTHD-PFVAAHADKVVFL 216
Cdd:PRK09544 123 GGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQvalYDLIDQLRR---ELDCAVLMVSHDlHLVMAKTDEVLCL 194
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
22-219 |
9.28e-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: 58.77 E-value: 9.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 22 ILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGteistlkekelalfrrhKIGFIfQQFNLIPVFS 101
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-----------------RISFS-PQTSWIMPGT 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 102 AEENVGLPLLLDNVsQKKATMTATRLLELVGLKGKEKHLP-----AQLSGGQQQRVAIARAFANEPAIILADEPTGALDS 176
Cdd:TIGR01271 503 IKDNIIFGLSYDEY-RYTSVIKACQLEEDIALFPEKDKTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 872553587 177 ENSKNIIAalRNACDEL-GQTAVVVTHDPFVAAHADKVVFLLDG 219
Cdd:TIGR01271 582 VTEKEIFE--SCLCKLMsNKTRILVTSKLEHLKKADKILLLHEG 623
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
26-218 |
1.04e-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: 58.87 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 26 INLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKElalfrRHKIGFIFQQFNLIPVFSAEEN 105
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAV-----RQSLGMCPQHNILFHHLTVAEH 1023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 106 VGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAA 185
Cdd:TIGR01257 1024 ILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDL 1103
|
170 180 190
....*....|....*....|....*....|...
gi 872553587 186 LRNAcdELGQTAVVVTHdpfvaaHADKVVFLLD 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 |
1.31e-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: 56.04 E-value: 1.31e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 872553587 144 LSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVAAHADKVVFLLDGE 220
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEGE 148
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
22-220 |
1.45e-09 |
|
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: 57.17 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 22 ILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGteistlkekelalfrrhKIGFIfQQFNLIPVFS 101
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-----------------RISFS-SQFSWIMPGT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 102 AEENVGLPLLLDNVsQKKATMTATRLLE-LVGLKGKEKHLPAQ----LSGGQQQRVAIARAFANEPAIILADEPTGALDS 176
Cdd:cd03291 114 IKENIIFGVSYDEY-RYKSVVKACQLEEdITKFPEKDNTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 872553587 177 ENSKNIIAALrnACDELG-QTAVVVTHDPFVAAHADKVVFLLDGE 220
Cdd:cd03291 193 FTEKEIFESC--VCKLMAnKTRILVTSKMEHLKKADKILILHEGS 235
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
5-224 |
2.56e-09 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 56.23 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 5 EIKRLekSFDIGDskVKILKGINLQIQKGDFVCIMGASGSGKttllqllggldipSV---------------GSIRVDGT 69
Cdd:COG0396 2 EIKNL--HVSVEG--KEILKGVNLTIKPGEVHAIMGPNGSGK-------------STlakvlmghpkyevtsGSILLDGE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 70 EISTLKEKELAlfrRHKIGFIFQQfnliPV---------F--SAEENVGLPLLldnvSQKKATMTATRLLELVGLKGK-- 136
Cdd:COG0396 65 DILELSPDERA---RAGIFLAFQY----PVeipgvsvsnFlrTALNARRGEEL----SAREFLKLLKEKMKELGLDEDfl 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 137 EKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGALDsenskniIAALR---NACDEL---GQTAVVVTHDP----FV 206
Cdd:COG0396 134 DRYVNEGFSGGEKKRNEILQMLLLEPKLAILDETDSGLD-------IDALRivaEGVNKLrspDRGILIITHYQrildYI 206
|
250
....*....|....*...
gi 872553587 207 aaHADKVVFLLDGEVIHE 224
Cdd:COG0396 207 --KPDFVHVLVDGRIVKS 222
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
22-224 |
3.69e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 56.81 E-value: 3.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 22 ILKGINLQIQKGDFVCIMGASGSGKTTLLQLLggldipsVGSIR---VDGTEISTLKEKELALFRRhkIGFIFQQFNLIP 98
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNAL-------AGRIQgnnFTGTILANNRKPTKQILKR--TGFVTQDDILYP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 99 VFSAEEN---VGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQ-----LSGGQQQRVAIARAFANEPAIILADEP 170
Cdd:PLN03211 154 HLTVRETlvfCSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEP 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 872553587 171 TGALDSENSKNIIAALRNACDElGQTAVVVTHDPF--VAAHADKVVFLLDGEVIHE 224
Cdd:PLN03211 234 TSGLDATAAYRLVLTLGSLAQK-GKTIVTSMHQPSsrVYQMFDSVLVLSEGRCLFF 288
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
22-207 |
4.91e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.85 E-value: 4.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 22 ILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALFRRHKIGfifqqfnLIPVFS 101
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLPG-------LKADLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 102 AEENVGLpllLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSEN--- 178
Cdd:PRK13543 99 TLENLHF---LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGitl 175
|
170 180 190
....*....|....*....|....*....|
gi 872553587 179 -SKNIIAALRNacdelGQTAVVVTHDPFVA 207
Cdd:PRK13543 176 vNRMISAHLRG-----GGAALVTTHGAYAA 200
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-221 |
6.11e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 56.33 E-value: 6.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 21 KILKGINLQIQKGDFVCIMGASGSGKttllqllggldipsvgsirvdgteiSTLKEKELALFRRHK--------IGFIFQ 92
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGK-------------------------STLLQSLLSQFEISEgrvwaersIAYVPQ 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 93 QF---------NLIpvFSAEENVGLplLLD--NVSQKKATMT--ATRLLELVGLKGkekhlpAQLSGGQQQRVAIARA-F 158
Cdd:PTZ00243 729 QAwimnatvrgNIL--FFDEEDAAR--LADavRVSQLEADLAqlGGGLETEIGEKG------VNLSGGQKARVSLARAvY 798
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 872553587 159 ANEPAIILaDEPTGALDSENSKNII-----AALRnacdelGQTAVVVTHDPFVAAHADKVVFLLDGEV 221
Cdd:PTZ00243 799 ANRDVYLL-DDPLSALDAHVGERVVeecflGALA------GKTRVLATHQVHVVPRADYVVALGDGRV 859
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-221 |
6.31e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 55.83 E-value: 6.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 3 IIEIKRLEKSFdigdSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKelalf 82
Cdd:PRK15439 11 LLCARSISKQY----SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 83 RRHKIG--FIFQQFNLIPVFSAEENVGLPLLLDNVSQKKatMTAtrLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFAN 160
Cdd:PRK15439 82 KAHQLGiyLVPQEPLLFPNLSVKENILFGLPKRQASMQK--MKQ--LLAALGCQLDLDSSAGSLEVADRQIVEILRGLMR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 872553587 161 EPAIILADEPTGALDSENSKNIIAALRnACDELGQTAVVVTHD-PFVAAHADKVVFLLDGEV 221
Cdd:PRK15439 158 DSRILILDEPTASLTPAETERLFSRIR-ELLAQGVGIVFISHKlPEIRQLADRISVMRDGTI 218
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
15-216 |
1.12e-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: 53.48 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 15 IGDSKVKILKGINLQIQKGDFVCIMGASGSGKTtllqllggldipsvgSIRVDG--TEISTLKEKELALFRRHKIGFIFQ 92
Cdd:cd03238 3 VSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKS---------------TLVNEGlyASGKARLISFLPKFSRNKLIFIDQ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 93 QFNLIpvfsaeeNVGLPLLldNVSQKKATmtatrllelvglkgkekhlpaqLSGGQQQRVAIARAFANEP--AIILADEP 170
Cdd:cd03238 68 LQFLI-------DVGLGYL--TLGQKLST----------------------LSGGELQRVKLASELFSEPpgTLFILDEP 116
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 872553587 171 TGALDSENSKNIIAALRNACDeLGQTAVVVTHDPFVAAHADKVVFL 216
Cdd:cd03238 117 STGLHQQDINQLLEVIKGLID-LGNTVILIEHNLDVLSSADWIIDF 161
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
21-221 |
3.84e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 53.63 E-value: 3.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 21 KILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKElALfrRHKIGFIFQ---QFNLI 97
Cdd:PRK09700 277 KKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLD-AV--KKGMAYITEsrrDNGFF 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 98 PVFSAEENVGLPLLLDN---------VSQKKATMTATRLLELVGLK--GKEKHLpAQLSGGQQQRVAIARAFANEPAIIL 166
Cdd:PRK09700 354 PNFSIAQNMAISRSLKDggykgamglFHEVDEQRTAENQRELLALKchSVNQNI-TELSGGNQQKVLISKWLCCCPEVII 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 872553587 167 ADEPTGALDSENSKNIIAALRNACDElGQTAVVVTHD-PFVAAHADKVVFLLDGEV 221
Cdd:PRK09700 433 FDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSElPEIITVCDRIAVFCEGRL 487
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
4-224 |
4.74e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.83 E-value: 4.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 4 IEIKRLEKSFDIGDSKvKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPS-VGSIRVDGT-----EISTLKEK 77
Cdd:PLN03232 615 ISIKNGYFSWDSKTSK-PTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAeTSSVVIRGSvayvpQVSWIFNA 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 78 ELalfrRHKIGFiFQQFNLIPVFSAEENVGLPLLLDnvsqkkatMTATRLLELVGLKGkekhlpAQLSGGQQQRVAIARA 157
Cdd:PLN03232 694 TV----RENILF-GSDFESERYWRAIDVTALQHDLD--------LLPGRDLTEIGERG------VNISGGQKQRVSMARA 754
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 158 FANEPAIILADEPTGALDSENSKNIIaalrNAC--DEL-GQTAVVVTHDPFVAAHADKVVFLLDGEVIHE 224
Cdd:PLN03232 755 VYSNSDIYIFDDPLSALDAHVAHQVF----DSCmkDELkGKTRVLVTNQLHFLPLMDRIILVSEGMIKEE 820
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
144-224 |
7.08e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.20 E-value: 7.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 144 LSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIaalrNAC--DELGQ-TAVVVTHDPFVAAHADKVVFLLDGE 220
Cdd:PLN03130 741 ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVF----DKCikDELRGkTRVLVTNQLHFLSQVDRIILVHEGM 816
|
....
gi 872553587 221 VIHE 224
Cdd:PLN03130 817 IKEE 820
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
142-203 |
8.16e-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: 52.63 E-value: 8.16e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 872553587 142 AQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENskniIAALRNACDELGQTAVVVTHD 203
Cdd:TIGR03719 160 TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES----VAWLERHLQEYPGTVVAVTHD 217
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
15-204 |
1.01e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 52.54 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 15 IGDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSV--GSIRVDG--------TEIS------------ 72
Cdd:PLN03140 888 VTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYieGDIRISGfpkkqetfARISgyceqndihspq 967
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 73 -TLKEKelalfrrhkigFIFQQFNLIPV-FSAEENVglpLLLDNVSQkkatmtatrLLELVGLKGKEKHLPA--QLSGGQ 148
Cdd:PLN03140 968 vTVRES-----------LIYSAFLRLPKeVSKEEKM---MFVDEVME---------LVELDNLKDAIVGLPGvtGLSTEQ 1024
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 872553587 149 QQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDElGQTAVVVTHDP 204
Cdd:PLN03140 1025 RKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDT-GRTVVCTIHQP 1079
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
17-222 |
1.33e-07 |
|
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: 51.45 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 17 DSKVK-ILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfrRHKIGFIFQQfn 95
Cdd:cd03288 30 ENNLKpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTL----RSRLSIILQD-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 96 liPV-FSAEENVGLpllldnvsQKKATMTATRL---LELVGLKGKEKHLPAQL-----------SGGQQQRVAIARAFAN 160
Cdd:cd03288 104 --PIlFSGSIRFNL--------DPECKCTDDRLweaLEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVR 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 872553587 161 EPAIILADEPTGALD--SEN--SKNIIAALRNacdelgQTAVVVTHDPFVAAHADKVVFLLDGEVI 222
Cdd:cd03288 174 KSSILIMDEATASIDmaTENilQKVVMTAFAD------RTVVTIAHRVSTILDADLVLVLSRGILV 233
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
144-203 |
1.47e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 51.73 E-value: 1.47e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 144 LSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHD 203
Cdd:PRK13409 454 LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHD 513
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
22-204 |
1.77e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 50.26 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 22 ILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELALFRRHKIGfifqqfnLIPVFS 101
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGHRNA-------MKPALT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 102 AEENvgLPLLLDNVSQKKATMTATrlLELVGLKGKEkHLPAQ-LSGGQQQRVAIAR-AFANEPAIILaDEPTGALDSENS 179
Cdd:PRK13539 90 VAEN--LEFWAAFLGGEELDIAAA--LEAVGLAPLA-HLPFGyLSAGQKRRVALARlLVSNRPIWIL-DEPTAALDAAAV 163
|
170 180
....*....|....*....|....*...
gi 872553587 180 K---NIIAALRNAcdelGQTAVVVTHDP 204
Cdd:PRK13539 164 AlfaELIRAHLAQ----GGIVIAATHIP 187
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
22-221 |
1.86e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 51.70 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 22 ILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfRRhkigfifqQFNLIPvfs 101
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLREL---RR--------QFSMIP--- 1390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 102 aeenvGLPLLLD-----NVSQKKATMTAT--RLLELVGLKGkekHLPAQLSG--------------GQQQRVAIARAFAN 160
Cdd:PTZ00243 1391 -----QDPVLFDgtvrqNVDPFLEASSAEvwAALELVGLRE---RVASESEGidsrvleggsnysvGQRQLMCMARALLK 1462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 872553587 161 E-PAIILADEPTGALDSENSKNIIAALRNACDelGQTAVVVTHDPFVAAHADKVVFLLDGEV 221
Cdd:PTZ00243 1463 KgSGFILMDEATANIDPALDRQIQATVMSAFS--AYTVITIAHRLHTVAQYDKIIVMDHGAV 1522
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
141-214 |
2.06e-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: 49.91 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 141 PAQLSGGQQQ------RVAIARAF-ANEPAIILaDEPTGALDSENSKNiiaALRNACDELGQTAV----VVTHDPFVAAH 209
Cdd:cd03240 113 RGRCSGGEKVlasliiRLALAETFgSNCGILAL-DEPTTNLDEENIEE---SLAEIIEERKSQKNfqliVITHDEELVDA 188
|
....*
gi 872553587 210 ADKVV 214
Cdd:cd03240 189 ADHIY 193
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-209 |
3.32e-07 |
|
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: 50.70 E-value: 3.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 2 NIIEIKRLEKSFdiGDskvKIL-KGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEistlkekela 80
Cdd:TIGR03719 321 KVIEAENLTKAF--GD---KLLiDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETV---------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 81 lfrrhKIGFIFQQF-NLIPVFSAEENV--GLPLLLDNvsqkKATMTATRLLELVGLKGKEKH-LPAQLSGGQQQRVAIAR 156
Cdd:TIGR03719 386 -----KLAYVDQSRdALDPNKTVWEEIsgGLDIIKLG----KREIPSRAYVGRFNFKGSDQQkKVGQLSGGERNRVHLAK 456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 872553587 157 AFANEPAIILADEPTGALDSENskniIAALRNACDELGQTAVVVTHDPF----VAAH 209
Cdd:TIGR03719 457 TLKSGGNVLLLDEPTNDLDVET----LRALEEALLNFAGCAVVISHDRWfldrIATH 509
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
144-203 |
3.78e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 50.55 E-value: 3.78e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 144 LSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHD 203
Cdd:COG1245 456 LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHD 515
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-188 |
7.56e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.73 E-value: 7.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 20 VKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKElALfrRHKIGFIFQQFNLIPV 99
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKE-AL--ENGISMVHQELNLVLQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 100 FSAEENVGL---PLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGALdS 176
Cdd:PRK10982 88 RSVMDNMWLgryPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL-T 166
|
170
....*....|....*.
gi 872553587 177 ENSKN----IIAALRN 188
Cdd:PRK10982 167 EKEVNhlftIIRKLKE 182
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
128-222 |
1.44e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.79 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 128 LELVGLKGkEKHLpAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENskniIAALRNACDELGQTAVVVTHD-PFV 206
Cdd:PRK11147 143 LAQLGLDP-DAAL-SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET----IEWLEGFLKTFQGSIIFISHDrSFI 216
|
90
....*....|....*.
gi 872553587 207 AAHADKVVFLLDGEVI 222
Cdd:PRK11147 217 RNMATRIVDLDRGKLV 232
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
145-232 |
1.47e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.95 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 145 SGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVAAHA--DKVVFLLDGEVI 222
Cdd:TIGR00956 211 SGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCSQDAYElfDKVIVLYEGYQI 290
|
90
....*....|....*...
gi 872553587 223 H----EHA----ESKGWK 232
Cdd:TIGR00956 291 YfgpaDKAkqyfEKMGFK 308
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
142-220 |
1.78e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.87 E-value: 1.78e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 872553587 142 AQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDELGQTAVVVTHDPFVAAHADKVVFLLDGE 220
Cdd:PTZ00265 578 SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRYANTIFVLSNRE 656
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
143-214 |
1.82e-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: 1.82e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 872553587 143 QLSGGQQQRVAIARAFANE-----PAIILaDEPTGALDSENSKNIIAAL-RNACDelGQTAVVVTHDPFVAAHADKVV 214
Cdd:cd03227 77 QLSGGEKELSALALILALAslkprPLYIL-DEIDRGLDPRDGQALAEAIlEHLVK--GAQVIVITHLPELAELADKLI 151
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-202 |
1.83e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 48.19 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 2 NIIEIKRLEKSFdigdSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDiPSVGSirvDGTEISTLKEKELAL 81
Cdd:NF000106 12 NAVEVRGLVKHF----GEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G-PDAGR---RPWRF*TWCANRRAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 82 frRHKIGFIFQ-QFNLIPVFSAEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFAN 160
Cdd:NF000106 84 --RRTIG*HRPvR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 872553587 161 EPAIILADEPTGALDSENSKNIIAALRNACDElGQTAVVVTH 202
Cdd:NF000106 162 RPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQ 202
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
23-214 |
1.91e-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: 47.64 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 23 LKGINLQIQKGDFVCIMGASGSGKTT---------------------LLQLLGGLDIPSVGSIRVDGTEIStLKEKELAL 81
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSlafdtiyaegqrryveslsayARQFLGQMDKPDVDSIEGLSPAIA-IDQKTTSR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 82 FRRHKIGFIFQQFNLIPVFSAEE----------NVGLPLLldnvSQKKATMTatrllelvglkgkekhlpaqLSGGQQQR 151
Cdd:cd03270 90 NPRSTVGTVTEIYDYLRLLFARVgirerlgflvDVGLGYL----TLSRSAPT--------------------LSGGEAQR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 872553587 152 VAIARAFANEPAIIL--ADEPTGALDSENSKNIIAALRNACDeLGQTAVVVTHDPFVAAHADKVV 214
Cdd:cd03270 146 IRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRD-LGNTVLVVEHDEDTIRAADHVI 209
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
11-231 |
1.97e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 48.56 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 11 KSFDIGDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfrRHKIGFI 90
Cdd:PRK10789 319 RQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSW----RSRLAVV 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 91 FQQFNLipvFSAEENVGLPLLLDNVSQKKATMTAtRL-------LEL-------VGLKGkekhlpAQLSGGQQQRVAIAR 156
Cdd:PRK10789 395 SQTPFL---FSDTVANNIALGRPDATQQEIEHVA-RLasvhddiLRLpqgydteVGERG------VMLSGGQKQRISIAR 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 157 AFANEPAIILADEPTGALDSENSKNIIAALRNACDelGQTAVVVTHDPFVAAHADKVVFLLDGEVI----HEH-AESKGW 231
Cdd:PRK10789 465 ALLLNAEILILDDALSAVDGRTEHQILHNLRQWGE--GRTVIISAHRLSALTEASEILVMQHGHIAqrgnHDQlAQQSGW 542
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-187 |
2.54e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 46.87 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 1 MNIIEIkrlekSFDIGDSKvkILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEIstlkEKELA 80
Cdd:PRK13540 2 LDVIEL-----DFDYHDQP--LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLC 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 81 LFRRhKIGFIFQQFNLIPVFSAEENVglpllLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFAN 160
Cdd:PRK13540 71 TYQK-QLCFVGHRSGINPYLTLRENC-----LYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMS 144
|
170 180
....*....|....*....|....*..
gi 872553587 161 EPAIILADEPTGALDSENSKNIIAALR 187
Cdd:PRK13540 145 KAKLWLLDEPLVALDELSLLTIITKIQ 171
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-223 |
6.11e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.81 E-value: 6.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 2 NIIEIKRLEKSFDIGdskvKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLggldipsVGSIRVDGTEIstlKEKELAl 81
Cdd:PRK15064 318 NALEVENLTKGFDNG----PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTL-------VGELEPDSGTV---KWSENA- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 82 frrhKIGFIFQQfnlipvfSAEENVGLPLLLDNVSQKKA------TMTAT--RLLelvgLKGKEKHLPAQ-LSGGQQQRV 152
Cdd:PRK15064 383 ----NIGYYAQD-------HAYDFENDLTLFDWMSQWRQegddeqAVRGTlgRLL----FSQDDIKKSVKvLSGGEKGRM 447
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 872553587 153 AIARAFANEPAIILADEPTGALDSENskniIAALRNACDELGQTAVVVTHD-PFVAAHADKVVFLLDGEVIH 223
Cdd:PRK15064 448 LFGKLMMQKPNVLVMDEPTNHMDMES----IESLNMALEKYEGTLIFVSHDrEFVSSLATRIIEITPDGVVD 515
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
14-226 |
8.33e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 46.44 E-value: 8.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 14 DIGDS--KVKILKG------INLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEIStlkekelalFR-- 83
Cdd:PRK11288 252 PLGEVrlRLDGLKGpglrepISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID---------IRsp 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 84 RHKI--GFIF-----QQFNLIPVFSAEENVGLP---------LLLDNvsqKKATMTATRLLELVGLKGKEKHLP-AQLSG 146
Cdd:PRK11288 323 RDAIraGIMLcpedrKAEGIIPVHSVADNINISarrhhlragCLINN---RWEAENADRFIRSLNIKTPSREQLiMNLSG 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 147 GQQQRVAIARAFANEPAIILADEPTGALDSeNSKNIIAALRNACDELGQTAVVVTHD-PFVAAHADKVVFL----LDGEV 221
Cdd:PRK11288 400 GNQQKAILGRWLSEDMKVILLDEPTRGIDV-GAKHEIYNVIYELAAQGVAVLFVSSDlPEVLGVADRIVVMregrIAGEL 478
|
....*
gi 872553587 222 IHEHA 226
Cdd:PRK11288 479 AREQA 483
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-46 |
9.39e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 45.79 E-value: 9.39e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 872553587 2 NIIEIKRLEKSfdIGDskVKILKGINLQIQKGDFVCIMGASGSGK 46
Cdd:CHL00131 6 PILEIKNLHAS--VNE--NEILKGLNLSINKGEIHAIMGPNGSGK 46
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-221 |
9.90e-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: 46.36 E-value: 9.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 3 IIEIKRLeKSFDIGDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLdIPSV--GSIRVDGTEISTlkeKELA 80
Cdd:TIGR02633 257 ILEARNL-TCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGA-YPGKfeGNVFINGKPVDI---RNPA 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 81 LFRRHKIGFI---FQQFNLIPVFSAEENVGLPLL--------LDNVSQKKATMTATRLLELvglKGKEKHLP-AQLSGGQ 148
Cdd:TIGR02633 332 QAIRAGIAMVpedRKRHGIVPILGVGKNITLSVLksfcfkmrIDAAAELQIIGSAIQRLKV---KTASPFLPiGRLSGGN 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 872553587 149 QQRVAIARAFANEPAIILADEPTGALDSeNSKNIIAALRNACDELGQTAVVVTHD-PFVAAHADKVVFLLDGEV 221
Cdd:TIGR02633 409 QQKAVLAKMLLTNPRVLILDEPTRGVDV-GAKYEIYKLINQLAQEGVAIIVVSSElAEVLGLSDRVLVIGEGKL 481
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
142-203 |
1.54e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.88 E-value: 1.54e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 872553587 142 AQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENskniIAALRNACDELGQTAVVVTHD 203
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES----VAWLEQFLHDYPGTVVAVTHD 219
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
143-209 |
2.48e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.11 E-value: 2.48e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 872553587 143 QLSGGQQQRVAIARAFANEPAIILADEPTGALDSENskniIAALRNACDELGQTAVVVTHDPF----VAAH 209
Cdd:PRK11819 445 VLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVET----LRALEEALLEFPGCAVVISHDRWfldrIATH 511
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
144-204 |
3.19e-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: 44.74 E-value: 3.19e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 872553587 144 LSGGQQQRVAIARAFANEPAIILADEPTGALdsenSKNIIAALRNACDELGQTAVVVTHDP 204
Cdd:TIGR00954 583 LSGGEKQRIAMARLFYHKPQFAILDECTSAV----SVDVEGYMYRLCREFGITLFSVSHRK 639
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
92-203 |
3.27e-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: 43.89 E-value: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 92 QQFNLIPVfSAEENVGLplLLDNVSQKKATMTATRLLELVGLKgkEKHLpAQLSGGQQQRVAIARAFANEPAIILADEPT 171
Cdd:cd03236 94 QYVDLIPK-AVKGKVGE--LLKKKDERGKLDELVDQLELRHVL--DRNI-DQLSGGELQRVAIAAALARDADFYFFDEPS 167
|
90 100 110
....*....|....*....|....*....|..
gi 872553587 172 GALDSENSKNIIAALRNACDElGQTAVVVTHD 203
Cdd:cd03236 168 SYLDIKQRLNAARLIRELAED-DNYVLVVEHD 198
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
144-224 |
3.69e-05 |
|
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: 44.62 E-value: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 144 LSGGQQQRVAIARAFANEPAIIL--ADEPTGALDSENSKNIIAALRNACDeLGQTAVVVTHDPFVAAHADKVVFL----- 216
Cdd:TIGR00630 489 LSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHQRDNRRLINTLKRLRD-LGNTLIVVEHDEDTIRAADYVIDIgpgag 567
|
....*....
gi 872553587 217 -LDGEVIHE 224
Cdd:TIGR00630 568 eHGGEVVAS 576
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
144-232 |
5.26e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.08 E-value: 5.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 144 LSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALrnacdELGQTAV-VVTHDP-FVAAHADKVVFLLDGEV 221
Cdd:PLN03073 628 LSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGL-----VLFQGGVlMVSHDEhLISGSVDELWVVSEGKV 702
|
90
....*....|.
gi 872553587 222 IHEHAESKGWK 232
Cdd:PLN03073 703 TPFHGTFHDYK 713
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
26-224 |
5.86e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 43.89 E-value: 5.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 26 INLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKElalfrRHKIGFIF-----QQFNLIPVF 100
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ-----RLARGLVYlpedrQSSGLYLDA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 101 SAEENVG------LPLLLDnvsQKKATMTATRLLELVGLKGKEKHLPAQ-LSGGQQQRVAIARAFANEPAIILADEPTGA 173
Cdd:PRK15439 357 PLAWNVCalthnrRGFWIK---PARENAVLERYRRALNIKFNHAEQAARtLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 872553587 174 LDSENSKNIIAALRNACDElgQTAVVVTHDPF--VAAHADKVVFLLDGEVIHE 224
Cdd:PRK15439 434 VDVSARNDIYQLIRSIAAQ--NVAVLFISSDLeeIEQMADRVLVMHQGEISGA 484
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
2-219 |
8.19e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 43.56 E-value: 8.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 2 NIIEIKRLEKSFDIGDSKVKILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGglDIPSVGSIrVDGTEISTLKEKELAL 81
Cdd:TIGR00956 758 DIFHWRNLTYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLA--ERVTTGVI-TGGDRLVNGRPLDSSF 834
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 82 FRRhkIGFIFQQFNLIP--------VFSAEenvglpLLLDNVSQKKATM----TATRLLE-------LVGLKGKekhlpa 142
Cdd:TIGR00956 835 QRS--IGYVQQQDLHLPtstvreslRFSAY------LRQPKSVSKSEKMeyveEVIKLLEmesyadaVVGVPGE------ 900
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 143 QLSGGQQQRVAIARAFANEPAIIL-ADEPTGALDSENSKNIIAALRNACDElGQTAVVVTHDP--FVAAHADKVVFLLDG 219
Cdd:TIGR00956 901 GLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADH-GQAILCTIHQPsaILFEEFDRLLLLQKG 979
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
144-224 |
1.08e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 43.07 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 144 LSGGQQQRVAIARAFANEPAIILADEPTGALDSeNSKNIIAALRNACDELGQTAVVVTHD-PFVAAHADKVVflldgeVI 222
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDV-GAKKEIYQLINQFKAEGLSIILVSSEmPEVLGMSDRIL------VM 468
|
..
gi 872553587 223 HE 224
Cdd:PRK10762 469 HE 470
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-175 |
1.32e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 43.19 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 22 ILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfrRHKIGFIFQ--------- 92
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDL----RKVLGIIPQapvlfsgtv 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 93 QFNLIPvFSAEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEkhlpaQLSGGQQQRVAIARAFANEPAIILADEPTG 172
Cdd:PLN03130 1330 RFNLDP-FNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGE-----NFSVGQRQLLSLARALLRRSKILVLDEATA 1403
|
...
gi 872553587 173 ALD 175
Cdd:PLN03130 1404 AVD 1406
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
96-224 |
1.42e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 42.61 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 96 LIPVFSAEENVGLPLL--------LDNVSQKKATMTATRLLELvglKGKEKHLP-AQLSGGQQQRVAIARAFANEPAIIL 166
Cdd:PRK13549 352 IVPVMGVGKNITLAALdrftggsrIDDAAELKTILESIQRLKV---KTASPELAiARLSGGNQQKAVLAKCLLLNPKILI 428
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 872553587 167 ADEPTGALDSeNSKNIIAALRNACDELGQTAVVVTHD-PFVAAHADKVVflldgeVIHE 224
Cdd:PRK13549 429 LDEPTRGIDV-GAKYEIYKLINQLVQQGVAIIVISSElPEVLGLSDRVL------VMHE 480
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
12-203 |
1.47e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 42.63 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 12 SFDIGDSKvkILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVdGTEIstlkekELALFRRHKIgfif 91
Cdd:PRK11147 326 NYQIDGKQ--LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKL------EVAYFDQHRA---- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 92 qqfNLIPvfsaEENVglpllLDNVSQKKATMTatrllelvgLKGKEKHL----------PAQ-------LSGGQQQRVAI 154
Cdd:PRK11147 393 ---ELDP----EKTV-----MDNLAEGKQEVM---------VNGRPRHVlgylqdflfhPKRamtpvkaLSGGERNRLLL 451
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 872553587 155 ARAFANEPAIILADEPTGALDSENskniIAALRNACDELGQTAVVVTHD 203
Cdd:PRK11147 452 ARLFLKPSNLLILDEPTNDLDVET----LELLEELLDSYQGTVLLVSHD 496
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
26-228 |
1.64e-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: 42.48 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 26 INLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEIStlkEKELALFRRHkigF--IFQQFNLipvFsaE 103
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT---ADNREAYRQL---FsaVFSDFHL---F--D 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 104 ENVGLPlllDNVSQKKatmtATRLLELVGLKGKEKH-----LPAQLSGGQQQRVAIARAFANEPAIILADEptGALD--- 175
Cdd:COG4615 420 RLLGLD---GEADPAR----ARELLERLELDHKVSVedgrfSTTDLSQGQRKRLALLVALLEDRPILVFDE--WAADqdp 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 176 -------SEnsknIIAALRnacdELGQTAVVVTHDPFVAAHADKVVFLLDGEVIHEHAES 228
Cdd:COG4615 491 efrrvfyTE----LLPELK----ARGKTVIAISHDDRYFDLADRVLKMDYGKLVELTGPA 542
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
142-214 |
1.86e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 1.86e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 872553587 142 AQLSGGQQQRVAIARAFANEPAII--LADEPTGAL---DSENSKNIIAALRNAcdelGQTAVVVTHDPFVAAHADKVV 214
Cdd:PRK00635 475 ATLSGGEQERTALAKHLGAELIGItyILDEPSIGLhpqDTHKLINVIKKLRDQ----GNTVLLVEHDEQMISLADRII 548
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
22-189 |
1.91e-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: 41.76 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 22 ILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLdIPSVGSIRVDGTEISTLKEKELalfrRHKIGFIFQQfnlIPVFS 101
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGVSWNSVPLQKW----RKAFGVIPQK---VFIFS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 102 AEENVGLpllldNVSQKKATMTATRLLELVGLKGKEKHLPAQL-----------SGGQQQRVAIARAFANEPAIILADEP 170
Cdd:cd03289 91 GTFRKNL-----DPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLDEP 165
|
170
....*....|....*....
gi 872553587 171 TGALDSENSKNIIAALRNA 189
Cdd:cd03289 166 SAHLDPITYQVIRKTLKQA 184
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
143-203 |
2.06e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 42.10 E-value: 2.06e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 872553587 143 QLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRnacdEL--GQTAVVVTHD 203
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIR----ELaeGKYVLVVEHD 270
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
68-203 |
2.28e-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: 42.08 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 68 GTEIST----LKEKELalfrR--HKIgfifQQFNLIP-VFSAeeNVGLplLLDNVSQKKAtmtATRLLELVGLKGKEKHL 140
Cdd:COG1245 145 GTELQDyfkkLANGEI----KvaHKP----QYVDLIPkVFKG--TVRE--LLEKVDERGK---LDELAEKLGLENILDRD 209
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 872553587 141 PAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALRNACDElGQTAVVVTHD 203
Cdd:COG1245 210 ISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHD 271
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
22-225 |
3.00e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 41.89 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 22 ILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTLKEKELalfrRHKIGFIFQ--------- 92
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDL----RRVLSIIPQspvlfsgtv 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 93 QFNLIPvFSAEENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEkhlpaQLSGGQQQRVAIARAFANEPAIILADEPTG 172
Cdd:PLN03232 1327 RFNIDP-FSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGE-----NFSVGQRQLLSLARALLRRSKILVLDEATA 1400
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 872553587 173 ALDSENSKNIIAALR---NACdelgqTAVVVTHDPFVAAHADKVVFLLDGEVIhEH 225
Cdd:PLN03232 1401 SVDVRTDSLIQRTIReefKSC-----TMLVIAHRLNTIIDCDKILVLSSGQVL-EY 1450
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-220 |
3.41e-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: 40.05 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 32 KGDFVCIMGASGSGKttllqllggldipsvgsirvdgteiSTLKEKELALFRRHKIGFIfqqfnlipVFSAEENvglpll 111
Cdd:smart00382 1 PGEVILIVGPPGSGK-------------------------TTLARALARELGPPGGGVI--------YIDGEDI------ 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 112 ldnvsqkkatmtaTRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNIIAALR---- 187
Cdd:smart00382 42 -------------LEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrll 108
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 872553587 188 -NACDELGQTAVVVTHDPFV------AAHADKVVFLLDGE 220
Cdd:smart00382 109 lLLKSEKNLTVILTTNDEKDlgpallRRRFDRRIVLLLIL 148
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
22-202 |
4.01e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 40.93 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 22 ILKGINLQIQKGDFVCIMGASGSGKTTLLQLLGGLDIPSV--GSIRVDGTEISTLKEKELAlfrRHKIGFIFQQFNLIPV 99
Cdd:PRK09580 16 ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVtgGTVEFKGKDLLELSPEDRA---GEGIFMAFQYPVEIPG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 100 FSAEenVGLPLLLDNVSQKKATMTATR--LLELVGLKGKEKHLPAQL---------SGGQQQRVAIARAFANEPAIILAD 168
Cdd:PRK09580 93 VSNQ--FFLQTALNAVRSYRGQEPLDRfdFQDLMEEKIALLKMPEDLltrsvnvgfSGGEKKRNDILQMAVLEPELCILD 170
|
170 180 190
....*....|....*....|....*....|....
gi 872553587 169 EPTGALDSENSKnIIAALRNACDELGQTAVVVTH 202
Cdd:PRK09580 171 ESDSGLDIDALK-IVADGVNSLRDGKRSFIIVTH 203
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
124-180 |
6.08e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.77 E-value: 6.08e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 872553587 124 ATRLLELVGLKGKEKHLPAQ-LSGGQQQRVAIARAFANEPAIILADEPTGALDSENSK 180
Cdd:PRK10938 381 AQQWLDILGIDKRTADAPFHsLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQ 438
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
144-214 |
6.98e-04 |
|
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: 39.91 E-value: 6.98e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 872553587 144 LSGGQQQRVAIARAFANE---PAIILADEPTGALDSENSKNIIAALrNACDELGQTAVVVTHDPFVAAHADKVV 214
Cdd:cd03271 170 LSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVL-QRLVDKGNTVVVIEHNLDVIKCADWII 242
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
139-216 |
9.81e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.58 E-value: 9.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 139 HLP-----AQLSGGQQQRVAIARAFAN---EPAIILADEPTGALDSENSKNIIAALRNACDElGQTAVVVTHDPFVAAHA 210
Cdd:PRK00635 800 YLPlgrplSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQ-GHTVVIIEHNMHVVKVA 878
|
....*.
gi 872553587 211 DKVVFL 216
Cdd:PRK00635 879 DYVLEL 884
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
143-175 |
1.14e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.23 E-value: 1.14e-03
10 20 30
....*....|....*....|....*....|...
gi 872553587 143 QLSGGQQQRVAIARAFANEPAIILADEPTGALD 175
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
30-202 |
2.02e-03 |
|
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: 39.61 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 30 IQKGDFVCIMGASGSGKTTLLQLLGGLDIPSVGSIRVDGTEISTlkekelalfrrhKIGFIFQQFNLIPVFSA------- 102
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT------------NISDVHQNMGYCPQFDAiddlltg 2029
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 103 EENVGLPLLLDNVSQKKATMTATRLLELVGLKGKEKHLPAQLSGGQQQRVAIARAFANEPAIILADEPTGALDSENSKNI 182
Cdd:TIGR01257 2030 REHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRML 2109
|
170 180
....*....|....*....|
gi 872553587 183 IAALRNACDElGQTAVVVTH 202
Cdd:TIGR01257 2110 WNTIVSIIRE-GRAVVLTSH 2128
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
144-175 |
2.63e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 38.94 E-value: 2.63e-03
10 20 30
....*....|....*....|....*....|..
gi 872553587 144 LSGGQQQRVAIARAFANEPAIILADEPTGALD 175
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGID 423
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
23-46 |
5.63e-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: 38.07 E-value: 5.63e-03
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
23-46 |
8.01e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 37.36 E-value: 8.01e-03
10 20
....*....|....*....|....
gi 872553587 23 LKGINLQIQKGDFVCIMGASGSGK 46
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGK 648
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
121-203 |
8.24e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 36.53 E-value: 8.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872553587 121 TMTATRLLELVGLKGkekhlPAQLSGGQQQRVAIARAFanepAIILaDepTGALDSENSKNIIAALRNacdelgqtAVVV 200
Cdd:COG0419 141 KLKQEILAQLSGLDP-----IETLSGGERLRLALADLL----SLIL-D--FGSLDEERLERLLDALEE--------LAII 200
|
...
gi 872553587 201 THD 203
Cdd:COG0419 201 THV 203
|
|
| |
