|
Name |
Accession |
Description |
Interval |
E-value |
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-220 |
1.12e-102 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 296.18 E-value: 1.12e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSKTYFLENETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLSEI 80
Cdd:COG1136 4 LLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 81 RNKKMGFVFQFHHLLAEFTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDP 160
Cdd:COG1136 84 RRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 931484041 161 LIIFADEPTGNLDEENTNKLLDVFGSL-KSEGRTIILVTHSVDISKFGSHVYKLKERELHA 220
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELnRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-218 |
1.33e-97 |
|
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: 282.84 E-value: 1.33e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 2 LQASTVSKTYFLENETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLSEIR 81
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 82 NKKMGFVFQFHHLLAEFTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPL 161
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 931484041 162 IIFADEPTGNLDEENTNKLLDVFGSL-KSEGRTIILVTHSVDISKFGSHVYKLKEREL 218
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
1-220 |
1.42e-77 |
|
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: 232.24 E-value: 1.42e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSKTYFLENETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLSEI 80
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 81 RNKKMGFVFQFHHLLAEFTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDP 160
Cdd:TIGR02211 81 RNKKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 931484041 161 LIIFADEPTGNLDEENTNKLLDVFGSLKSEGRT-IILVTHSVDISKFGSHVYKLKERELHA 220
Cdd:TIGR02211 161 SLVLADEPTGNLDNNNAKIIFDLMLELNRELNTsFLVVTHDLELAKKLDRVLEMKDGQLFN 221
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-219 |
1.15e-74 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 224.93 E-value: 1.15e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSKTYfleNETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLSEI 80
Cdd:COG2884 1 MIRFENVSKRY---PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 81 RnKKMGFVFQFHHLLAEFTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDP 160
Cdd:COG2884 78 R-RRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 161 LIIFADEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTHSVD-ISKFGSHVYKLKERELH 219
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLElVDRMPKRVLELEDGRLV 216
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-199 |
8.14e-67 |
|
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: 205.36 E-value: 8.14e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSKTYFLENETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLSEI 80
Cdd:COG4181 8 IIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 81 RNKKMGFVFQFHHLLAEFTCLENVALPALVNGSAQnkAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDP 160
Cdd:COG4181 88 RARHVGFVFQSFQLLPTLTALENVMLPLELAGRRD--ARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 931484041 161 LIIFADEPTGNLDEENTNKLLDVFGSLKSE-GRTIILVTH 199
Cdd:COG4181 166 AILFADEPTGNLDAATGEQIIDLLFELNRErGTTLVLVTH 205
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-202 |
5.45e-63 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 196.46 E-value: 5.45e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSKTYFLENETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRlsei 80
Cdd:COG1116 7 ALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDR---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 81 rnkkmGFVFQFHHLLAEFTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDP 160
Cdd:COG1116 83 -----GVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 931484041 161 LIIFADEPTGNLDEENTNKLLDVFGSL-KSEGRTIILVTHSVD 202
Cdd:COG1116 158 EVLLMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHDVD 200
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-199 |
1.03e-62 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 195.21 E-value: 1.03e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSKTYflenETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfSHDDTRLSEI 80
Cdd:COG1126 1 MIEIENLHKSF----GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 81 RnKKMGFVFQ----FHHLlaefTCLENVAL-PALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARA 155
Cdd:COG1126 76 R-RKVGMVFQqfnlFPHL----TVLENVTLaPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 931484041 156 MINDPLIIFADEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTH 199
Cdd:COG1126 151 LAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTH 194
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-205 |
5.50e-62 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 193.11 E-value: 5.50e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSKTYFLENETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLSEI 80
Cdd:PRK11629 5 LLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 81 RNKKMGFVFQFHHLLAEFTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDP 160
Cdd:PRK11629 85 RNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 931484041 161 LIIFADEPTGNLDEENTNKLLDVFGSL-KSEGRTIILVTHSVDISK 205
Cdd:PRK11629 165 RLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAK 210
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-203 |
2.71e-61 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 190.54 E-value: 2.71e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSKTYfleNETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLSEI 80
Cdd:TIGR02673 1 MIEFHNVSKAY---PGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 81 RnKKMGFVFQFHHLLAEFTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDP 160
Cdd:TIGR02673 78 R-RRIGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 931484041 161 LIIFADEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTHSVDI 203
Cdd:TIGR02673 157 PLLLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSL 199
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-202 |
2.41e-59 |
|
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: 185.75 E-value: 2.41e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 2 LQASTVSKTYFLENETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDsvdvfshdDTRLSEiR 81
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVD--------GEPVTG-P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 82 NKKMGFVFQFHHLLAEFTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPL 161
Cdd:cd03293 72 GPDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 931484041 162 IIFADEPTGNLDEENTNKL-LDVFGSLKSEGRTIILVTHSVD 202
Cdd:cd03293 152 VLLLDEPFSALDALTREQLqEELLDIWRETGKTVLLVTHDID 193
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
19-199 |
2.28e-57 |
|
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: 180.80 E-value: 2.28e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 19 EVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFsHDDTRLSEIRnKKMGFVFQFHHLLAEF 98
Cdd:cd03262 14 HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLT-DDKKNINELR-QKVGMVFQQFNLFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 99 TCLENVAL-PALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLDEENT 177
Cdd:cd03262 92 TVLENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELV 171
|
170 180
....*....|....*....|..
gi 931484041 178 NKLLDVFGSLKSEGRTIILVTH 199
Cdd:cd03262 172 GEVLDVMKDLAEEGMTMVVVTH 193
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
1-218 |
4.84e-56 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 177.60 E-value: 4.84e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSKTYFLENETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLSEI 80
Cdd:NF038007 1 MLNMQNAEKCYITKTIKTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKIIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 81 RNKKMGFVFQFHHLLAEFTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDP 160
Cdd:NF038007 81 RRELIGYIFQSFNLIPHLSIFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 931484041 161 LIIFADEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTHSVDISKFGSHVYKLKEREL 218
Cdd:NF038007 161 ALLLADEPTGNLDSKNARAVLQQLKYINQKGTTIIMVTHSDEASTYGNRIINMKDGKL 218
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-205 |
1.77e-54 |
|
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: 173.92 E-value: 1.77e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSKTYFLENETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLSEI 80
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 81 RnKKMGFVFQFHHLLAEFTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDP 160
Cdd:cd03258 81 R-RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 931484041 161 LIIFADEPTGNLDEENTNKLLDVFGSLKSE-GRTIILVTHSVDISK 205
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVK 205
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-203 |
5.42e-54 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 173.32 E-value: 5.42e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSKTYflENETiEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLSEI 80
Cdd:COG3638 2 MLELRNLSKRY--PGGT-PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 81 RnKKMGFVFQFHHLLAEFTCLENVALPAL--------VNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAI 152
Cdd:COG3638 79 R-RRIGMIFQQFNLVPRLSVLTNVLAGRLgrtstwrsLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 931484041 153 ARAMINDPLIIFADEPTGNLDEENTNKLLDVFGSL-KSEGRTIILVTHSVDI 203
Cdd:COG3638 158 ARALVQEPKLILADEPVASLDPKTARQVMDLLRRIaREDGITVVVNLHQVDL 209
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
7-203 |
6.30e-54 |
|
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: 171.82 E-value: 6.30e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 7 VSKTYfleNETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLSEIRnKKMG 86
Cdd:cd03292 6 VTKTY---PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR-RKIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 87 FVFQFHHLLAEFTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFAD 166
Cdd:cd03292 82 VVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIAD 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 931484041 167 EPTGNLDEENTNKLLDVFGSLKSEGRTIILVTHSVDI 203
Cdd:cd03292 162 EPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKEL 198
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
7-220 |
2.38e-53 |
|
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: 170.98 E-value: 2.38e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 7 VSKTYfleNETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfshDDTRLSEIRnKKMG 86
Cdd:COG1122 6 LSFSY---PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDI---TKKNLRELR-RKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 87 FVFQF--HHLLAEfTCLENVALpALVN-GSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLII 163
Cdd:COG1122 79 LVFQNpdDQLFAP-TVEEDVAF-GPENlGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 931484041 164 FADEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTHSVD-ISKFGSHVYKLKERELHA 220
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDlVAELADRVIVLDDGRIVA 214
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-218 |
1.30e-52 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 179.15 E-value: 1.30e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSKTYFLENETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLSEI 80
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 81 RNKKMGFVFQFHHLLAEFTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDP 160
Cdd:PRK10535 84 RREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 931484041 161 LIIFADEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTHSVDISKFGSHVYKLKEREL 218
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-199 |
5.95e-52 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 170.64 E-value: 5.95e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSKTYFLENETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLSEI 80
Cdd:COG1135 1 MIELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 81 RnKKMGFVFQFHHLLAEFTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDP 160
Cdd:COG1135 81 R-RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 931484041 161 LIIFADEPTGNLDEENTNKLLDVFGSLKSE-GRTIILVTH 199
Cdd:COG1135 160 KVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITH 199
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-215 |
2.02e-51 |
|
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: 165.33 E-value: 2.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 7 VSKTYflENETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfshDDTRLSEIRnKKMG 86
Cdd:cd03225 5 LSFSY--PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDL---TKLSLKELR-RKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 87 FVFQF--HHLLAEfTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIF 164
Cdd:cd03225 79 LVFQNpdDQFFGP-TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 931484041 165 ADEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTHSVD-ISKFGSHVYKLKE 215
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDlLLELADRVIVLED 209
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
7-213 |
1.19e-50 |
|
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: 163.17 E-value: 1.19e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 7 VSKTYFleneTIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLSEIRNKKMG 86
Cdd:TIGR03608 4 ISKKFG----DKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRREKLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 87 FVFQFHHLLAEFTCLENVALP-ALVNGSAQNKAYRRAQdLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFA 165
Cdd:TIGR03608 80 YLFQNFALIENETVEENLDLGlKYKKLSKKEKREKKKE-ALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 931484041 166 DEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTHSVDISKFGSHVYKL 213
Cdd:TIGR03608 159 DEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVAKQADRVIEL 206
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-202 |
1.44e-50 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 164.08 E-value: 1.44e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 2 LQASTVSKTYflenETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDdtrlSEIR 81
Cdd:COG1131 1 IEVRGLTKRY----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDP----AEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 82 nKKMGFVFQFHHLLAEFTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPL 161
Cdd:COG1131 73 -RRIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 931484041 162 IIFADEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTHSVD 202
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLE 192
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
18-204 |
2.38e-50 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 163.41 E-value: 2.38e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 18 IEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLSEIRNKKMGFVFQFHHLLAE 97
Cdd:PRK10584 23 LSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKHVGFVFQSFMLIPT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 98 FTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLDEENT 177
Cdd:PRK10584 103 LNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTG 182
|
170 180
....*....|....*....|....*...
gi 931484041 178 NKLLDVFGSLKSE-GRTIILVTHSVDIS 204
Cdd:PRK10584 183 DKIADLLFSLNREhGTTLILVTHDLQLA 210
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
7-215 |
3.98e-49 |
|
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: 160.43 E-value: 3.98e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 7 VSKTYfleNETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLSEIRnKKMG 86
Cdd:cd03256 6 LSKTY---PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR-RQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 87 FVFQFHHLLAEFTCLENVALPALVNGSAQN--------KAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMIN 158
Cdd:cd03256 82 MIFQQFNLIERLSVLENVLSGRLGRRSTWRslfglfpkEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 931484041 159 DPLIIFADEPTGNLDEENTNKLLDVFGSL-KSEGRTIILVTHSVDISK-FGSHVYKLKE 215
Cdd:cd03256 162 QPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAReYADRIVGLKD 220
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-201 |
5.29e-49 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 160.26 E-value: 5.29e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSKTYflenETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFS-HDDTRlsE 79
Cdd:PRK09493 1 MIEFKNVSKHF----GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpKVDER--L 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 80 IRnKKMGFVFQFHHLLAEFTCLENVAL-PALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMIN 158
Cdd:PRK09493 75 IR-QEAGMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAV 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 931484041 159 DPLIIFADEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTHSV 201
Cdd:PRK09493 154 KPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEI 196
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-204 |
6.44e-49 |
|
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: 159.59 E-value: 6.44e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSKTYFLENETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfSHDDTRLSEI 80
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDL-LKLSRRLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 81 RNKKMGFVFQ--FHHLLAEFTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKK---NRLPLEISGGERQRVAIARA 155
Cdd:cd03257 80 RRKEIQMVFQdpMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEevlNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 931484041 156 MINDPLIIFADEPTGNLDEENTNKLLDVFGSLKSE-GRTIILVTHsvDIS 204
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITH--DLG 207
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
19-220 |
1.47e-48 |
|
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: 158.99 E-value: 1.47e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 19 EVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLSEIRnKKMGFVFQFHHLLAEF 98
Cdd:COG1127 19 VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELR-RRIGMLFQGGALFDSL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 99 TCLENVALPALVNGS-AQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLDEENT 177
Cdd:COG1127 98 TVFENVAFPLREHTDlSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITS 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 931484041 178 NKLLDVFGSLKSE-GRTIILVTHSVD-ISKFGSHVYKLKERELHA 220
Cdd:COG1127 178 AVIDELIRELRDElGLTSVVVTHDLDsAFAIADRVAVLADGKIIA 222
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
7-202 |
1.88e-48 |
|
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: 158.07 E-value: 1.88e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 7 VSKTYflenETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfshddTRLSEIRnKKMG 86
Cdd:cd03259 6 LSKTY----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-----TGVPPER-RNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 87 FVFQ----FHHLlaefTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLI 162
Cdd:cd03259 76 MVFQdyalFPHL----TVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 931484041 163 IFADEPTGNLDEENTNKLLD-VFGSLKSEGRTIILVTHSVD 202
Cdd:cd03259 152 LLLDEPLSALDAKLREELREeLKELQRELGITTIYVTHDQE 192
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-199 |
1.93e-47 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 159.49 E-value: 1.93e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSKTYflenETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfshddTRLS-E 79
Cdd:COG3842 5 ALELENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV-----TGLPpE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 80 IRNkkMGFVFQ----FHHLlaefTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARA 155
Cdd:COG3842 76 KRN--VGMVFQdyalFPHL----TVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARA 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 931484041 156 MINDPLIIFADEPTGNLDeentNKL-----LDVFGSLKSEGRTIILVTH 199
Cdd:COG3842 150 LAPEPRVLLLDEPLSALD----AKLreemrEELRRLQRELGITFIYVTH 194
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-218 |
3.72e-47 |
|
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: 155.53 E-value: 3.72e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSKTYfleNETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLSEI 80
Cdd:TIGR02315 1 MLEVENLSKVY---PNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 81 RnKKMGFVFQFHHLLAEFTCLENVALPALVNGSAQNKA--------YRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAI 152
Cdd:TIGR02315 78 R-RRIGMIFQHYNLIERLTVLENVLHGRLGYKPTWRSLlgrfseedKERALSALERVGLADKAYQRADQLSGGQQQRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 931484041 153 ARAMINDPLIIFADEPTGNLDEENTNKLLDVFGSL-KSEGRTIILVTHSVDISK-FGSHVYKLKEREL 218
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRInKEDGITVIINLHQVDLAKkYADRIVGLKAGEI 224
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-219 |
5.13e-47 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 154.65 E-value: 5.13e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSKTYFLENETievLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSvdvfsHDDTRL--S 78
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQA---LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSG-----HDITRLknR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 79 EIR--NKKMGFVFQFHHLLAEFTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAM 156
Cdd:PRK10908 73 EVPflRRQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 931484041 157 INDPLIIFADEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTHSVD-ISKFGSHVYKLKERELH 219
Cdd:PRK10908 153 VNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGlISRRSYRMLTLSDGHLH 216
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
19-210 |
9.53e-47 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 154.40 E-value: 9.53e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 19 EVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVV-----FDsvdvFSH--DDTRLSEIRnKKMGFVFQF 91
Cdd:COG4161 16 QALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNiaghqFD----FSQkpSEKAIRLLR-QKVGMVFQQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 92 HHLLAEFTCLEN-VALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTG 170
Cdd:COG4161 91 YNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 931484041 171 NLDEENTNKLLDVFGSLKSEGRTIILVTHSVDIS-KFGSHV 210
Cdd:COG4161 171 ALDPEITAQVVEIIRELSQTGITQVIVTHEVEFArKVASQV 211
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
20-202 |
2.31e-46 |
|
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: 153.43 E-value: 2.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 20 VLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLSEIRnKKMGFVFQFHHLLAEFT 99
Cdd:cd03261 15 VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR-RRMGMLFQSGALFDSLT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 100 CLENVALPALVNGSAQNKAYR-RAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLDEENTN 178
Cdd:cd03261 94 VFENVAFPLREHTRLSEEEIReIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASG 173
|
170 180
....*....|....*....|....*
gi 931484041 179 KLLDVFGSLKSE-GRTIILVTHSVD 202
Cdd:cd03261 174 VIDDLIRSLKKElGLTSIMVTHDLD 198
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-220 |
4.84e-46 |
|
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: 152.89 E-value: 4.84e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSKTYflenETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLSei 80
Cdd:COG1120 1 MLEAENLSVGY----GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELA-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 81 rnKKMGFVFQFHHLLAEFTCLENVAL------PALVNGSAQNkaYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIAR 154
Cdd:COG1120 75 --RRIAYVPQEPPAPFGLTVRELVALgryphlGLFGRPSAED--REAVEEALERTGLEHLADRPVDELSGGERQRVLIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 931484041 155 AMINDPLIIFADEPTGNLDEENTNKLLDVFGSL-KSEGRTIILVTHSVDI-SKFGSHVYKLKERELHA 220
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLaRERGRTVVMVLHDLNLaARYADRLVLLKDGRIVA 218
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-199 |
6.22e-46 |
|
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: 151.82 E-value: 6.22e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSKTYFLENE---TIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDS----VDVFSHD 73
Cdd:COG4778 4 LLEVENLSKTFTLHLQggkRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHdggwVDLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 74 DTRLSEIRNKKMGFVFQFHHLLAEFTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIgdkKNRL----PLEISGGERQR 149
Cdd:COG4778 84 PREILALRRRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNL---PERLwdlpPATFSGGEQQR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 931484041 150 VAIARAMINDPLIIFADEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTH 199
Cdd:COG4778 161 VNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFH 210
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
21-202 |
7.75e-46 |
|
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: 152.80 E-value: 7.75e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 21 LQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLSEIRNKKMGFVFQFHHLLAEFTC 100
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 101 LENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLDEENTNKL 180
Cdd:cd03294 120 LENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREM 199
|
170 180
....*....|....*....|...
gi 931484041 181 LDVFGSLKSE-GRTIILVTHSVD 202
Cdd:cd03294 200 QDELLRLQAElQKTIVFITHDLD 222
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-205 |
9.89e-46 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 154.57 E-value: 9.89e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSKTYFLENETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLSEI 80
Cdd:PRK11153 1 MIELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 81 RnKKMGFVFQFHHLLAEFTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDP 160
Cdd:PRK11153 81 R-RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 931484041 161 LIIFADEPTGNLDEENTNKLLDVFGSLKSE-GRTIILVTHSVDISK 205
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVK 205
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-204 |
3.17e-45 |
|
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: 156.99 E-value: 3.17e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSKTYFL-ENETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLSE 79
Cdd:COG1123 260 LLEVRNLSKRYPVrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 80 IRnKKMGFVFQ--FHHLLAEFTCLENVALPALVNGSA-QNKAYRRAQDLLDKFDIG-DKKNRLPLEISGGERQRVAIARA 155
Cdd:COG1123 340 LR-RRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLLsRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIARA 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 931484041 156 MINDPLIIFADEPTGNLDEENTNKLLDVFGSLKSE-GRTIILVTHsvDIS 204
Cdd:COG1123 419 LALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISH--DLA 466
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
19-210 |
3.66e-45 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 150.55 E-value: 3.66e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 19 EVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKV-----VFDsvdvFSH--DDTRLSEIRnKKMGFVFQF 91
Cdd:PRK11124 16 QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLniagnHFD----FSKtpSDKAIRELR-RNVGMVFQQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 92 HHLLAEFTCLEN-VALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTG 170
Cdd:PRK11124 91 YNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 931484041 171 NLDEENTNKLLDVFGSLKSEGRTIILVTHSVDIS-KFGSHV 210
Cdd:PRK11124 171 ALDPEITAQIVSIIRELAETGITQVIVTHEVEVArKTASRV 211
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-215 |
9.47e-44 |
|
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: 144.64 E-value: 9.47e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 2 LQASTVSKTYfleNETIeVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLSEIR 81
Cdd:cd03229 1 LELKNVSKRY---GQKT-VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 82 nkKMGFVFQFHHLLAEFTCLENVALPalvngsaqnkayrraqdlldkfdigdkknrlpleISGGERQRVAIARAMINDPL 161
Cdd:cd03229 77 --RIGMVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 931484041 162 IIFADEPTGNLDEENTNKLLDVFGSLKSE-GRTIILVTHSVD-ISKFGSHVYKLKE 215
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDeAARLADRVVVLRD 176
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
7-218 |
1.22e-43 |
|
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: 146.68 E-value: 1.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 7 VSKTYfleNETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLseirNKKMG 86
Cdd:cd03295 6 VTKRY---GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVEL----RRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 87 FVFQFHHLLAEFTCLENVAL-PALvNGSAQNKAYRRAQDLLDKFDIGDKK--NRLPLEISGGERQRVAIARAMINDPLII 163
Cdd:cd03295 79 YVIQQIGLFPHMTVEENIALvPKL-LKWPKEKIRERADELLALVGLDPAEfaDRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 931484041 164 FADEPTGNLDEENTNKLLDVFGSLKSE-GRTIILVTHSVDIS-KFGSHVYKLKEREL 218
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAfRLADRIAIMKNGEI 214
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
20-218 |
1.60e-43 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 144.96 E-value: 1.60e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 20 VLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfshDDTRLSEIRnKKMGFVFQFHHLLAEfT 99
Cdd:COG4619 15 ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPL---SAMPPPEWR-RQVAYVPQEPALWGG-T 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 100 CLENVALPALVNGSAQNKAyrRAQDLLDKFDIGDK-KNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLDEENTN 178
Cdd:COG4619 90 VRDNLPFPFQLRERKFDRE--RALELLERLGLPPDiLDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 931484041 179 KLLDVFGSL-KSEGRTIILVTHSVD-ISKFGSHVYKLKEREL 218
Cdd:COG4619 168 RVEELLREYlAEEGRAVLWVSHDPEqIERVADRVLTLEAGRL 209
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-199 |
4.11e-43 |
|
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: 145.33 E-value: 4.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSKTYFLENETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRlsei 80
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKA---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 81 RNKKMGFVFQ-----FHhllAEFTCLENVALPALVNGSAQNKayRRAQDLLDKFDIGDK-KNRLPLEISGGERQRVAIAR 154
Cdd:COG1124 77 FRRRVQMVFQdpyasLH---PRHTVDRILAEPLRIHGLPDRE--ERIAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIAR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 931484041 155 AMINDPLIIFADEPTGNLDEENTNKLLDVFGSLKSE-GRTIILVTH 199
Cdd:COG1124 152 ALILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSH 197
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-202 |
6.03e-43 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 145.39 E-value: 6.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSKTYFLENETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRlsei 80
Cdd:COG4525 3 MLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 81 rnkkmGFVFQFHHLLAEFTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDP 160
Cdd:COG4525 79 -----GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADP 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 931484041 161 LIIFADEPTGNLD----EENTNKLLDVFgslKSEGRTIILVTHSVD 202
Cdd:COG4525 154 RFLLMDEPFGALDaltrEQMQELLLDVW---QRTGKGVFLITHSVE 196
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
18-200 |
7.21e-43 |
|
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: 143.86 E-value: 7.21e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 18 IEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSL-----DRPTDGKVVFDSVDVFSHDDTRLsEIRnKKMGFVFQfH 92
Cdd:cd03260 13 KHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDVL-ELR-RRVGMVFQ-K 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 93 HLLAEFTCLENVALPALVNGSAQNKAYR-RAQDLLDKFDIGDK-KNRL-PLEISGGERQRVAIARAMINDPLIIFADEPT 169
Cdd:cd03260 90 PNPFPGSIYDNVAYGLRLHGIKLKEELDeRVEEALRKAALWDEvKDRLhALGLSGGQQQRLCLARALANEPEVLLLDEPT 169
|
170 180 190
....*....|....*....|....*....|.
gi 931484041 170 GNLDEENTNKLLDVFGSLKSEgRTIILVTHS 200
Cdd:cd03260 170 SALDPISTAKIEELIAELKKE-YTIVIVTHN 199
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-221 |
1.27e-42 |
|
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: 143.84 E-value: 1.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSKTYflenETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLsei 80
Cdd:COG4555 1 MIEVENLSKKY----GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREAR--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 81 rnKKMGFVFQFHHLLAEFTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDP 160
Cdd:COG4555 74 --RQIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 931484041 161 LIIFADEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTHSV-DISKFGSHVYKLKERELHAL 221
Cdd:COG4555 152 KVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMqEVEALCDRVVILHKGKVVAQ 213
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
20-202 |
2.69e-42 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 146.06 E-value: 2.69e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 20 VLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHddtrLSeIRNKKMGFVFQ----FHHLl 95
Cdd:COG1118 17 LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTN----LP-PRERRVGFVFQhyalFPHM- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 96 aefTCLENVA--LPALVNGSAQNKAyrRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLD 173
Cdd:COG1118 91 ---TVAENIAfgLRVRPPSKAEIRA--RVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALD 165
|
170 180 190
....*....|....*....|....*....|....*.
gi 931484041 174 -------EENTNKLLDVFgslkseGRTIILVTHSVD 202
Cdd:COG1118 166 akvrkelRRWLRRLHDEL------GGTTVFVTHDQE 195
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-169 |
5.27e-42 |
|
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: 139.32 E-value: 5.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 21 LQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfsHDDTRlsEIRNKKMGFVFQFHHLLAEFTC 100
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDL--TDDER--KSLRKEIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 931484041 101 LENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRL----PLEISGGERQRVAIARAMINDPLIIFADEPT 169
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
7-199 |
1.21e-41 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 144.45 E-value: 1.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 7 VSKTYflenETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfshddTRLS-EIRNkkM 85
Cdd:COG3839 9 VSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV-----TDLPpKDRN--I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 86 GFVFQ----FHHLlaefTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPL 161
Cdd:COG3839 78 AMVFQsyalYPHM----TVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPK 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 931484041 162 IIFADEPTGNLDeentNKLldvFGSLKSE--------GRTIILVTH 199
Cdd:COG3839 154 VFLLDEPLSNLD----AKL---RVEMRAEikrlhrrlGTTTIYVTH 192
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
18-199 |
2.40e-41 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 141.09 E-value: 2.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 18 IEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTR----------LSEIRNKkMGF 87
Cdd:COG4598 21 LEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRDgelvpadrrqLQRIRTR-LGM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 88 VFQFHHLLAEFTCLENVAL-PALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFAD 166
Cdd:COG4598 100 VFQSFNLWSHMTVLENVIEaPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFD 179
|
170 180 190
....*....|....*....|....*....|...
gi 931484041 167 EPTGNLDEENTNKLLDVFGSLKSEGRTIILVTH 199
Cdd:COG4598 180 EPTSALDPELVGEVLKVMRDLAEEGRTMLVVTH 212
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
19-199 |
1.74e-40 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 138.73 E-value: 1.74e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 19 EVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKV-----VFDSVDVFSHDDTRLSEIRnKKMGFVFQFHH 93
Cdd:PRK11264 17 TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTARSLSQQKGLIRQLR-QHVGFVFQNFN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 94 LLAEFTCLENVAL-PALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNL 172
Cdd:PRK11264 96 LFPHRTVLENIIEgPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSAL 175
|
170 180
....*....|....*....|....*..
gi 931484041 173 DEENTNKLLDVFGSLKSEGRTIILVTH 199
Cdd:PRK11264 176 DPELVGEVLNTIRQLAQEKRTMVIVTH 202
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
20-220 |
5.73e-40 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 137.14 E-value: 5.73e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 20 VLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGkvvfdSVDVFSHDDTRlseiRNKKMGFVFQFHHLLAEF- 98
Cdd:COG1121 21 VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSG-----TVRLFGKPPRR----ARRRIGYVPQRAEVDWDFp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 99 -TCLENVALPALVN----GSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLD 173
Cdd:COG1121 92 iTVRDVVLMGRYGRrglfRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVD 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 931484041 174 EENTNKLLDVFGSLKSEGRTIILVTHSVD-ISKFGSHVYKLKeRELHA 220
Cdd:COG1121 172 AATEEALYELLRELRREGKTILVVTHDLGaVREYFDRVLLLN-RGLVA 218
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
20-203 |
9.61e-39 |
|
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: 133.72 E-value: 9.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 20 VLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfshddTRLS--EIRNKKMGFVFQFHHLLAE 97
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDI-----TGLPphEIARLGIGRTFQIPRLFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 98 FTCLENVALPALVNGS----------AQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADE 167
Cdd:cd03219 90 LTVLENVMVAAQARTGsglllararrEEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDE 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 931484041 168 PTGNLDEENTNKLLDVFGSLKSEGRTIILVTHSVDI 203
Cdd:cd03219 170 PAAGLNPEETEELAELIRELRERGITVLLVEHDMDV 205
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
7-215 |
1.16e-38 |
|
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: 131.35 E-value: 1.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 7 VSKTYflENETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfshDDTRLSEIRnKKMG 86
Cdd:cd03228 6 VSFSY--PGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDL---RDLDLESLR-KNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 87 FVFQFHHLLAEfTCLENValpalvngsaqnkayrraqdlldkfdigdkknrlpleISGGERQRVAIARAMINDPLIIFAD 166
Cdd:cd03228 80 YVPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILD 121
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 931484041 167 EPTGNLDEENTNKLLDVFGSLkSEGRTIILVTHSVDISKFGSHVYKLKE 215
Cdd:cd03228 122 EATSALDPETEALILEALRAL-AKGKTVIVIAHRLSTIRDADRIIVLDD 169
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
19-220 |
1.28e-38 |
|
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: 132.66 E-value: 1.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 19 EVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfshddtrlsEIRNKKMGFVFQFHHLLAEF 98
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL---------EKERKRIGYVPQRRSIDRDF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 99 --TCLENVALPAL----VNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNL 172
Cdd:cd03235 84 piSVRDVVLMGLYghkgLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGV 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 931484041 173 DEENTNKLLDVFGSLKSEGRTIILVTHSVD-ISKFGSHVYKLKeRELHA 220
Cdd:cd03235 164 DPKTQEDIYELLRELRREGMTILVVTHDLGlVLEYFDRVLLLN-RTVVA 211
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-204 |
1.42e-38 |
|
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: 135.57 E-value: 1.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSKTYFLENETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRP---TDGKVVFDSVDVFSHDDTRL 77
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 78 SEIRNKKMGFVFQfhhllAEFTCL-------ENVALPALVNGSAQNK-AYRRAQDLLDKFDIGDKKNRL---PLEISGGE 146
Cdd:COG0444 81 RKIRGREIQMIFQ-----DPMTSLnpvmtvgDQIAEPLRIHGGLSKAeARERAIELLERVGLPDPERRLdryPHELSGGM 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 931484041 147 RQRVAIARAMINDPLIIFADEPTGNLDEENTNKLLDVFGSLKSE-GRTIILVTHsvDIS 204
Cdd:COG0444 156 RQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITH--DLG 212
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-202 |
5.23e-38 |
|
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: 129.83 E-value: 5.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 2 LQASTVSKTYflenETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDtrlsEIR 81
Cdd:cd03230 1 IEVRNLSKRY----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPE----EVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 82 nKKMGFVFQFHHLLAEFTCLENvalpalvngsaqnkayrraqdlldkfdigdkknrlpLEISGGERQRVAIARAMINDPL 161
Cdd:cd03230 73 -RRIGYLPEEPSLYENLTVREN------------------------------------LKLSGGMKQRLALAQALLHDPE 115
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 931484041 162 IIFADEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTHSVD 202
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILE 156
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-212 |
5.35e-38 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 132.34 E-value: 5.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 18 IEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSL-----DRPTDGKVVFDSVDVFSHDdtrLSEIRnKKMGFVFQFH 92
Cdd:PRK14247 16 VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMD---VIELR-RRVQMVFQIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 93 HLLAEFTCLENVALPALVNGSAQNKA--YRRAQDLLDKFDIGDK-KNRLPL---EISGGERQRVAIARAMINDPLIIFAD 166
Cdd:PRK14247 92 NPIPNLSIFENVALGLKLNRLVKSKKelQERVRWALEKAQLWDEvKDRLDApagKLSGGQQQRLCIARALAFQPEVLLAD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 931484041 167 EPTGNLDEENTNKLLDVFGSLKSEgRTIILVTH----SVDISKFGSHVYK 212
Cdd:PRK14247 172 EPTANLDPENTAKIESLFLELKKD-MTIVLVTHfpqqAARISDYVAFLYK 220
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-215 |
9.07e-38 |
|
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: 128.90 E-value: 9.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 7 VSKTYflenETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLSeirnKKMG 86
Cdd:cd00267 5 LSFRY----GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELR----RRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 87 FVFQfhhllaeftclenvalpalvngsaqnkayrraqdlldkfdigdkknrlpleISGGERQRVAIARAMINDPLIIFAD 166
Cdd:cd00267 77 YVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 931484041 167 EPTGNLDEENTNKLLDVFGSLKSEGRTIILVTHSVD-ISKFGSHVYKLKE 215
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPElAELAADRVIVLKD 155
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-199 |
1.43e-37 |
|
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: 130.18 E-value: 1.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSKTYFLENETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfsHDDTRlsEI 80
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV--VKEPA--EA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 81 RnKKMGFVFQFHHLLAEFTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDP 160
Cdd:cd03266 77 R-RRLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 931484041 161 LIIFADEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTH 199
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTH 194
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
19-202 |
1.63e-37 |
|
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: 130.18 E-value: 1.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 19 EVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVfdsvdVFSHDDTRLS-EIRnKKMGFVFQFHHLLAE 97
Cdd:cd03265 14 EAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRAT-----VAGHDVVREPrEVR-RRIGIVFQDLSVDDE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 98 FTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLDEENT 177
Cdd:cd03265 88 LTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTR 167
|
170 180
....*....|....*....|....*.
gi 931484041 178 NKLLDVFGSLKSE-GRTIILVTHSVD 202
Cdd:cd03265 168 AHVWEYIEKLKEEfGMTILLTTHYME 193
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-199 |
1.69e-37 |
|
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: 129.68 E-value: 1.69e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 6 TVSKTYFLENETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDdtrlseiRNKKM 85
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE-------RRKSI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 86 GFVFQ--FHHLlaeFTclENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLII 163
Cdd:cd03226 74 GYVMQdvDYQL---FT--DSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190
....*....|....*....|....*....|....*.
gi 931484041 164 FADEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTH 199
Cdd:cd03226 149 IFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITH 184
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
20-215 |
1.89e-37 |
|
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: 130.59 E-value: 1.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 20 VLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGkvvfDSVDVFSHD--DTRLSEIRnKKMGFV-FQFHHLLA 96
Cdd:COG1119 18 ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYG----NDVRLFGERrgGEDVWELR-KRIGLVsPALQLRFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 97 EFTCLENVALPAL--VNGSAQN---KAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGN 171
Cdd:COG1119 93 RDETVLDVVLSGFfdSIGLYREptdEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 931484041 172 LDEENTNKLLDVFGSL-KSEGRTIILVTHSV-DISKFGSHVYKLKE 215
Cdd:COG1119 173 LDLGARELLLALLDKLaAEGAPTLVLVTHHVeEIPPGITHVLLLKD 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-202 |
2.26e-37 |
|
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: 136.19 E-value: 2.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSKTYflENETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPT---DGKVVFDSVDVFSHDDtrl 77
Cdd:COG1123 4 LLEVRDLSVRY--PGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSE--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 78 sEIRNKKMGFVFQ-FHHLLAEFTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAM 156
Cdd:COG1123 79 -ALRGRRIGMVFQdPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 931484041 157 INDPLIIFADEPTGNLDEENTNKLLDVFGSLKSE-GRTIILVTHSVD 202
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLG 204
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
19-220 |
2.40e-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: 128.32 E-value: 2.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 19 EVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDdtrlSEIRNKKMGFVFQfhhllaef 98
Cdd:cd03214 13 TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLS----PKELARKIAYVPQ-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 99 tclenvalpalvngsaqnkayrraqdLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLDEENTN 178
Cdd:cd03214 81 --------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQI 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 931484041 179 KLLDVFGSL-KSEGRTIILVTHSVDI-SKFGSHVYKLKERELHA 220
Cdd:cd03214 135 ELLELLRRLaRERGKTVVMVLHDLNLaARYADRVILLKDGRIVA 178
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
7-199 |
6.17e-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: 128.53 E-value: 6.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 7 VSKTYflenETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfshDDTRLSEiRNKKMg 86
Cdd:cd03301 6 VTKRF----GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV---TDLPPKD-RDIAM- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 87 fVFQFHHLLAEFTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFAD 166
Cdd:cd03301 77 -VFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190
....*....|....*....|....*....|....
gi 931484041 167 EPTGNLDEENTNKLLDVFGSLKSE-GRTIILVTH 199
Cdd:cd03301 156 EPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTH 189
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-219 |
8.79e-37 |
|
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: 128.08 E-value: 8.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 2 LQASTVSKTYflenETIEVLQGVNLLVSKGSFVvILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDtrlsEIR 81
Cdd:cd03264 1 LQLENLTKRY----GKKRALDGVSLTLGPGMYG-LLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQ----KLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 82 nKKMGFVFQFHHLLAEFTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPL 161
Cdd:cd03264 72 -RRIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 931484041 162 IIFADEPTGNLDEENTNKLLDVFGSLkSEGRTIILVTHSV-DISKFGSHVYKLKERELH 219
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSEL-GEDRIVILSTHIVeDVESLCNQVAVLNKGKLV 208
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-199 |
9.26e-37 |
|
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: 127.60 E-value: 9.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSKTYfleNETIeVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLSEI 80
Cdd:COG4133 2 MLEAENLSCRR---GERL-LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 81 rnkkmGFVFQFHHLLAEFTCLENVALPALVNGSAQNKAyrRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDP 160
Cdd:COG4133 78 -----AYLGHADGLKPELTVRENLRFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPA 150
|
170 180 190
....*....|....*....|....*....|....*....
gi 931484041 161 LIIFADEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTH 199
Cdd:COG4133 151 PLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-203 |
2.15e-36 |
|
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: 128.23 E-value: 2.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSKTYflenETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfshddTRLS-- 78
Cdd:COG0411 4 LLEVRGLTKRF----GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDI-----TGLPph 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 79 EIRNKKMGFVFQFHHLLAEFTCLENVALPALVNGSA---------------QNKAYRRAQDLLDKFDIGDKKNRLPLEIS 143
Cdd:COG0411 75 RIARLGIARTFQNPRLFPELTVLENVLVAAHARLGRgllaallrlprarreEREARERAEELLERVGLADRADEPAGNLS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 931484041 144 GGERQRVAIARAMINDPLIIFADEPTGNLDEENTNKLLDVFGSLKSE-GRTIILVTHSVDI 203
Cdd:COG0411 155 YGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDL 215
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
21-199 |
8.53e-36 |
|
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: 126.30 E-value: 8.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 21 LQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDdtrlseIRNKKMGFVFQFHHLLAEFTC 100
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP------VQERNVGFVFQHYALFRHMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 101 LENVAL-----PALVNGSAQNKAyRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLDEE 175
Cdd:cd03296 92 FDNVAFglrvkPRSERPPEAEIR-AKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAK 170
|
170 180
....*....|....*....|....*
gi 931484041 176 NTNKLLDVFGSLKSE-GRTIILVTH 199
Cdd:cd03296 171 VRKELRRWLRRLHDElHVTTVFVTH 195
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
7-199 |
1.73e-35 |
|
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: 125.04 E-value: 1.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 7 VSKTYflenETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfshddTRLSeIRNKKMG 86
Cdd:cd03300 6 VSKFY----GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI-----TNLP-PHKRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 87 FVFQFHHLLAEFTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFAD 166
Cdd:cd03300 76 TVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190
....*....|....*....|....*....|....
gi 931484041 167 EPTGNLDEENTNKLLDVFGSLKSE-GRTIILVTH 199
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLQKElGITFVFVTH 189
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
27-202 |
2.65e-35 |
|
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: 124.33 E-value: 2.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 27 LVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFshdDTRLSEI---RNKKMGFVFQFHHLLAEFTCLEN 103
Cdd:cd03297 19 FDLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLF---DSRKKINlppQQRKIGLVFQQYALFPHLNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 104 VALPALVNGSAQNKAyrRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLDEENTNKLLDV 183
Cdd:cd03297 96 LAFGLKRKRNREDRI--SVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPE 173
|
170 180
....*....|....*....|
gi 931484041 184 FGSLKSE-GRTIILVTHSVD 202
Cdd:cd03297 174 LKQIKKNlNIPVIFVTHDLS 193
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-202 |
4.40e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 125.97 E-value: 4.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 2 LQASTVSKTYFLENET-IEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVF-----------DSVDV 69
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTeLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeknkkktKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 70 FSHDD----TRLSEIRN-----KKMGFVFQF-HHLLAEFTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKK-NRL 138
Cdd:PRK13651 83 VLEKLviqkTRFKKIKKikeirRRVGVVFQFaEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESYlQRS 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 931484041 139 PLEISGGERQRVAIARAMINDPLIIFADEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTHSVD 202
Cdd:PRK13651 163 PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLD 226
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
25-210 |
1.13e-34 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 122.94 E-value: 1.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 25 NLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDvfsHDDTRLSEiRNKKMgfVFQ----FHHLlaefTC 100
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQD---LTALPPAE-RPVSM--LFQennlFPHL----TV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 101 LENVAL---PALvNGSAQNKAyrRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLD---- 173
Cdd:COG3840 89 AQNIGLglrPGL-KLTAEQRA--QVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDpalr 165
|
170 180 190
....*....|....*....|....*....|....*....
gi 931484041 174 EEntnkLLDVFGSLKSE-GRTIILVTHSV-DISKFGSHV 210
Cdd:COG3840 166 QE----MLDLVDELCRErGLTVLMVTHDPeDAARIADRV 200
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
19-210 |
2.30e-34 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 123.16 E-value: 2.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 19 EVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDS------------VDVFSHDDTRLSEIRnkkMG 86
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdkdgqLKVADKNQLRLLRTR---LT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 87 FVFQFHHLLAEFTCLENV-ALPALVNGSAQNKAYRRAQDLLDKFDIGDK-KNRLPLEISGGERQRVAIARAMINDPLIIF 164
Cdd:PRK10619 96 MVFQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERaQGKYPVHLSGGQQQRVSIARALAMEPEVLL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 931484041 165 ADEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTHSVDISK-FGSHV 210
Cdd:PRK10619 176 FDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARhVSSHV 222
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
7-199 |
2.66e-34 |
|
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: 128.80 E-value: 2.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 7 VSKTYflENETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfshDDTRLSEIRNkKMG 86
Cdd:COG2274 479 VSFRY--PGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDL---RQIDPASLRR-QIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 87 FVFQFHHLLAEfTCLENValpALVNGSAQNKAYRRAqdlLDKFDIGDKKNRLPL-----------EISGGERQRVAIARA 155
Cdd:COG2274 553 VVLQDVFLFSG-TIRENI---TLGDPDATDEEIIEA---ARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIARA 625
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 931484041 156 MINDPLIIFADEPTGNLDEENTNKLLDVFGSLKsEGRTIILVTH 199
Cdd:COG2274 626 LLRNPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAH 668
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-202 |
2.83e-34 |
|
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: 121.84 E-value: 2.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 2 LQASTVSKTYflENETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGkvvfdSVDVFSHDDTRLSEIR 81
Cdd:cd03263 1 LQIRNLTKTY--KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSG-----TAYINGYSIRTDRKAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 82 NKKMGFVFQFHHLLAEFTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPL 161
Cdd:cd03263 74 RQSLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPS 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 931484041 162 IIFADEPTGNLDEENTNKLLDVFGSLKSeGRTIILVTHSVD 202
Cdd:cd03263 154 VLLLDEPTSGLDPASRRAIWDLILEVRK-GRSIILTTHSMD 193
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
7-199 |
5.03e-34 |
|
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: 122.15 E-value: 5.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 7 VSKTYflENETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFshDDTRLSEIRnKKMG 86
Cdd:TIGR04520 6 VSFSY--PESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTL--DEENLWEIR-KKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 87 FVF-----QFHHLLAE----FTcLENVALPalvngsaQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMI 157
Cdd:TIGR04520 81 MVFqnpdnQFVGATVEddvaFG-LENLGVP-------REEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 931484041 158 NDPLIIFADEPTGNLDEENTNKLLDVFGSLKSE-GRTIILVTH 199
Cdd:TIGR04520 153 MRPDIIILDEATSMLDPKGRKEVLETIRKLNKEeGITVISITH 195
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-199 |
1.01e-33 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 118.86 E-value: 1.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 2 LQASTVSKTYflENETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDdtrLSEIR 81
Cdd:cd03246 1 LEVENVSFRY--PGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWD---PNELG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 82 nKKMGFVFQFHHLLAEfTCLENValpalvngsaqnkayrraqdlldkfdigdkknrlpleISGGERQRVAIARAMINDPL 161
Cdd:cd03246 76 -DHVGYLPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPR 116
|
170 180 190
....*....|....*....|....*....|....*...
gi 931484041 162 IIFADEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTH 199
Cdd:cd03246 117 ILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAH 154
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
21-218 |
2.09e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 121.00 E-value: 2.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 21 LQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTR-LSEIRnKKMGFVFQF--HHLLAE 97
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdIKQIR-KKVGLVFQFpeSQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 98 fTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDK-KNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLDEEN 176
Cdd:PRK13649 102 -TVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESlFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 931484041 177 TNKLLDVFGSLKSEGRTIILVTHSV-DISKFGSHVYKLKEREL 218
Cdd:PRK13649 181 RKELMTLFKKLHQSGMTIVLVTHLMdDVANYADFVYVLEKGKL 223
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-218 |
2.26e-33 |
|
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: 125.64 E-value: 2.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 2 LQASTVSKTYfleNETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDV--FSHDDTRlse 79
Cdd:COG4988 337 IELEDVSFSY---PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLsdLDPASWR--- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 80 irnKKMGFVFQFHHLLAEfTCLENVALPALVNGSAQ-NKAYRRAQ------DLLDKFD--IGDKKNRLpleiSGGERQRV 150
Cdd:COG4988 411 ---RQIAWVPQNPYLFAG-TIRENLRLGRPDASDEElEAALEAAGldefvaALPDGLDtpLGEGGRGL----SGGQAQRL 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 931484041 151 AIARAMINDPLIIFADEPTGNLDEENTNKLLDVFGSLkSEGRTIILVTHSVDISKFGSHVYKLKEREL 218
Cdd:COG4988 483 ALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILITHRLALLAQADRILVLDDGRI 549
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
26-205 |
2.29e-33 |
|
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: 119.13 E-value: 2.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 26 LLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFShddtrlSEIRNKKMGFVFQFHHLLAEFTCLENVA 105
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTA------APPADRPVSMLFQENNLFAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 106 LpALVNGSAQNKAYRRAQD-LLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLDEENTNKLLD-V 183
Cdd:cd03298 93 L-GLSPGLKLTAEDRQAIEvALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDlV 171
|
170 180
....*....|....*....|..
gi 931484041 184 FGSLKSEGRTIILVTHSVDISK 205
Cdd:cd03298 172 LDLHAETKMTVLMVTHQPEDAK 193
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-199 |
8.35e-33 |
|
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: 124.11 E-value: 8.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 2 LQASTVSKTYflENETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLSEir 81
Cdd:COG4987 334 LELEDVSFRY--PGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRR-- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 82 nkKMGFVFQFHHLLAEfTCLENValpALVNGSAQNKAYRRAqdlLDKFDIGDKKNRLP--LE---------ISGGERQRV 150
Cdd:COG4987 410 --RIAVVPQRPHLFDT-TLRENL---RLARPDATDEELWAA---LERVGLGDWLAALPdgLDtwlgeggrrLSGGERRRL 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 931484041 151 AIARAMINDPLIIFADEPTGNLDEENTNKLL-DVFGSLKseGRTIILVTH 199
Cdd:COG4987 481 ALARALLRDAPILLLDEPTEGLDAATEQALLaDLLEALA--GRTVLLITH 528
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
21-202 |
8.79e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 119.74 E-value: 8.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 21 LQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKV-VFDSVDVFSHDDTRLSEIRnKKMGFVFQF-HHLLAEF 98
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVtIGERVITAGKKNKKLKPLR-KKVGIVFQFpEHQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 99 TCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDK-KNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLDEENT 177
Cdd:PRK13634 102 TVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEElLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGR 181
|
170 180
....*....|....*....|....*.
gi 931484041 178 NKLLDVFGSLKSE-GRTIILVTHSVD 202
Cdd:PRK13634 182 KEMMEMFYKLHKEkGLTTVLVTHSME 207
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
18-211 |
1.40e-32 |
|
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: 117.15 E-value: 1.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 18 IEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfshddTRLS--EIRNKKMGFVFQFHHLL 95
Cdd:cd03224 13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDI-----TGLPphERARAGIGYVPEGRRIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 96 AEFTCLENVALPALVNGSAQNKayRRAQDLLDKFDI-GDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNL-- 172
Cdd:cd03224 88 PELTVEENLLLGAYARRRAKRK--ARLERVYELFPRlKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLap 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 931484041 173 ---DEentnkLLDVFGSLKSEGRTIILVTHSVDIS-KFGSHVY 211
Cdd:cd03224 166 kivEE-----IFEAIRELRDEGVTILLVEQNARFAlEIADRAY 203
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
19-199 |
3.53e-32 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 119.42 E-value: 3.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 19 EVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfshddTRLSEiRNKKMGFVFQFHHLLAEF 98
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV-----SRLHA-RDRKVGFVFQHYALFRHM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 99 TCLENVA--LPALVNGSAQNKAY--RRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLDE 174
Cdd:PRK10851 90 TVFDNIAfgLTVLPRRERPNAAAikAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDA 169
|
170 180
....*....|....*....|....*.
gi 931484041 175 ENTNKLLDVFGSLKSEGR-TIILVTH 199
Cdd:PRK10851 170 QVRKELRRWLRQLHEELKfTSVFVTH 195
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-199 |
1.05e-31 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 120.51 E-value: 1.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSKTYFleneTIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfSHDDTRlsEI 80
Cdd:COG1129 4 LLEMRGISKSFG----GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPV-RFRSPR--DA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 81 RNKKMGFVFQFHHLLAEFTCLENVAL------PALVNgsaQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIAR 154
Cdd:COG1129 77 QAAGIAIIHQELNLVPNLSVAENIFLgreprrGGLID---WRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIAR 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 931484041 155 AMINDP-LIIFaDEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTH 199
Cdd:COG1129 154 ALSRDArVLIL-DEPTASLTEREVERLFRIIRRLKAQGVAIIYISH 198
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
7-199 |
1.46e-31 |
|
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: 114.61 E-value: 1.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 7 VSKTYflENETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDdtrLSEIRnKKMG 86
Cdd:cd03245 8 VSFSY--PNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLD---PADLR-RNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 87 FVFQFHHLLAEfTCLENVALPALvngSAQNKAYRRAQDL--LDKFdIGDKKNRLPLEI-------SGGERQRVAIARAMI 157
Cdd:cd03245 82 YVPQDVTLFYG-TLRDNITLGAP---LADDERILRAAELagVTDF-VNKHPNGLDLQIgergrglSGGQRQAVALARALL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 931484041 158 NDPLIIFADEPTGNLDEENTNKLLDVFGSLKSeGRTIILVTH 199
Cdd:cd03245 157 NDPPILLLDEPTSAMDMNSEERLKERLRQLLG-DKTLIIITH 197
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
19-199 |
2.05e-31 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 120.27 E-value: 2.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 19 EVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfshDDTRLSEIRnKKMGFVFQFHHLLAEf 98
Cdd:COG1132 354 PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDI---RDLTLESLR-RQIGVVPQDTFLFSG- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 99 TCLENVALpalvnGSAQ------NKAYRRAQ------DLLDKFD--IGDKKNRLpleiSGGERQRVAIARAMINDPLIIF 164
Cdd:COG1132 429 TIRENIRY-----GRPDatdeevEEAAKAAQahefieALPDGYDtvVGERGVNL----SGGQRQRIAIARALLKDPPILI 499
|
170 180 190
....*....|....*....|....*....|....*
gi 931484041 165 ADEPTGNLDEENTNKLLDVFGSLkSEGRTIILVTH 199
Cdd:COG1132 500 LDEATSALDTETEALIQEALERL-MKGRTTIVIAH 533
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
21-218 |
2.44e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 115.70 E-value: 2.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 21 LQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTR-LSEIRnKKMGFVFQFHHL-LAEF 98
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnLKKLR-KKVSLVFQFPEAqLFEN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 99 TCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDK-KNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLDEENT 177
Cdd:PRK13641 102 TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 931484041 178 NKLLDVFGSLKSEGRTIILVTHSV-DISKFGSHVYKLKEREL 218
Cdd:PRK13641 182 KEMMQLFKDYQKAGHTVILVTHNMdDVAEYADDVLVLEHGKL 223
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-206 |
2.95e-31 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 114.80 E-value: 2.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSKTYflenETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRlsei 80
Cdd:PRK11248 1 MLQISHLYADY----GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 81 rnkkmGFVFQFHHLLAEFTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDP 160
Cdd:PRK11248 73 -----GVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANP 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 931484041 161 LIIFADEPTGNLD----EENTNKLLDVFgslKSEGRTIILVTHSVDISKF 206
Cdd:PRK11248 148 QLLLLDEPFGALDaftrEQMQTLLLKLW---QETGKQVLLITHDIEEAVF 194
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-218 |
3.15e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 115.17 E-value: 3.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSKTYfleNETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfSHDDTRLSEI 80
Cdd:PRK13639 1 ILETRDLKYSY---PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 81 RnKKMGFVFQF--HHLLAEfTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMIN 158
Cdd:PRK13639 77 R-KTVGIVFQNpdDQLFAP-TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 931484041 159 DPLIIFADEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTHSVD-ISKFGSHVYKLKEREL 218
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDlVPVYADKVYVMSDGKI 215
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
20-202 |
3.42e-31 |
|
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: 113.97 E-value: 3.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 20 VLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfshddTRLS-EIRNKkmGFVFQFHHLLAEF 98
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI-----TNLPpEKRDI--SYVPQNYALFPHM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 99 TCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLDEENTN 178
Cdd:cd03299 87 TVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKE 166
|
170 180
....*....|....*....|....*
gi 931484041 179 KLLDVFGSLKSE-GRTIILVTHSVD 202
Cdd:cd03299 167 KLREELKKIRKEfGVTVLHVTHDFE 191
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
6-208 |
3.76e-31 |
|
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: 113.03 E-value: 3.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 6 TVSKTYFLENETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSS-LDRPTD-GKVVFDSVDVfshddtRLSEIRnK 83
Cdd:cd03213 10 TVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrRTGLGVsGEVLINGRPL------DKRSFR-K 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 84 KMGFVFQFHHLLAEFTCLENVALPALVNGsaqnkayrraqdlldkfdigdkknrlpleISGGERQRVAIARAMINDPLII 163
Cdd:cd03213 83 IIGYVPQDDILHPTLTVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLL 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 931484041 164 FADEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTHSVDISKFGS 208
Cdd:cd03213 134 FLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFEL 178
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-200 |
7.84e-31 |
|
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: 118.16 E-value: 7.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 2 LQASTVSKTYfleNETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDV--FSHDDTRlse 79
Cdd:TIGR02857 322 LEFSGVSVAY---PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLadADADSWR--- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 80 irnKKMGFVFQFHHLLAEfTCLENVAL------PALVNGSAQNK-AYRRAQDLLDKFD--IGDKKNRLpleiSGGERQRV 150
Cdd:TIGR02857 396 ---DQIAWVPQHPFLFAG-TIAENIRLarpdasDAEIREALERAgLDEFVAALPQGLDtpIGEGGAGL----SGGQAQRL 467
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 931484041 151 AIARAMINDPLIIFADEPTGNLDEENTNKLLDVFGSLkSEGRTIILVTHS 200
Cdd:TIGR02857 468 ALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHR 516
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-200 |
1.78e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 112.63 E-value: 1.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 19 EVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSL-----DRPTDGKVVFDSVDVFSHDDTRLsEIRnKKMGFVFQFHH 93
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVDPI-EVR-REVGMVFQYPN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 94 LLAEFTCLENVALPALVNGSAQNKAY--RRAQDLLDKFDIGDK-KNRL---PLEISGGERQRVAIARAMINDPLIIFADE 167
Cdd:PRK14267 96 PFPHLTIYDNVAIGVKLNGLVKSKKEldERVEWALKKAALWDEvKDRLndyPSNLSGGQRQRLVIARALAMKPKILLMDE 175
|
170 180 190
....*....|....*....|....*....|...
gi 931484041 168 PTGNLDEENTNKLLDVFGSLKSEgRTIILVTHS 200
Cdd:PRK14267 176 PTANIDPVGTAKIEELLFELKKE-YTIVLVTHS 207
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-202 |
2.07e-30 |
|
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: 112.17 E-value: 2.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 21 LQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLseirnkkmgFVFQFHHLLAEFTC 100
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM---------VVFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 101 LENVALPALVNGSAQNKAYRRA--QDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLDEENTN 178
Cdd:TIGR01184 72 RENIALAVDRVLPDLSKSERRAivEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180
....*....|....*....|....*
gi 931484041 179 KLLDVFGSLKSEGR-TIILVTHSVD 202
Cdd:TIGR01184 152 NLQEELMQIWEEHRvTVLMVTHDVD 176
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
21-206 |
3.45e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 112.83 E-value: 3.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 21 LQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfSHDDTRLSEIRnKKMGFVFQF-HHLLAEFT 99
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDI-TDKKVKLSDIR-KKVGLVFQYpEYQLFEET 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 100 CLENVALPALVNGSAQNKAYRRAQDLLD--KFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLDEENT 177
Cdd:PRK13637 101 IEKDIAFGPINLGLSEEEIENRVKRAMNivGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGR 180
|
170 180 190
....*....|....*....|....*....|.
gi 931484041 178 NKLLDVFGSLKSE-GRTIILVTHSV-DISKF 206
Cdd:PRK13637 181 DEILNKIKELHKEyNMTIILVSHSMeDVAKL 211
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
36-199 |
2.28e-29 |
|
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: 111.43 E-value: 2.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 36 ILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfshddtRLSEIRNKKMGFVFQFHHLLAEFTCLENVALPALVNGSAQ 115
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDV------TNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 116 NKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLD----EENTNKLLDVFGSLkseG 191
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDkklrDQMQLELKTIQEQL---G 151
|
....*...
gi 931484041 192 RTIILVTH 199
Cdd:TIGR01187 152 ITFVFVTH 159
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
25-201 |
2.81e-29 |
|
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: 108.80 E-value: 2.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 25 NLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfshddTRLSEIRnKKMGFVFQFHHLLAEFTCLENV 104
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSH-----TGLAPYQ-RPVSMLFQENNLFAHLTVRQNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 105 AL---PAL-VNGSAQNKAYRRAQDLldkfDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLDEENTNKL 180
Cdd:TIGR01277 92 GLglhPGLkLNAEQQEKVVDAAQQV----GIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEM 167
|
170 180
....*....|....*....|..
gi 931484041 181 LDVFGSLKSE-GRTIILVTHSV 201
Cdd:TIGR01277 168 LALVKQLCSErQRTLLMVTHHL 189
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
7-201 |
3.69e-29 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 109.38 E-value: 3.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 7 VSKTYflenETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFS-HDDTRLseirnkkm 85
Cdd:PRK11247 18 VSKRY----GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEaREDTRL-------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 86 gfVFQFHHLLAEFTCLENVALPalVNGSAQNKAyRRAqdlLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFA 165
Cdd:PRK11247 86 --MFQDARLLPWKKVIDNVGLG--LKGQWRDAA-LQA---LAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLL 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 931484041 166 DEPTGNLDEENTNKLLDVFGSLKSE-GRTIILVTHSV 201
Cdd:PRK11247 158 DEPLGALDALTRIEMQDLIESLWQQhGFTVLLVTHDV 194
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
24-215 |
4.59e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 109.82 E-value: 4.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 24 VNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLSEIRNKKMGFVFQF-HHLLAEFTCLE 102
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQFpESQLFEETVLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 103 NVALPALVNGSAQNKAYRRAQDLLDKFDIGDK-KNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLDEENTNKLL 181
Cdd:PRK13643 105 DVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEfWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMM 184
|
170 180 190
....*....|....*....|....*....|....*
gi 931484041 182 DVFGSLKSEGRTIILVTHSV-DISKFGSHVYKLKE 215
Cdd:PRK13643 185 QLFESIHQSGQTVVLVTHLMdDVADYADYVYLLEK 219
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-199 |
7.45e-29 |
|
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: 107.30 E-value: 7.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 2 LQASTVSKTYflenETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfshddTRLSEIR 81
Cdd:cd03268 1 LKTNDLTKTY----GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY-----QKNIEAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 82 NkKMGFVFQFHHLLAEFTCLENVALPALVNGsaqnKAYRRAQDLLDKF---DIGDKKNRLpleISGGERQRVAIARAMIN 158
Cdd:cd03268 72 R-RIGALIEAPGFYPNLTARENLRLLARLLG----IRKKRIDEVLDVVglkDSAKKKVKG---FSLGMKQRLGIALALLG 143
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 931484041 159 DPLIIFADEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTH 199
Cdd:cd03268 144 NPDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSH 184
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
20-199 |
1.40e-28 |
|
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: 112.15 E-value: 1.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 20 VLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLSEIrnkkMGFvfqfhhllaeft 99
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRH----IGY------------ 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 100 clenvaLP---ALVNGS-AQN-------------KAYRRAQ--DLLDKF------DIGDKKNRLpleiSGGERQRVAIAR 154
Cdd:COG4618 411 ------LPqdvELFDGTiAENiarfgdadpekvvAAAKLAGvhEMILRLpdgydtRIGEGGARL----SGGQRQRIGLAR 480
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 931484041 155 AMINDPLIIFADEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTH 199
Cdd:COG4618 481 ALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITH 525
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
19-200 |
2.01e-28 |
|
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: 111.68 E-value: 2.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 19 EVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLSeirnKKMGFVFQFHHLLAEf 98
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVR----RRVSVCAQDAHLFDT- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 99 TCLENVALPAL-VNGSAQNKAYRRAQ--DLLDKF------DIGDKKNRLpleiSGGERQRVAIARAMINDPLIIFADEPT 169
Cdd:TIGR02868 424 TVRENLRLARPdATDEELWAALERVGlaDWLRALpdgldtVLGEGGARL----SGGERQRLALARALLADAPILLLDEPT 499
|
170 180 190
....*....|....*....|....*....|..
gi 931484041 170 GNLDEENTNKLL-DVFGSLksEGRTIILVTHS 200
Cdd:TIGR02868 500 EHLDAETADELLeDLLAAL--SGRTVVLITHH 529
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
7-202 |
2.06e-28 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 110.12 E-value: 2.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 7 VSKTYFLENETIEV-LQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLSEIRNKKM 85
Cdd:PRK10070 29 LSKEQILEKTGLSLgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 86 GFVFQFHHLLAEFTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFA 165
Cdd:PRK10070 109 AMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLM 188
|
170 180 190
....*....|....*....|....*....|....*...
gi 931484041 166 DEPTGNLDEENTNKLLDVFGSLKSE-GRTIILVTHSVD 202
Cdd:PRK10070 189 DEAFSALDPLIRTEMQDELVKLQAKhQRTIVFISHDLD 226
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
11-199 |
2.54e-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: 106.55 E-value: 2.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 11 YFLENETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfshDDTRLSEIRnKKMGFVFQ 90
Cdd:cd03253 7 TFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDI---REVTLDSLR-RAIGVVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 91 FHHLLAEfTCLENVALPalvNGSAQNKAYRRAQDlldKFDIGDKKNRLP-----------LEISGGERQRVAIARAMIND 159
Cdd:cd03253 83 DTVLFND-TIGYNIRYG---RPDATDEEVIEAAK---AAQIHDKIMRFPdgydtivgergLKLSGGEKQRVAIARAILKN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 931484041 160 PLIIFADEPTGNLDEENTNKLLDVFGSLkSEGRTIILVTH 199
Cdd:cd03253 156 PPILLLDEATSALDTHTEREIQAALRDV-SKGRTTIVIAH 194
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-202 |
3.15e-28 |
|
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: 104.43 E-value: 3.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 2 LQASTVSKTYflenETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDtrlSEIR 81
Cdd:cd03216 1 LELRGITKRF----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASP---RDAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 82 NKKMGFVFQfhhllaeftclenvalpalvngsaqnkayrraqdlldkfdigdkknrlpleISGGERQRVAIARAMINDPL 161
Cdd:cd03216 74 RAGIAMVYQ---------------------------------------------------LSVGERQMVEIARALARNAR 102
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 931484041 162 IIFADEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTHSVD 202
Cdd:cd03216 103 LLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLD 143
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-202 |
3.98e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 107.10 E-value: 3.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSKTYFLENETIE--VLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDvfSHDDTRLS 78
Cdd:PRK13633 4 MIKCKNVSYKYESNEESTEklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLD--TSDEENLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 79 EIRNKKmGFVFQF--HHLLAEFTcLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAM 156
Cdd:PRK13633 82 DIRNKA-GMVFQNpdNQIVATIV-EEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGIL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 931484041 157 INDPLIIFADEPTGNLDEENTNKLLDVFGSL-KSEGRTIILVTHSVD 202
Cdd:PRK13633 160 AMRPECIIFDEPTAMLDPSGRREVVNTIKELnKKYGITIILITHYME 206
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-220 |
8.06e-28 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 105.97 E-value: 8.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSktYFLENETIevLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLSEI 80
Cdd:COG4559 1 MLEAENLS--VRLGGRTL--LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 81 RnkkmGFVFQFHHLLAEFTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMI--- 157
Cdd:COG4559 77 R----AVLPQHSSLAFPFTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlw 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 158 ----NDPLIIFADEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTHsvDI---SKFGSHVYKLKERELHA 220
Cdd:COG4559 153 epvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLH--DLnlaAQYADRILLLHQGRLVA 220
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
7-199 |
8.66e-28 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 105.39 E-value: 8.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 7 VSKTYflENETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfshDDTRLSEIRnKKMG 86
Cdd:cd03251 6 VTFRY--PGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDV---RDYTLASLR-RQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 87 FVFQFHHLLAEfTCLENVAL------PALVNGSAQNkAYrrAQDLLDKFD------IGDKKNRLpleiSGGERQRVAIAR 154
Cdd:cd03251 80 LVSQDVFLFND-TVAENIAYgrpgatREEVEEAARA-AN--AHEFIMELPegydtvIGERGVKL----SGGQRQRIAIAR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 931484041 155 AMINDPLIIFADEPTGNLDEENTNKLLDVFGSLkSEGRTIILVTH 199
Cdd:cd03251 152 ALLKDPPILILDEATSALDTESERLVQAALERL-MKNRTTFVIAH 195
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
19-200 |
1.03e-27 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 105.50 E-value: 1.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 19 EVLQGVNLLVSKGSFVVILGPSGSGKSTLLnilSSLDRPTD--------GKVVFDSVDVFShDDTRLSEIRnKKMGFVFQ 90
Cdd:COG1117 25 QALKDINLDIPENKVTALIGPSGCGKSTLL---RCLNRMNDlipgarveGEILLDGEDIYD-PDVDVVELR-RRVGMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 91 ----FHHllaefTCLENVALPALVNGSAQN--------KAYRRAqDLLDkfDIGDKKNRLPLEISGGERQRVAIARAMIN 158
Cdd:COG1117 100 kpnpFPK-----SIYDNVAYGLRLHGIKSKseldeiveESLRKA-ALWD--EVKDRLKKSALGLSGGQQQRLCIARALAV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 931484041 159 DPLIIFADEPTGNLDEENTNKLLDVFGSLKSEgRTIILVTHS 200
Cdd:COG1117 172 EPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHN 212
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
12-199 |
1.95e-27 |
|
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: 104.23 E-value: 1.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 12 FLENETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfshDDTRLSEIRNkKMGFVFQF 91
Cdd:cd03254 10 FSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDI---RDISRKSLRS-MIGVVLQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 92 HHLLAEfTCLENVALPALVNGSAQ-NKAYRRAQ--DLLDKF------DIGDKKNRLpleiSGGERQRVAIARAMINDPLI 162
Cdd:cd03254 86 TFLFSG-TIMENIRLGRPNATDEEvIEAAKEAGahDFIMKLpngydtVLGENGGNL----SQGERQLLAIARAMLRDPKI 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 931484041 163 IFADEPTGNLDEENTNKLLDVFGSLKsEGRTIILVTH 199
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLM-KGRTSIIIAH 196
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
24-202 |
2.41e-27 |
|
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: 106.72 E-value: 2.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 24 VNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSvDVFSHDDTRLS---EIRNkkMGFVFQFHHLLAEFTC 100
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGG-EVLQDSARGIFlppHRRR--IGYVFQEARLFPHLSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 101 LENVALpALVNGSAQNKAYRRAQ--DLLDkfdIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLDEENTN 178
Cdd:COG4148 95 RGNLLY-GRKRAPRAERRISFDEvvELLG---IGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKA 170
|
170 180
....*....|....*....|....*
gi 931484041 179 KLLDVFGSLKSEGRT-IILVTHSVD 202
Cdd:COG4148 171 EILPYLERLRDELDIpILYVSHSLD 195
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-202 |
2.51e-27 |
|
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: 103.51 E-value: 2.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 2 LQASTVSKTYflenETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDsvdvfshdDTRLSEIR 81
Cdd:cd03269 1 LEVENVTKRF----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFD--------GKPLDIAA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 82 NKKMGFVFQFHHLLAEFTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPL 161
Cdd:cd03269 69 RNRIGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 931484041 162 IIFADEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTHSVD 202
Cdd:cd03269 149 LLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQME 189
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
18-197 |
3.11e-27 |
|
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: 103.91 E-value: 3.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 18 IEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfshddTRLS--EIRNKKMGFVFQFHHLL 95
Cdd:COG0410 16 IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDI-----TGLPphRIARLGIGYVPEGRRIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 96 AEFTCLENVALPALVNGSAQNKAyRRAQDLLDKF-DIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNL-- 172
Cdd:COG0410 91 PSLTVEENLLLGAYARRDRAEVR-ADLERVYELFpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLap 169
|
170 180
....*....|....*....|....*...
gi 931484041 173 ---DEentnkLLDVFGSLKSEGRTIILV 197
Cdd:COG0410 170 livEE-----IFEIIRRLNREGVTILLV 192
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
21-173 |
3.16e-27 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 105.97 E-value: 3.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 21 LQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLSEIRnKKMGFVFQ--FHHLLAEF 98
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLR-RRMQMVFQdpYASLNPRM 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 931484041 99 TCLENVALPALVNGSAQNKAYR-RAQDLLDKfdIG---DKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLD 173
Cdd:COG4608 113 TVGDIIAEPLRIHGLASKAERReRVAELLEL--VGlrpEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
13-202 |
5.35e-27 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 102.56 E-value: 5.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 13 LENETI-----EVLQGVNLLVSKGSFVVILGPSGSGKSTLLN-ILSSLDRP--TDGKVVFDSVDVfshddTRLSeIRNKK 84
Cdd:COG4136 4 LENLTItlggrPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAaIAGTLSPAfsASGEVLLNGRRL-----TALP-AEQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 85 MGFVFQFHHLLAEFTCLENV--ALPALVNGSAQNkayRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLI 162
Cdd:COG4136 78 IGILFQDDLLFPHLSVGENLafALPPTIGRAQRR---ARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 931484041 163 IFADEPTGNLDEENTNKLLD-VFGSLKSEGRTIILVTHSVD 202
Cdd:COG4136 155 LLLDEPFSKLDAALRAQFREfVFEQIRQRGIPALLVTHDEE 195
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
21-215 |
8.53e-27 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 106.65 E-value: 8.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 21 LQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfshddtrlsEIRNKKM------GFVFQfHHL 94
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV---------RIRSPRDaialgiGMVHQ-HFM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 95 LAE-FTCLENVAL---PALVNGSAQNKAYRRAQDLLDKFDigdkknrLPL-------EISGGERQRVAIARAMINDP-LI 162
Cdd:COG3845 91 LVPnLTVAENIVLglePTKGGRLDRKAARARIRELSERYG-------LDVdpdakveDLSVGEQQRVEILKALYRGArIL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 931484041 163 IFaDEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTHsvdiskfgshvyKLKE 215
Cdd:COG3845 164 IL-DEPTAVLTPQEADELFEILRRLAAEGKSIIFITH------------KLRE 203
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
24-199 |
9.21e-27 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 105.30 E-value: 9.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 24 VNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfSHDDTRLSEIrnkkmGFVFQFHHLLAEFTCLEN 103
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL-SHVPPYQRPI-----NMMFQSYALFPHMTVEQN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 104 VALpalvnGSAQNKAYR-----RAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLDEENTN 178
Cdd:PRK11607 112 IAF-----GLKQDKLPKaeiasRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRD 186
|
170 180
....*....|....*....|..
gi 931484041 179 KL-LDVFGSLKSEGRTIILVTH 199
Cdd:PRK11607 187 RMqLEVVDILERVGVTCVMVTH 208
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
18-199 |
1.41e-26 |
|
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: 106.72 E-value: 1.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 18 IEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfshDDTRLSEIRNKkMGFVFQFHHLLAE 97
Cdd:TIGR02203 345 RPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDL---ADYTLASLRRQ-VALVSQDVVLFND 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 98 fTCLENVALPALVNG------SAQNKAYrrAQDLLDK------FDIGDKKNRLpleiSGGERQRVAIARAMINDPLIIFA 165
Cdd:TIGR02203 421 -TIANNIAYGRTEQAdraeieRALAAAY--AQDFVDKlplgldTPIGENGVLL----SGGQRQRLAIARALLKDAPILIL 493
|
170 180 190
....*....|....*....|....*....|....
gi 931484041 166 DEPTGNLDEENTNKLLDVFGSLKsEGRTIILVTH 199
Cdd:TIGR02203 494 DEATSALDNESERLVQAALERLM-QGRTTLVIAH 526
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
20-199 |
1.88e-26 |
|
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: 106.28 E-value: 1.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 20 VLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLSeirnKKMGFVFQ----FHHLL 95
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFG----KHIGYLPQdvelFPGTV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 96 AEFTCL--ENVALPALVNGSAQNKAYRRAQDLLDKFD--IGDKKNRLpleiSGGERQRVAIARAMINDPLIIFADEPTGN 171
Cdd:TIGR01842 409 AENIARfgENADPEKIIEAAKLAGVHELILRLPDGYDtvIGPGGATL----SGGQRQRIALARALYGDPKLVVLDEPNSN 484
|
170 180
....*....|....*....|....*...
gi 931484041 172 LDEENTNKLLDVFGSLKSEGRTIILVTH 199
Cdd:TIGR01842 485 LDEEGEQALANAIKALKARGITVVVITH 512
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
20-173 |
2.23e-26 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 104.03 E-value: 2.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 20 VLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfshddTRLSeIRNKKMGFVFQFHHLLAEFT 99
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV-----THRS-IQQRDICMVFQSYALFPHMS 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 931484041 100 CLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLD 173
Cdd:PRK11432 95 LGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-200 |
2.36e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 102.09 E-value: 2.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSKTYF--LENETIeVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfshddTRLS 78
Cdd:COG1101 1 MLELKNLSKTFNpgTVNEKR-ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV-----TKLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 79 E-IRNKKMGFVFQ------FHHLlaefTCLENVALPALVN-----GSAQNKAYR-RAQDLLDKFDIGdKKNRLPLEI--- 142
Cdd:COG1101 75 EyKRAKYIGRVFQdpmmgtAPSM----TIEENLALAYRRGkrrglRRGLTKKRReLFRELLATLGLG-LENRLDTKVgll 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 931484041 143 SGGERQRVAIARAMINDPLIIFADEPTGNLDEENTNKLLDVFGSLKSEGR-TIILVTHS 200
Cdd:COG1101 150 SGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNlTTLMVTHN 208
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
10-203 |
2.53e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 102.51 E-value: 2.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 10 TYFLENETiEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfsHDDTRlSEIRNKkMGFVF 89
Cdd:PRK13647 11 HFRYKDGT-KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREV--NAENE-KWVRSK-VGLVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 90 QF--HHLLAEfTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADE 167
Cdd:PRK13647 86 QDpdDQVFSS-TVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDE 164
|
170 180 190
....*....|....*....|....*....|....*.
gi 931484041 168 PTGNLDEENTNKLLDVFGSLKSEGRTIILVTHSVDI 203
Cdd:PRK13647 165 PMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDL 200
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-199 |
4.40e-26 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 103.49 E-value: 4.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 2 LQASTVSKTYflenETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfshddTRLS-EI 80
Cdd:PRK09452 15 VELRGISKSF----DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI-----THVPaEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 81 RNkkMGFVFQFHHLLAEFTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDP 160
Cdd:PRK09452 86 RH--VNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKP 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 931484041 161 LIIFADEPTGNLDEENTNKLLDVFGSLKSE-GRTIILVTH 199
Cdd:PRK09452 164 KVLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTH 203
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-202 |
5.41e-26 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 101.24 E-value: 5.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSKTyFLENETievLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLdrPTDGKVVFDSVDVFSHD---DTRL 77
Cdd:PRK09984 4 IIRVEKLAKT-FNQHQA---LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL--ITGDKSAGSHIELLGRTvqrEGRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 78 S-EIRNKK--MGFVFQFHHLLAEFTCLENVALPALVNGSAQNKAYR--------RAQDLLDKFDIGDKKNRLPLEISGGE 146
Cdd:PRK09984 78 ArDIRKSRanTGYIFQQFNLVNRLSVLENVLIGALGSTPFWRTCFSwftreqkqRALQALTRVGMVHFAHQRVSTLSGGQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 931484041 147 RQRVAIARAMINDPLIIFADEPTGNLDEENTNKLLDVFGSL-KSEGRTIILVTHSVD 202
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVD 214
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
20-202 |
1.44e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 100.45 E-value: 1.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 20 VLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDdtrLSEIRnKKMGFVFQ-----FHHL 94
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEN---LKEIR-KKIGIIFQnpdnqFIGA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 95 LAE----FTcLENVALPalvngsaQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTG 170
Cdd:PRK13632 100 TVEddiaFG-LENKKVP-------PKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTS 171
|
170 180 190
....*....|....*....|....*....|...
gi 931484041 171 NLDEENTNKLLDVFGSLKSEG-RTIILVTHSVD 202
Cdd:PRK13632 172 MLDPKGKREIKKIMVDLRKTRkKTLISITHDMD 204
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-199 |
1.97e-25 |
|
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: 97.38 E-value: 1.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 2 LQASTVSKTYfLENETiEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRlseir 81
Cdd:cd03247 1 LSINNVSFSY-PEQEQ-QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKAL----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 82 NKKMGFVFQFHHLLAEfTCLENVALPalvngsaqnkayrraqdlldkfdigdkknrlpleISGGERQRVAIARAMINDPL 161
Cdd:cd03247 74 SSLISVLNQRPYLFDT-TLRNNLGRR----------------------------------FSGGERQRLALARILLQDAP 118
|
170 180 190
....*....|....*....|....*....|....*...
gi 931484041 162 IIFADEPTGNLDEENTNKLLDVFGSLkSEGRTIILVTH 199
Cdd:cd03247 119 IVLLDEPTVGLDPITERQLLSLIFEV-LKDKTLIWITH 155
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
14-199 |
3.02e-25 |
|
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: 98.50 E-value: 3.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 14 ENETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRP---TDGKVVFDSVDvfSHDDTRLSEIrnkkmGFVFQ 90
Cdd:cd03234 16 WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQP--RKPDQFQKCV-----AYVRQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 91 FHHLLAEFTCLENVALPA-LVNGSAQNKAYRRAQD---LLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFAD 166
Cdd:cd03234 89 DDILLPGLTVRETLTYTAiLRLPRKSSDAIRKKRVedvLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILD 168
|
170 180 190
....*....|....*....|....*....|...
gi 931484041 167 EPTGNLDEENTNKLLDVFGSLKSEGRTIILVTH 199
Cdd:cd03234 169 EPTSGLDSFTALNLVSTLSQLARRNRIVILTIH 201
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
25-202 |
4.66e-25 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 98.12 E-value: 4.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 25 NLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDvfsHDDTRLSEiRNKKMgfVFQFHHLLAEFTCLENV 104
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD---HTTTPPSR-RPVSM--LFQENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 105 AL---PALVNGSAQNkayRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLDEENTNKLL 181
Cdd:PRK10771 93 GLglnPGLKLNAAQR---EKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEML 169
|
170 180
....*....|....*....|..
gi 931484041 182 DVFGSLKSEGR-TIILVTHSVD 202
Cdd:PRK10771 170 TLVSQVCQERQlTLLMVSHSLE 191
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
24-220 |
5.67e-25 |
|
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: 100.19 E-value: 5.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 24 VNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLSEIRNKKMGFVFQFHHLLAEFTCLEN 103
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 104 valpaLVNG-SAQNKAYRRAQD--LLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLDEENTNKL 180
Cdd:TIGR02142 96 -----LRYGmKRARPSERRISFerVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEI 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 931484041 181 LDVFGSLKSEGRT-IILVTHSVD-ISKFGSHVYKLKERELHA 220
Cdd:TIGR02142 171 LPYLERLHAEFGIpILYVSHSLQeVLRLADRVVVLEDGRVAA 212
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
14-199 |
6.19e-25 |
|
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: 101.68 E-value: 6.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 14 ENETIEVLQGVNLLVSKGSFVVILGPSGSGKS-TLLNILSSLDRP---TDGKVVFDSVDVFSHDDTRLSEIRNKKMGFVF 89
Cdd:COG4172 19 GGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPaahPSGSILFDGQDLLGLSERELRRIRGNRIAMIF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 90 QfhhllaE-FTCL-----------ENVALPALVNGSAqnkAYRRAQDLLDKFDIGDKKNRL---PLEISGGERQRVAIAR 154
Cdd:COG4172 99 Q------EpMTSLnplhtigkqiaEVLRLHRGLSGAA---ARARALELLERVGIPDPERRLdayPHQLSGGQRQRVMIAM 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 931484041 155 AMINDPLIIFADEPTGNLDEENTNKLLDVFGSLKSE-GRTIILVTH 199
Cdd:COG4172 170 ALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITH 215
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
7-199 |
6.53e-25 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 100.10 E-value: 6.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 7 VSKTYflenETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDsvdvfshdDTRLSEIRNKK-- 84
Cdd:PRK11000 9 VTKAY----GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIG--------EKRMNDVPPAErg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 85 MGFVFQFHHLLAEFTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIF 164
Cdd:PRK11000 77 VGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 931484041 165 ADEPTGNLDeentnKLLDVfgSLKSE--------GRTIILVTH 199
Cdd:PRK11000 157 LDEPLSNLD-----AALRV--QMRIEisrlhkrlGRTMIYVTH 192
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-199 |
6.60e-25 |
|
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: 97.61 E-value: 6.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 18 IEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfshDDTRLSEIRNkKMGFVFQFHHLLAE 97
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDI---RDLNLRWLRS-QIGLVSQEPVLFDG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 98 fTCLENVALPA-------LVNGSAQNKAYRRAQDLLDKFD--IGDKKNRLpleiSGGERQRVAIARAMINDPLIIFADEP 168
Cdd:cd03249 92 -TIAENIRYGKpdatdeeVEEAAKKANIHDFIMSLPDGYDtlVGERGSQL----SGGQKQRIAIARALLRNPKILLLDEA 166
|
170 180 190
....*....|....*....|....*....|....
gi 931484041 169 TGNLDEENT---NKLLDVFgslkSEGRTIILVTH 199
Cdd:cd03249 167 TSALDAESEklvQEALDRA----MKGRTTIVIAH 196
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
16-199 |
7.22e-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: 101.42 E-value: 7.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 16 ETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLD--RPTDGKVVF----------------------------- 64
Cdd:TIGR03269 11 DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIIYhvalcekcgyverpskvgepcpvcggtle 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 65 -DSVDVFSHDDTRLSEIRnKKMGFVFQ-FHHLLAEFTCLENV--ALPALvnGSAQNKAYRRAQDLLDKFDIGDKKNRLPL 140
Cdd:TIGR03269 91 pEEVDFWNLSDKLRRRIR-KRIAIMLQrTFALYGDDTVLDNVleALEEI--GYEGKEAVGRAVDLIEMVQLSHRITHIAR 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 141 EISGGERQRVAIARAMINDPLIIFADEPTGNLDEENTNKLLDVF-GSLKSEGRTIILVTH 199
Cdd:TIGR03269 168 DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALeEAVKASGISMVLTSH 227
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
20-199 |
2.61e-24 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 94.99 E-value: 2.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 20 VLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDsvdvfshddtrlseiRNKKMGFVFQFHHLLAEF- 98
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRA---------------GGARVAYVPQRSEVPDSLp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 99 -TCLENVAL----PALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLD 173
Cdd:NF040873 72 lTVRDLVAMgrwaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180
....*....|....*....|....*.
gi 931484041 174 EENTNKLLDVFGSLKSEGRTIILVTH 199
Cdd:NF040873 152 AESRERIIALLAEEHARGATVVVVTH 177
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
12-202 |
6.71e-24 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 94.78 E-value: 6.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 12 FLENETIeVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfshddTRLS-EIRNKKMGFVFQ 90
Cdd:PRK10247 15 YLAGDAK-ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDI-----STLKpEIYRQQVSYCAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 91 FHHLLAEfTCLENVALPALVNGSAQNKAyrRAQDLLDKFDIGDKKNRLPL-EISGGERQRVAIARAMINDPLIIFADEPT 169
Cdd:PRK10247 89 TPTLFGD-TVYDNLIFPWQIRNQQPDPA--IFLDDLERFALPDTILTKNIaELSGGEKQRISLIRNLQFMPKVLLLDEIT 165
|
170 180 190
....*....|....*....|....*....|....
gi 931484041 170 GNLDEENTNKLLDVFGSLKSE-GRTIILVTHSVD 202
Cdd:PRK10247 166 SALDESNKHNVNEIIHRYVREqNIAVLWVTHDKD 199
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-173 |
8.05e-24 |
|
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: 94.92 E-value: 8.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 2 LQASTVSKTYflenETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFS---HDDTRLS 78
Cdd:cd03218 1 LRAENLSKRY----GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKlpmHKRARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 79 eirnkkMGFVFQFHHLLAEFTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMIN 158
Cdd:cd03218 77 ------IGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALAT 150
|
170
....*....|....*
gi 931484041 159 DPLIIFADEPTGNLD 173
Cdd:cd03218 151 NPKFLLLDEPFAGVD 165
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-199 |
9.59e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 95.95 E-value: 9.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSKTYflenETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDvFSHDDTR---- 76
Cdd:COG4152 1 MLELKGLTKRF----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEP-LDPEDRRrigy 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 77 LSEIR--NKKMgfvfqfhhllaefTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIAR 154
Cdd:COG4152 76 LPEERglYPKM-------------KVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIA 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 931484041 155 AMINDP-LIIFaDEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTH 199
Cdd:COG4152 143 ALLHDPeLLIL-DEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSH 187
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
14-210 |
1.39e-23 |
|
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: 94.32 E-value: 1.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 14 ENETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLseirnKKMGFVF-QFH 92
Cdd:cd03267 30 KYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFL-----RRIGVVFgQKT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 93 HLLAEFTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNL 172
Cdd:cd03267 105 QLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 931484041 173 D---EENTNKLLDVFGslKSEGRTIILVTHSV-DISKFGSHV 210
Cdd:cd03267 185 DvvaQENIRNFLKEYN--RERGTTVLLTSHYMkDIEALARRV 224
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-215 |
1.80e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 94.85 E-value: 1.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 19 EVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfsHDDTRLSEIR--NKKMGFVFQFhhllA 96
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITI--THKTKDKYIRpvRKRIGMVFQF----P 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 97 EFTCLENVALPALVNGSAQ-----NKAYRRAQDLLdkFDIGDKKNRL---PLEISGGERQRVAIARAMINDPLIIFADEP 168
Cdd:PRK13646 95 ESQLFEDTVEREIIFGPKNfkmnlDEVKNYAHRLL--MDLGFSRDVMsqsPFQMSGGQMRKIAIVSILAMNPDIIVLDEP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 931484041 169 TGNLDEENTNKLLDVFGSLKSE-GRTIILVTHSV-DISKFGSHVYKLKE 215
Cdd:PRK13646 173 TAGLDPQSKRQVMRLLKSLQTDeNKTIILVSHDMnEVARYADEVIVMKE 221
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-173 |
2.46e-23 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 95.68 E-value: 2.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSKTYflENETiEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVvfdsvdvfSHDDTRLSEI 80
Cdd:PRK11650 3 GLKLQAVRKSY--DGKT-QVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEI--------WIGGRVVNEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 81 ----RNKKMgfVFQFHHLLAEFTCLENVALpALVN-GSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARA 155
Cdd:PRK11650 72 epadRDIAM--VFQNYALYPHMSVRENMAY-GLKIrGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRA 148
|
170
....*....|....*...
gi 931484041 156 MINDPLIIFADEPTGNLD 173
Cdd:PRK11650 149 IVREPAVFLFDEPLSNLD 166
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-173 |
3.49e-23 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 93.68 E-value: 3.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSktYFLENETIevLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLSEI 80
Cdd:PRK13548 2 MLEARNLS--VRLGGRTL--LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 81 RnkkmGFVFQFHHLLAEFTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMI--- 157
Cdd:PRK13548 78 R----AVLPQHSSLSFPFTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlw 153
|
170
....*....|....*....
gi 931484041 158 ---NDPLIIFADEPTGNLD 173
Cdd:PRK13548 154 epdGPPRWLLLDEPTSALD 172
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
19-203 |
6.95e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 93.37 E-value: 6.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 19 EVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfshDDTR--LSEIRnKKMGFVFQF-HHLL 95
Cdd:PRK13636 20 HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI---DYSRkgLMKLR-ESVGMVFQDpDNQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 96 AEFTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLDEE 175
Cdd:PRK13636 96 FSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPM 175
|
170 180
....*....|....*....|....*....
gi 931484041 176 NTNKLLDVFGSLKSE-GRTIILVTHSVDI 203
Cdd:PRK13636 176 GVSEIMKLLVEMQKElGLTIIIATHDIDI 204
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
19-199 |
7.28e-23 |
|
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: 92.55 E-value: 7.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 19 EVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLseirNKKMGFVFQfHHLLAEF 98
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWL----RRQVGVVLQ-ENVLFNR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 99 TCLENVAL--PA-----LVNGSAQNKAYRRAQDLLDKFD--IGDKKNRLpleiSGGERQRVAIARAMINDPLIIFADEPT 169
Cdd:cd03252 91 SIRDNIALadPGmsmerVIEAAKLAGAHDFISELPEGYDtiVGEQGAGL----SGGQRQRIAIARALIHNPRILIFDEAT 166
|
170 180 190
....*....|....*....|....*....|
gi 931484041 170 GNLDEENTNKLLDVFGSLkSEGRTIILVTH 199
Cdd:cd03252 167 SALDYESEHAIMRNMHDI-CAGRTVIIIAH 195
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-209 |
9.17e-23 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 92.68 E-value: 9.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSKTYflenETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLSEI 80
Cdd:PRK11701 6 LLSVRGLTKLY----GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 81 RNKKM-----GFVFQfhH----LLAEFTCLENVALPALVNGsaqNKAYRR----AQDLLDKFDIG-DKKNRLPLEISGGE 146
Cdd:PRK11701 82 ERRRLlrtewGFVHQ--HprdgLRMQVSAGGNIGERLMAVG---ARHYGDiratAGDWLERVEIDaARIDDLPTTFSGGM 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 931484041 147 RQRVAIARAMINDPLIIFADEPTGNLDEENTNKLLDVFGSLKSE-GRTIILVTHSVDISKFGSH 209
Cdd:PRK11701 157 QQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAH 220
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1-199 |
1.15e-22 |
|
nickel import ATP-binding protein NikE; This family represents the NikE 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. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 92.56 E-value: 1.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSKTY-----FLENETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDT 75
Cdd:TIGR02769 2 LLEVRDVTHTYrtgglFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 76 RLSEIRnKKMGFVFQ--FHHLLAEFTCLENVALPaLVNGSAQNKAYR--RAQDLLDKFDI-GDKKNRLPLEISGGERQRV 150
Cdd:TIGR02769 82 QRRAFR-RDVQLVFQdsPSAVNPRMTVRQIIGEP-LRHLTSLDESEQkaRIAELLDMVGLrSEDADKLPRQLSGGQLQRI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 931484041 151 AIARAMINDPLIIFADEPTGNLDEENTNKLLDVFGSLKSE-GRTIILVTH 199
Cdd:TIGR02769 160 NIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAfGTAYLFITH 209
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
18-173 |
1.18e-22 |
|
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: 95.14 E-value: 1.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 18 IEVLQGVNLLVSKGSFVVILGPSGSGKSTL-LNILssldR--PTDGKVVFDSVDVFSHDDTRLSEIRnKKMGFVFQ--FH 92
Cdd:COG4172 299 VKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALL----RliPSEGEIRFDGQDLDGLSRRALRPLR-RRMQVVFQdpFG 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 93 HLLAEFTCLENVALPALVNGSAQNKAYRRAQ--DLLDkfDIG---DKKNRLPLEISGGERQRVAIARAMINDPLIIFADE 167
Cdd:COG4172 374 SLSPRMTVGQIIAEGLRVHGPGLSAAERRARvaEALE--EVGldpAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDE 451
|
....*.
gi 931484041 168 PTGNLD 173
Cdd:COG4172 452 PTSALD 457
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-168 |
1.97e-22 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 91.24 E-value: 1.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSKTYflenETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfshddTRLS-E 79
Cdd:COG1137 3 TLEAENLVKSY----GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI-----THLPmH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 80 IRNKK-MGFVFQ----FHHLLAEftclENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIAR 154
Cdd:COG1137 74 KRARLgIGYLPQeasiFRKLTVE----DNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIAR 149
|
170
....*....|....
gi 931484041 155 AMINDPLIIFADEP 168
Cdd:COG1137 150 ALATNPKFILLDEP 163
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
7-202 |
3.06e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 91.99 E-value: 3.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 7 VSKTYFLENE-TIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfSHDDTRLSEIRN--K 83
Cdd:PRK13645 12 VSYTYAKKTPfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAI-PANLKKIKEVKRlrK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 84 KMGFVFQF-HHLLAEFTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIG-DKKNRLPLEISGGERQRVAIARAMINDPL 161
Cdd:PRK13645 91 EIGLVFQFpEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPeDYVKRSPFELSGGQKRRVALAGIIAMDGN 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 931484041 162 IIFADEPTGNLDEENTNKLLDVFGSL-KSEGRTIILVTHSVD 202
Cdd:PRK13645 171 TLVLDEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMD 212
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-199 |
3.16e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 92.59 E-value: 3.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 5 STVSKTYflenETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHddTRLSEIRnkk 84
Cdd:PRK13536 45 AGVSKSY----GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPAR--ARLARAR--- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 85 MGFVFQFHHLLAEFTCLENValpaLVNGSAQNKAYRRAQ----DLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDP 160
Cdd:PRK13536 116 IGVVPQFDNLDLEFTVRENL----LVFGRYFGMSTREIEavipSLLEFARLESKADARVSDLSGGMKRRLTLARALINDP 191
|
170 180 190
....*....|....*....|....*....|....*....
gi 931484041 161 LIIFADEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTH 199
Cdd:PRK13536 192 QLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTH 230
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-200 |
4.48e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 90.88 E-value: 4.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 7 VSKTYFLENETiEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDR------PTDGKVVFDSVDVFSHDDTRLsei 80
Cdd:PRK14246 13 ISRLYLYINDK-AILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKL--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 81 rNKKMGFVFQFHHLLAEFTCLENVALPALVNGSAQNKAYRR-AQDLLDKF----DIGDKKNRLPLEISGGERQRVAIARA 155
Cdd:PRK14246 89 -RKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKREIKKiVEECLRKVglwkEVYDRLNSPASQLSGGQQQRLTIARA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 931484041 156 MINDPLIIFADEPTGNLDEENTNKLLDVFGSLKSEgRTIILVTHS 200
Cdd:PRK14246 168 LALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHN 211
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
20-199 |
5.00e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 90.46 E-value: 5.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 20 VLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLSeirnKKMGFVFQfHHLLAE-F 98
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA----RRLALLPQ-HHLTPEgI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 99 TCLENVAL---PAL-VNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLDE 174
Cdd:PRK11231 92 TVRELVAYgrsPWLsLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDI 171
|
170 180
....*....|....*....|....*
gi 931484041 175 ENTNKLLDVFGSLKSEGRTIILVTH 199
Cdd:PRK11231 172 NHQVELMRLMRELNTQGKTVVTVLH 196
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
26-199 |
5.29e-22 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 89.91 E-value: 5.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 26 LLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVvfdsvdvfsHDDTRLSEIRNKKMGFVFQFHHLLAEFTCleNVA 105
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTV---------KVAGASPGKGWRHIGYVPQRHEFAWDFPI--SVA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 106 lPALVNGSAQNKA-YRRAQ--------DLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLDEEN 176
Cdd:TIGR03771 70 -HTVMSGRTGHIGwLRRPCvadfaavrDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPT 148
|
170 180
....*....|....*....|...
gi 931484041 177 TNKLLDVFGSLKSEGRTIILVTH 199
Cdd:TIGR03771 149 QELLTELFIELAGAGTAILMTTH 171
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
2-201 |
5.82e-22 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 90.03 E-value: 5.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 2 LQASTVSKTYflenETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFS---HDDTRLS 78
Cdd:TIGR04406 2 LVAENLIKSY----KKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHlpmHERARLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 79 eirnkkMGFVFQFHHLLAEFTCLENV--ALPALVNGSAQNKAyRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAM 156
Cdd:TIGR04406 78 ------IGYLPQEASIFRKLTVEENImaVLEIRKDLDRAERE-ERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARAL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 931484041 157 INDPLIIFADEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTHSV 201
Cdd:TIGR04406 151 ATNPKFILLDEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNV 195
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
14-202 |
7.60e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 91.07 E-value: 7.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 14 ENETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLS-------EIRN---- 82
Cdd:PRK13631 35 QENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELitnpyskKIKNfkel 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 83 -KKMGFVFQF-HHLLAEFTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDK-KNRLPLEISGGERQRVAIARAMIND 159
Cdd:PRK13631 115 rRRVSMVFQFpEYQLFKDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSyLERSPFGLSGGQKRRVAIAGILAIQ 194
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 931484041 160 PLIIFADEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTHSVD 202
Cdd:PRK13631 195 PEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTME 237
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
6-173 |
8.87e-22 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 91.18 E-value: 8.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 6 TVSKTYFLENETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLSEIRnKKM 85
Cdd:PRK11308 16 PVKRGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLR-QKI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 86 GFVFQ--FHHL---------LAEftclenvalPALVN---GSAQNKAyrRAQDLLDKfdIGDKK---NRLPLEISGGERQ 148
Cdd:PRK11308 95 QIVFQnpYGSLnprkkvgqiLEE---------PLLINtslSAAERRE--KALAMMAK--VGLRPehyDRYPHMFSGGQRQ 161
|
170 180
....*....|....*....|....*
gi 931484041 149 RVAIARAMINDPLIIFADEPTGNLD 173
Cdd:PRK11308 162 RIAIARALMLDPDVVVADEPVSALD 186
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-202 |
9.07e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 90.43 E-value: 9.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSKTYfleNETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDvfSHDDTRLSEI 80
Cdd:PRK13644 1 MIRLENVSYSY---PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGID--TGDFSKLQGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 81 RnKKMGFVFQ------FHHLLAEFTCL--ENVALPALvngsaqnKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAI 152
Cdd:PRK13644 76 R-KLVGIVFQnpetqfVGRTVEEDLAFgpENLCLPPI-------EIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVAL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 931484041 153 ARAMINDPLIIFADEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTHSVD 202
Cdd:PRK13644 148 AGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLE 197
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
23-199 |
1.86e-21 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 88.89 E-value: 1.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 23 GVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDsvdvfSHDDTRLSEIRNKKMGFVFQFHH--LLAEFTC 100
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLR-----GQHIEGLPGHQIARMGVVRTFQHvrLFREMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 101 LEN--VALPALVN-----GSAQNKAYRRAQD--------LLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFA 165
Cdd:PRK11300 98 IENllVAQHQQLKtglfsGLLKTPAFRRAESealdraatWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILML 177
|
170 180 190
....*....|....*....|....*....|....*
gi 931484041 166 DEPTGNLDEENTNKLLDVFGSLKSE-GRTIILVTH 199
Cdd:PRK11300 178 DEPAAGLNPKETKELDELIAELRNEhNVTVLLIEH 212
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
14-215 |
1.89e-21 |
|
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: 87.91 E-value: 1.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 14 ENETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLN-ILSSLDRpTDGKVVFdsvdvfshddtrlseirNKKMGFVFQFh 92
Cdd:cd03250 14 EQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGELEK-LSGSVSV-----------------PGSIAYVSQE- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 93 hllaeftclenvalPALVNGSAQN----------KAYRRA-------QDL-----LDKFDIGDKKNRLpleiSGGERQRV 150
Cdd:cd03250 75 --------------PWIQNGTIREnilfgkpfdeERYEKVikacalePDLeilpdGDLTEIGEKGINL----SGGQKQRI 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 931484041 151 AIARAMINDPLIIFADEPTGNLDEENTNKLLD-VFGSLKSEGRTIILVTHSVDISKFGSHVYKLKE 215
Cdd:cd03250 137 SLARAVYSDADIYLLDDPLSAVDAHVGRHIFEnCILGLLLNNKTRILVTHQLQLLPHADQIVVLDN 202
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
20-215 |
2.20e-21 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 91.71 E-value: 2.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 20 VLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLseirNKKMGFVFQfHHLLAEFT 99
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYL----HRQVALVGQ-EPVLFSGS 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 100 CLENVALPALVNGSAQNKAYRR---AQDLLDKF------DIGDKKNRLpleiSGGERQRVAIARAMINDPLIIFADEPTG 170
Cdd:TIGR00958 571 VRENIAYGLTDTPDEEIMAAAKaanAHDFIMEFpngydtEVGEKGSQL----SGGQKQRIAIARALVRKPRVLILDEATS 646
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 931484041 171 NLDEENTNKLLDvfgSLKSEGRTIILVTHSVDISKFGSHVYKLKE 215
Cdd:TIGR00958 647 ALDAECEQLLQE---SRSRASRTVLLIAHRLSTVERADQILVLKK 688
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
24-201 |
2.28e-21 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 89.05 E-value: 2.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 24 VNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLSEIRnKKMGFVFQFHHLLAEFTCLEN 103
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVR-KRMSMLFQSGALFTDMNVFDN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 104 VALP---------ALVNGSAQNKayrraqdlLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLDE 174
Cdd:PRK11831 105 VAYPlrehtqlpaPLLHSTVMMK--------LEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDP 176
|
170 180
....*....|....*....|....*...
gi 931484041 175 ENTNKLLDVFGSLKSE-GRTIILVTHSV 201
Cdd:PRK11831 177 ITMGVLVKLISELNSAlGVTCVVVSHDV 204
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
21-202 |
2.54e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 88.92 E-value: 2.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 21 LQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVvfdSVDVFSHDDTRLSEIRnKKMGFVFQfhHLLAEF-- 98
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTI---TVGGMVLSEETVWDVR-RQVGMVFQ--NPDNQFvg 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 99 -TCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLDEENT 177
Cdd:PRK13635 97 aTVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGR 176
|
170 180
....*....|....*....|....*.
gi 931484041 178 NKLLDVFGSLKSEGR-TIILVTHSVD 202
Cdd:PRK13635 177 REVLETVRQLKEQKGiTVLSITHDLD 202
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-197 |
2.80e-21 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 88.01 E-value: 2.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSKTYflenETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfshDDTRLSEI 80
Cdd:PRK11614 5 MLSFDKVSAHY----GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDI---TDWQTAKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 81 RNKKMGFVFQFHHLLAEFTCLENVALPALVNGSAQ-NKAYRRAQDLLDKfdIGDKKNRLPLEISGGERQRVAIARAMIND 159
Cdd:PRK11614 78 MREAVAIVPEGRRVFSRMTVEENLAMGGFFAERDQfQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQ 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 931484041 160 PLIIFADEPTGNLDEENTNKLLDVFGSLKSEGRTIILV 197
Cdd:PRK11614 156 PRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLV 193
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
20-199 |
3.11e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 89.48 E-value: 3.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 20 VLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHddTRLSEIRnkkMGFVFQFHHLLAEFT 99
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSR--ARHARQR---VGVVPQFDNLDPDFT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 100 CLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLDEENTNK 179
Cdd:PRK13537 97 VRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHL 176
|
170 180
....*....|....*....|
gi 931484041 180 LLDVFGSLKSEGRTIILVTH 199
Cdd:PRK13537 177 MWERLRSLLARGKTILLTTH 196
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
20-204 |
3.70e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 90.29 E-value: 3.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 20 VLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLSeirnKKMGFVFQFHHLLAEFT 99
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAAS----RRVASVPQDTSLSFEFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 100 CLENVAL---PALVNGSAQNKAYRRAQD-LLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLDEE 175
Cdd:PRK09536 94 VRQVVEMgrtPHRSRFDTWTETDRAAVErAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDIN 173
|
170 180
....*....|....*....|....*....
gi 931484041 176 NTNKLLDVFGSLKSEGRTIILVTHSVDIS 204
Cdd:PRK09536 174 HQVRTLELVRRLVDDGKTAVAAIHDLDLA 202
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
36-202 |
5.56e-21 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 89.16 E-value: 5.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 36 ILGPSGSGKSTLLNILSSLDRPTDGKVVF-DSVDVFSHDDTRLS-EIRnkKMGFVFQFHHLLAEFTclenvalpalVNGs 113
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLnGRVLFDAEKGICLPpEKR--RIGYVFQDARLFPHYK----------VRG- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 114 aqNKAYRRAQDLLDKFD-------IGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLDEENTNKLLDVFGS 186
Cdd:PRK11144 96 --NLRYGMAKSMVAQFDkivallgIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLER 173
|
170
....*....|....*..
gi 931484041 187 LKSEGRTIIL-VTHSVD 202
Cdd:PRK11144 174 LAREINIPILyVSHSLD 190
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
5-201 |
5.58e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 87.92 E-value: 5.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 5 STVSKTYFLENETIEV-------LQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDR--PT---DGKVVFDSVDVFSh 72
Cdd:PRK14243 3 TLNGTETVLRTENLNVyygsflaVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHGKNLYA- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 73 DDTRLSEIRnKKMGFVFQFHHLLAEfTCLENVALPALVNGSAQN------KAYRRAQdLLDkfDIGDKKNRLPLEISGGE 146
Cdd:PRK14243 82 PDVDPVEVR-RRIGMVFQKPNPFPK-SIYDNIAYGARINGYKGDmdelveRSLRQAA-LWD--EVKDKLKQSGLSLSGGQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 931484041 147 RQRVAIARAMINDPLIIFADEPTGNLDEENTNKLLDVFGSLKsEGRTIILVTHSV 201
Cdd:PRK14243 157 QQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELK-EQYTIIIVTHNM 210
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
18-215 |
7.24e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 90.23 E-value: 7.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 18 IEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDvFSHDDTRLSEirNKKMGFVFQFHHLLAE 97
Cdd:PRK09700 18 VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNIN-YNKLDHKLAA--QLGIGIIYQELSVIDE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 98 FTCLENVALPAL-------VNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTG 170
Cdd:PRK09700 95 LTVLENLYIGRHltkkvcgVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTS 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 931484041 171 NLDEENTNKLLDVFGSLKSEGRTIILVTHSV-DISKFGSHVYKLKE 215
Cdd:PRK09700 175 SLTNKEVDYLFLIMNQLRKEGTAIVYISHKLaEIRRICDRYTVMKD 220
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
21-210 |
7.93e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 87.50 E-value: 7.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 21 LQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDdtrLSEIRnKKMGFVFQ-----FHHLL 95
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDN---FEKLR-KHIGIVFQnpdnqFVGSI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 96 AEFTC---LENVALPalvngsaQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNL 172
Cdd:PRK13648 101 VKYDVafgLENHAVP-------YDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSML 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 931484041 173 DEENTNKLLDVFGSLKSEGR-TIILVTHSVDISKFGSHV 210
Cdd:PRK13648 174 DPDARQNLLDLVRKVKSEHNiTIISITHDLSEAMEADHV 212
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
19-201 |
1.11e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 86.75 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 19 EVLQGVNLLVSKGSFVVILGPSGSGKSTLLNilsSLDRPTD--------GKVVFDSVDVFS-HDDTrlSEIRnKKMGFVF 89
Cdd:PRK14239 19 KALNSVSLDFYPNEITALIGPSGSGKSTLLR---SINRMNDlnpevtitGSIVYNGHNIYSpRTDT--VDLR-KEIGMVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 90 QFHHLLAeFTCLENVALPALVNGSAQNKAYRRA-QDLLDKFDIGDK-KNRL---PLEISGGERQRVAIARAMINDPLIIF 164
Cdd:PRK14239 93 QQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAvEKSLKGASIWDEvKDRLhdsALGLSGGQQQRVCIARVLATSPKIIL 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 931484041 165 ADEPTGNLDEENTNKLLDVFGSLKSEgRTIILVTHSV 201
Cdd:PRK14239 172 LDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSM 207
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
7-202 |
1.39e-20 |
|
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: 89.09 E-value: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 7 VSKTYF-LENETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVF----DSVDVfsHDDTRLSEIR 81
Cdd:TIGR03269 285 VSKRYIsVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDM--TKPGPDGRGR 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 82 NKK-MGFVFQFHHLLAEFTCLENVA------LPalvngsaQNKAYRRAQDLLDKFDIGDKK-----NRLPLEISGGERQR 149
Cdd:TIGR03269 363 AKRyIGILHQEYDLYPHRTVLDNLTeaigleLP-------DELARMKAVITLKMVGFDEEKaeeilDKYPDELSEGERHR 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 931484041 150 VAIARAMINDPLIIFADEPTGNLDEENTNKLLD-VFGSLKSEGRTIILVTHSVD 202
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDPITKVDVTHsILKAREEMEQTFIIVSHDMD 489
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-202 |
1.75e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 88.81 E-value: 1.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 21 LQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDV-FShdDTRlsEIRNKKMGFVFQFHHLLAEFT 99
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrFA--STT--AALAAGVAIIYQELHLVPEMT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 100 CLENV---ALPA---LVNGSAqnkAYRRAQDLLDKFDIgDKKNRLPL-EISGGERQRVAIARAMINDPLIIFADEPTGNL 172
Cdd:PRK11288 96 VAENLylgQLPHkggIVNRRL---LNYEAREQLEHLGV-DIDPDTPLkYLSIGQRQMVEIAKALARNARVIAFDEPTSSL 171
|
170 180 190
....*....|....*....|....*....|
gi 931484041 173 DEENTNKLLDVFGSLKSEGRTIILVTHSVD 202
Cdd:PRK11288 172 SAREIEQLFRVIRELRAEGRVILYVSHRME 201
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-201 |
1.86e-20 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 86.66 E-value: 1.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSKTY-----FLENETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDT 75
Cdd:PRK10419 3 LLNVSGLSHHYahgglSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 76 RLSEIRnKKMGFVFQ--FHHLLAEFTCLENVALPA--LVNGSAQNKAyRRAQDLLDKFDIGDK-KNRLPLEISGGERQRV 150
Cdd:PRK10419 83 QRKAFR-RDIQMVFQdsISAVNPRKTVREIIREPLrhLLSLDKAERL-ARASEMLRAVDLDDSvLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 931484041 151 AIARAMINDPLIIFADEPTGNLDEENTNKLLDVFGSLKSEGRT-IILVTHSV 201
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTaCLFITHDL 212
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
17-211 |
4.63e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 85.62 E-value: 4.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 17 TIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDdtrLSEIRnKKMGFVFQF-HHLL 95
Cdd:PRK13652 16 SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKEN---IREVR-KFVGLVFQNpDDQI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 96 AEFTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLDEE 175
Cdd:PRK13652 92 FSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQ 171
|
170 180 190
....*....|....*....|....*....|....*...
gi 931484041 176 NTNKLLDVFGSL-KSEGRTIILVTHSVD-ISKFGSHVY 211
Cdd:PRK13652 172 GVKELIDFLNDLpETYGMTVIFSTHQLDlVPEMADYIY 209
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
19-199 |
4.71e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 87.81 E-value: 4.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 19 EVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDsvdvfshddtrlseiRNKKMGFVFQFHHLLAEF 98
Cdd:COG0488 12 PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP---------------KGLRIGYLPQEPPLDDDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 99 TCLENV----------------ALPALVNGSAQNKAY----------------RRAQDLLDKFDIGDKKNRLPL-EISGG 145
Cdd:COG0488 77 TVLDTVldgdaelraleaeleeLEAKLAEPDEDLERLaelqeefealggweaeARAEEILSGLGFPEEDLDRPVsELSGG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 931484041 146 ERQRVAIARAMINDPLIIFADEPTGNLDEENTNKLLDVfgsLKSEGRTIILVTH 199
Cdd:COG0488 157 WRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEF---LKNYPGTVLVVSH 207
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
31-199 |
4.79e-20 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 87.80 E-value: 4.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 31 GSFVVILGPSGSGKSTLLNILSSLDRP---TDGKVVFDSVDVFSHDDTRLSeirnkkmGFVFQFHHLLAEFTCLENVALP 107
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKEMRAIS-------AYVQQDDLFIPTLTVREHLMFQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 108 ALV---NGSAQNKAYRRAQDLLDKFDIGDKKNRL------PLEISGGERQRVAIARAMINDPLIIFADEPTGNLDEENTN 178
Cdd:TIGR00955 124 AHLrmpRRVTKKEKRERVDEVLQALGLRKCANTRigvpgrVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAY 203
|
170 180
....*....|....*....|.
gi 931484041 179 KLLDVFGSLKSEGRTIILVTH 199
Cdd:TIGR00955 204 SVVQVLKGLAQKGKTIICTIH 224
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
20-199 |
6.54e-20 |
|
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: 84.44 E-value: 6.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 20 VLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLSEirnkKMGFVFQFHHLLAEfT 99
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHS----KVSLVGQEPVLFAR-S 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 100 CLENVA--LPALVNGS---AQNKAYrrAQDLLDKF------DIGDKKNRLpleiSGGERQRVAIARAMINDPLIIFADEP 168
Cdd:cd03248 104 LQDNIAygLQSCSFECvkeAAQKAH--AHSFISELasgydtEVGEKGSQL----SGGQKQRVAIARALIRNPQVLILDEA 177
|
170 180 190
....*....|....*....|....*....|..
gi 931484041 169 TGNLDEENTNKLLD-VFGSLksEGRTIILVTH 199
Cdd:cd03248 178 TSALDAESEQQVQQaLYDWP--ERRTVLVIAH 207
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
21-199 |
7.52e-20 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 87.32 E-value: 7.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 21 LQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfsHDDTRLSEIRNkkMGFVFQFHHLLAEfTC 100
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDI--RTVTRASLRRN--IAVVFQDAGLFNR-SI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 101 LENV------ALPALVNGSAQNKAyrrAQDLL----DKFD--IGDKKNRLpleiSGGERQRVAIARAMINDPLIIFADEP 168
Cdd:PRK13657 426 EDNIrvgrpdATDEEMRAAAERAQ---AHDFIerkpDGYDtvVGERGRQL----SGGERQRLAIARALLKDPPILILDEA 498
|
170 180 190
....*....|....*....|....*....|.
gi 931484041 169 TGNLDEENTNKLLDVFGSLkSEGRTIILVTH 199
Cdd:PRK13657 499 TSALDVETEAKVKAALDEL-MKGRTTFIIAH 528
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
24-202 |
1.07e-19 |
|
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: 86.99 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 24 VNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfshdDTRLSEIRnKKMGFVFQ----FHHLlaefT 99
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI----ETNLDAVR-QSLGMCPQhnilFHHL----T 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 100 CLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLDEENTNK 179
Cdd:TIGR01257 1020 VAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRS 1099
|
170 180
....*....|....*....|...
gi 931484041 180 LLDVFGSLKSeGRTIILVTHSVD 202
Cdd:TIGR01257 1100 IWDLLLKYRS-GRTIIMSTHHMD 1121
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
16-205 |
1.07e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 86.68 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 16 ETIEVLQGVNLLVSKGSFVVILGPSGSGKS-TLLNILSSLDRP----TDGKVVFDSVDVFSHDDTRLSEIRNKKMGFVFQ 90
Cdd:PRK15134 20 TVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGVRGNKIAMIFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 91 --------FHHL---LAEFTCLENvalpalvnGSAQNKAYRRAQDLLDKFDIGDKKNRL---PLEISGGERQRVAIARAM 156
Cdd:PRK15134 100 epmvslnpLHTLekqLYEVLSLHR--------GMRREAARGEILNCLDRVGIRQAAKRLtdyPHQLSGGERQRVMIAMAL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 931484041 157 INDPLIIFADEPTGNLDEENTNKLLDVFGSLKSE-GRTIILVTHSVDISK 205
Cdd:PRK15134 172 LTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVR 221
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
19-199 |
2.86e-19 |
|
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: 81.80 E-value: 2.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 19 EVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLD--RPTDGKVVFDSVDVfshddTRLS--EIRNKKMGFVFQfhhl 94
Cdd:cd03217 14 EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDI-----TDLPpeERARLGIFLAFQ---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 95 laeftclENVALPALVNGsaqnkayrraqDLLDKFDIGdkknrlpleISGGERQRVAIARAMINDPLIIFADEPTGNLDE 174
Cdd:cd03217 85 -------YPPEIPGVKNA-----------DFLRYVNEG---------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI 137
|
170 180
....*....|....*....|....*
gi 931484041 175 ENTNKLLDVFGSLKSEGRTIILVTH 199
Cdd:cd03217 138 DALRLVAEVINKLREEGKSVLIITH 162
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
14-199 |
4.45e-19 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 84.93 E-value: 4.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 14 ENETIE---VLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTD--GKVVFDsvdvfshdDTRLSEIRNKKMGFV 88
Cdd:PLN03211 74 ETRQIQertILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILAN--------NRKPTKQILKRTGFV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 89 FQFHHLLAEFTCLEN---VALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLE-----ISGGERQRVAIARAMINDP 160
Cdd:PLN03211 146 TQDDILYPHLTVRETlvfCSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINP 225
|
170 180 190
....*....|....*....|....*....|....*....
gi 931484041 161 LIIFADEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTH 199
Cdd:PLN03211 226 SLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMH 264
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
19-169 |
4.47e-19 |
|
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: 82.19 E-value: 4.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 19 EVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfshddTRLS-EIRNKK-MGFVFQFHHLLA 96
Cdd:TIGR03410 14 HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDI-----TKLPpHERARAgIAYVPQGREIFP 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 931484041 97 EFTCLENVALPALVNGSAQNKayrRAQDLLDKFDI-GDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPT 169
Cdd:TIGR03410 89 RLTVEENLLTGLAALPRRSRK---IPDEIYELFPVlKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-203 |
5.09e-19 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 82.44 E-value: 5.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSKTYfleNETiEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLSei 80
Cdd:COG4604 1 MIEIKNVSKRY---GGK-VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELA-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 81 rnKKMGFVFQFHHLLAEFTCLENVALpalvnG---------SAQNKAY-RRAqdlLDKFDIGDKKNRLPLEISGGERQRV 150
Cdd:COG4604 75 --KRLAILRQENHINSRLTVRELVAF-----GrfpyskgrlTAEDREIiDEA---IAYLDLEDLADRYLDELSGGQRQRA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 931484041 151 AIARAMINDPLIIFADEPTGNLDEENTNKLLDVFGSLKSE-GRTIILVTHsvDI 203
Cdd:COG4604 145 FIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLH--DI 196
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
13-203 |
5.11e-19 |
|
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: 81.81 E-value: 5.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 13 LENETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVvfdsvdvfshddtrlseIRNKKMGFVFQFH 92
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV-----------------TVRGRVSSLLGLG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 93 H-LLAEFTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNrLPL-EISGGERQRVAIARAMINDPLIIFADEPTG 170
Cdd:cd03220 93 GgFNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFID-LPVkTYSSGMKARLAFAIATALEPDILLIDEVLA 171
|
170 180 190
....*....|....*....|....*....|...
gi 931484041 171 NLDEENTNKLLDVFGSLKSEGRTIILVTHSVDI 203
Cdd:cd03220 172 VGDAAFQEKCQRRLRELLKQGKTVILVSHDPSS 204
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
19-199 |
5.51e-19 |
|
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: 81.25 E-value: 5.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 19 EVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfshddTRLSEIRNKKMGFVFQFHHLLAEF 98
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPL-----AEQRDEPHENILYLGHLPGLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 99 TCLENVALPALVNGSAQnkayRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLDEENTN 178
Cdd:TIGR01189 89 SALENLHFWAAIHGGAQ----RTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVA 164
|
170 180
....*....|....*....|.
gi 931484041 179 KLLDVFGSLKSEGRTIILVTH 199
Cdd:TIGR01189 165 LLAGLLRAHLARGGIVLLTTH 185
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-220 |
6.18e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 82.05 E-value: 6.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSKTYFLEN------------------ETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKV 62
Cdd:COG1134 4 MIEVENVSKSYRLYHepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 63 vfdsvdvfshddtrlseIRNKKMGFVFQ----FHhllAEFTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNrL 138
Cdd:COG1134 84 -----------------EVNGRVSALLElgagFH---PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFID-Q 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 139 PLEI-SGGERQRVAIARAMINDP--LIIfaDEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTHSVD-ISKFGSHVYKLK 214
Cdd:COG1134 143 PVKTySSGMRARLAFAVATAVDPdiLLV--DEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGaVRRLCDRAIWLE 220
|
....*.
gi 931484041 215 ERELHA 220
Cdd:COG1134 221 KGRLVM 226
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-217 |
8.32e-19 |
|
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: 79.41 E-value: 8.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 2 LQASTVSKTYflENETIevLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHddtrlseir 81
Cdd:cd03221 1 IELENLSKTY--GGKLL--LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGY--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 82 nkkmgfvfqFHHLlaeftclenvalpalvngsaqnkayrraqdlldkfdigdkknrlpleiSGGERQRVAIARAMINDPL 161
Cdd:cd03221 68 ---------FEQL------------------------------------------------SGGEKMRLALAKLLLENPN 90
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 931484041 162 IIFADEPTGNLDEENTNKLLDVfgsLKSEGRTIILVTHSVD-ISKFGSHVYKLKERE 217
Cdd:cd03221 91 LLLLDEPTNHLDLESIEALEEA---LKEYPGTVILVSHDRYfLDQVATKIIELEDGK 144
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
20-216 |
9.62e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 84.09 E-value: 9.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 20 VLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSL--------DRPTDGKVVF-------------------DSVDvfSH 72
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLwpygsgriARPAGARVLFlpqrpylplgtlreallypATAE--AF 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 73 DDTRLSEIrnkkmgfvfqfhhllaeftcLENVALPALVngsaqnkayrraqDLLDkfDIGDKKNRLpleiSGGERQRVAI 152
Cdd:COG4178 456 SDAELREA--------------------LEAVGLGHLA-------------ERLD--EEADWDQVL----SLGEQQRLAF 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 931484041 153 ARAMINDPLIIFADEPTGNLDEENTNKLLDVfgsLKSE--GRTIILVTHSVDISKFGSHVYKLKER 216
Cdd:COG4178 497 ARLLLHKPDWLFLDEATSALDEENEAALYQL---LREElpGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-199 |
1.49e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 83.34 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 2 LQASTVSKTYflENETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLseiR 81
Cdd:PRK11160 339 LTLNNVSFTY--PDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAL---R 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 82 NkKMGFVFQFHHLLAEfTCLENValpALVNGSAQNKAYRRA------QDLLDKFD-----IGDKKNRLpleiSGGERQRV 150
Cdd:PRK11160 414 Q-AISVVSQRVHLFSA-TLRDNL---LLAAPNASDEALIEVlqqvglEKLLEDDKglnawLGEGGRQL----SGGEQRRL 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 931484041 151 AIARAMINDPLIIFADEPTGNLDEENTNKLLDVFGSLkSEGRTIILVTH 199
Cdd:PRK11160 485 GIARALLHDAPLLLLDEPTEGLDAETERQILELLAEH-AQNKTVLMITH 532
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
12-213 |
3.61e-18 |
|
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: 78.35 E-value: 3.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 12 FLENETIEVLQGVNLLvskgsfvvILGPSGSGKSTLLNILSSL--------DRPTDGkvvfdsvDVFshddtrlseirnk 83
Cdd:cd03223 16 LLKDLSFEIKPGDRLL--------ITGPSGTGKSSLFRALAGLwpwgsgriGMPEGE-------DLL------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 84 kmgFVFQfHHLLAEFTCLENVALPAlvngsaqnkayrraQDLLdkfdigdkknrlpleiSGGERQRVAIARAMINDPLII 163
Cdd:cd03223 68 ---FLPQ-RPYLPLGTLREQLIYPW--------------DDVL----------------SGGEQQRLAFARLLLHKPKFV 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 931484041 164 FADEPTGNLDEENTNKLLDVfgsLKSEGRTIILVTHSVDISKFGSHVYKL 213
Cdd:cd03223 114 FLDEATSALDEESEDRLYQL---LKELGITVISVGHRPSLWKFHDRVLDL 160
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
24-199 |
4.60e-18 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 82.24 E-value: 4.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 24 VNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLseirNKKMGFVFQFHHLLAEfTCLEN 103
Cdd:TIGR01192 354 VSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESL----RKSIATVFQDAGLFNR-SIREN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 104 VAL-------PALVNGSAQNKAYRRAQDLLDKFD--IGDKKNRLpleiSGGERQRVAIARAMINDPLIIFADEPTGNLDE 174
Cdd:TIGR01192 429 IRLgregatdEEVYEAAKAAAAHDFILKRSNGYDtlVGERGNRL----SGGERQRLAIARAILKNAPILVLDEATSALDV 504
|
170 180
....*....|....*....|....*
gi 931484041 175 ENTNKLLDVFGSLkSEGRTIILVTH 199
Cdd:TIGR01192 505 ETEARVKNAIDAL-RKNRTTFIIAH 528
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-202 |
1.04e-17 |
|
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: 81.02 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSKTYflenETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLdRPT---DGKVVFDSVDVFShddTRL 77
Cdd:TIGR02633 1 LLEMKGIVKTF----GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHgtwDGEIYWSGSPLKA---SNI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 78 SEIRNKKMGFVFQFHHLLAEFTCLENVAL--PALVNGS--AQNKAYRRAQDLLDKFDIGDKKNRLPL-EISGGERQRVAI 152
Cdd:TIGR02633 73 RDTERAGIVIIHQELTLVPELSVAENIFLgnEITLPGGrmAYNAMYLRAKNLLRELQLDADNVTRPVgDYGGGQQQLVEI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 931484041 153 ARAMINDPLIIFADEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTHSVD 202
Cdd:TIGR02633 153 AKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLN 202
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
20-202 |
1.06e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 79.46 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 20 VLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLSEIRNKkMGFVFQF-HHLLAEF 98
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTVWDIREK-VGIVFQNpDNQFVGA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 99 TCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLDEENTN 178
Cdd:PRK13640 101 TVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKE 180
|
170 180
....*....|....*....|....*
gi 931484041 179 KLLDVFGSLKSE-GRTIILVTHSVD 202
Cdd:PRK13640 181 QILKLIRKLKKKnNLTVISITHDID 205
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
19-200 |
1.16e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 77.99 E-value: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 19 EVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfshDDTRLSEirnkkmgfvfQFHHL---- 94
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI---DDPDVAE----------ACHYLghrn 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 95 --LAEFTCLENVALPALVNGSAQnkayRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMI-NDPLIIFaDEPTGN 171
Cdd:PRK13539 83 amKPALTVAENLEFWAAFLGGEE----LDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVsNRPIWIL-DEPTAA 157
|
170 180
....*....|....*....|....*....
gi 931484041 172 LDEENTNKLLDVFGSLKSEGRTIILVTHS 200
Cdd:PRK13539 158 LDAAAVALFAELIRAHLAQGGIVIAATHI 186
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
20-199 |
1.17e-17 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 77.92 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 20 VLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfshDDTRLSEIRNkkMGFVFQFHHLLAEFT 99
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL---DFQRDSIARG--LLYLGHAPGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 100 CLENVALPALVNGSAQnkayrrAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLDEENTNK 179
Cdd:cd03231 90 VLENLRFWHADHSDEQ------VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
|
170 180
....*....|....*....|
gi 931484041 180 LLDVFGSLKSEGRTIILVTH 199
Cdd:cd03231 164 FAEAMAGHCARGGMVVLTTH 183
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
14-202 |
1.33e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 79.01 E-value: 1.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 14 ENETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSvDVFSHDDtrLSEIRnKKMGFVFQF-H 92
Cdd:PRK13650 16 EDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG-DLLTEEN--VWDIR-HKIGMVFQNpD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 93 HLLAEFTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNL 172
Cdd:PRK13650 92 NQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSML 171
|
170 180 190
....*....|....*....|....*....|.
gi 931484041 173 DEENTNKLLDVFGSLKSE-GRTIILVTHSVD 202
Cdd:PRK13650 172 DPEGRLELIKTIKGIRDDyQMTVISITHDLD 202
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
21-199 |
4.58e-17 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 79.29 E-value: 4.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 21 LQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfshDDTRLSEIRNKkMGFVFQFHHLLAEfTC 100
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL---RDYTLASLRNQ-VALVSQNVHLFND-TI 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 101 LENVALpalvngsAQNKAYRRAQ-----------DLLDKFD------IGDKKNRLpleiSGGERQRVAIARAMINDPLII 163
Cdd:PRK11176 434 ANNIAY-------ARTEQYSREQieeaarmayamDFINKMDngldtvIGENGVLL----SGGQRQRIAIARALLRDSPIL 502
|
170 180 190
....*....|....*....|....*....|....*.
gi 931484041 164 FADEPTGNLDEENTNKLLDVFGSLKSEgRTIILVTH 199
Cdd:PRK11176 503 ILDEATSALDTESERAIQAALDELQKN-RTSLVIAH 537
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
19-199 |
5.44e-17 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 76.64 E-value: 5.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 19 EVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLD--RPTDGKVVFDSVDVfshddTRLS-EIRNKK-MGFVFQ---- 90
Cdd:COG0396 14 EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDI-----LELSpDERARAgIFLAFQypve 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 91 -----FHHLLAefTCLENVALPALVNGSAQNKAYRRAQDL-LDKfdigDKKNRlplEI----SGGERQRVAIARAMINDP 160
Cdd:COG0396 89 ipgvsVSNFLR--TALNARRGEELSAREFLKLLKEKMKELgLDE----DFLDR---YVnegfSGGEKKRNEILQMLLLEP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 931484041 161 -LIIFaDEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTH 199
Cdd:COG0396 160 kLAIL-DETDSGLDIDALRIVAEGVNKLRSPDRGILIITH 198
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
21-220 |
8.16e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 76.42 E-value: 8.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 21 LQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLdRPTDGKVVFDSVDVFSHDDTRLSEIR-----NKKMGFVFQFHHLL 95
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAELARHRaylsqQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 96 AeftclenVALPALVNGSAQNKAyrrAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAM------INDP--LIIFaDE 167
Cdd:COG4138 91 A-------LHQPAGASSEAVEQL---LAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwptINPEgqLLLL-DE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 931484041 168 PTGNLDEENTNKLLDVFGSLKSEGRTIILVTHsvDIS---KFGSHVYKLKERELHA 220
Cdd:COG4138 160 PMNSLDVAQQAALDRLLRELCQQGITVVMSSH--DLNhtlRHADRVWLLKQGKLVA 213
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-220 |
8.46e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 76.58 E-value: 8.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 19 EVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSvDVFSHDDTRLSEIRnKKMGFVFQFHHLLAEF 98
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQG-KPLDYSKRGLLALR-QQVATVFQDPEQQIFY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 99 TCLENVALPALVN-GSAQNKAYRRAQDLLDKFDIGDKKNRlPLE-ISGGERQRVAIARAMINDPLIIFADEPTGNLDEEN 176
Cdd:PRK13638 93 TDIDSDIAFSLRNlGVPEAEITRRVDEALTLVDAQHFRHQ-PIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAG 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 931484041 177 TNKLLDVFGSLKSEGRTIILVTHSVD-ISKFGSHVYKLKERELHA 220
Cdd:PRK13638 172 RTQMIAIIRRIVAQGNHVIISSHDIDlIYEISDAVYVLRQGQILT 216
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-201 |
1.11e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 76.09 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 2 LQASTVSKTYflenETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfshDDTRLSEIR 81
Cdd:PRK10895 4 LTAKNLAKAY----KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDI---SLLPLHARA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 82 NKKMGFVFQFHHLLAEFTCLENV-ALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDP 160
Cdd:PRK10895 77 RRGIGYLPQEASIFRRLSVYDNLmAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 931484041 161 LIIFADEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTHSV 201
Cdd:PRK10895 157 KFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNV 197
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-199 |
2.39e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 77.03 E-value: 2.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSKTYflenETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVvfdsvdvfshddtRLSEi 80
Cdd:COG0488 315 VLELEGLSKSY----GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV-------------KLGE- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 81 rNKKMGFVFQFHHLL-AEFTCLENVAlpalvnGSAQNKAYRRAQDLLDKFDI-GDKKNRLPLEISGGERQRVAIARAMIN 158
Cdd:COG0488 377 -TVKIGYFDQHQEELdPDKTVLDELR------DGAPGGTEQEVRGYLGRFLFsGDDAFKPVGVLSGGEKARLALAKLLLS 449
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 931484041 159 DP-LIIFaDEPTGNLDEENTNKLLDvfgSLKS-EGrTIILVTH 199
Cdd:COG0488 450 PPnVLLL-DEPTNHLDIETLEALEE---ALDDfPG-TVLLVSH 487
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
18-218 |
3.09e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 75.51 E-value: 3.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 18 IEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLseirNKKMGFVFQF-HHLLA 96
Cdd:PRK13642 20 VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNL----RRKIGMVFQNpDNQFV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 97 EFTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLDEEN 176
Cdd:PRK13642 96 GATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 931484041 177 TNKLLDVFGSLKSEGR-TIILVTHSVDISKFGSHVYKLKEREL 218
Cdd:PRK13642 176 RQEIMRVIHEIKEKYQlTVLSITHDLDEAASSDRILVMKAGEI 218
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
14-199 |
4.00e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 75.51 E-value: 4.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 14 ENETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGkvvfdSVDVFSHDDTRLsEIRN-KKMGFVF-QF 91
Cdd:COG4586 31 EYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSG-----EVRVLGYVPFKR-RKEFaRRIGVVFgQR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 92 HHLLAEFTCLENVALPALVNGsAQNKAYRRAQDLLDK-FDIGDKKNRlPL-EISGGERQRVAIARAMINDPLIIFADEPT 169
Cdd:COG4586 105 SQLWWDLPAIDSFRLLKAIYR-IPDAEYKKRLDELVElLDLGELLDT-PVrQLSLGQRMRCELAAALLHRPKILFLDEPT 182
|
170 180 190
....*....|....*....|....*....|.
gi 931484041 170 GNLDEENTNKLLDVFGSL-KSEGRTIILVTH 199
Cdd:COG4586 183 IGLDVVSKEAIREFLKEYnRERGTTILLTSH 213
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-210 |
5.37e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 75.86 E-value: 5.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSKTYflenETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGkvvfdSVDVFSHDDTRLSEI 80
Cdd:PRK15439 11 LLCARSISKQY----SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSG-----TLEIGGNPCARLTPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 81 RNKKMG--FVFQFHHLLAEFTCLENValpaLVNGSAQNKAYRRAQDLLDKFDIgdkknRLPLEISGG-----ERQRVAIA 153
Cdd:PRK15439 82 KAHQLGiyLVPQEPLLFPNLSVKENI----LFGLPKRQASMQKMKQLLAALGC-----QLDLDSSAGslevaDRQIVEIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 931484041 154 RAMINDPLIIFADEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTHSV-DISKFGSHV 210
Cdd:PRK15439 153 RGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLpEIRQLADRI 210
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
28-199 |
5.64e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 75.16 E-value: 5.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 28 VSKGSFVVILGPSGSGKS-TLLNILSSLDRPtdGKVVFDSVDVFSHDDTRLSEIRNKK-----MGFVFQ--FHHLLAEFT 99
Cdd:PRK11022 30 VKQGEVVGIVGESGSGKSvSSLAIMGLIDYP--GRVMAEKLEFNGQDLQRISEKERRNlvgaeVAMIFQdpMTSLNPCYT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 100 CLENVaLPALVNGSAQNKAYR--RAQDLLDKFDIGDKKNRL---PLEISGGERQRVAIARAMINDPLIIFADEPTGNLDE 174
Cdd:PRK11022 108 VGFQI-MEAIKVHQGGNKKTRrqRAIDLLNQVGIPDPASRLdvyPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDV 186
|
170 180
....*....|....*....|....*.
gi 931484041 175 ENTNKLLDVFGSL-KSEGRTIILVTH 199
Cdd:PRK11022 187 TIQAQIIELLLELqQKENMALVLITH 212
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-198 |
6.09e-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: 72.46 E-value: 6.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 20 VLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfshddTRLS--EIRNKKMGFVFQFHH---L 94
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPV-----TRRSprDAIRAGIAYVPEDRKregL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 95 LAEFTCLENVALPALvngsaqnkayrraqdlldkfdigdkknrlpleISGGERQRVAIARAMINDPLIIFADEPTGNLDE 174
Cdd:cd03215 90 VLDLSVAENIALSSL--------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDV 137
|
170 180
....*....|....*....|....
gi 931484041 175 ENTNKLLDVFGSLKSEGRTIILVT 198
Cdd:cd03215 138 GAKAEIYRLIRELADAGKAVLLIS 161
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-201 |
9.80e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 73.53 E-value: 9.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 16 ETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDR-----PTDGKVVFDSVDVFSHDdTRLSEIRnKKMGFVFQ 90
Cdd:PRK14258 18 DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIYERR-VNLNRLR-RQVSMVHP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 91 FHHLLAeFTCLENVAL--------PAL-VNGSAQNKAyrRAQDLLDkfDIGDKKNRLPLEISGGERQRVAIARAMINDPL 161
Cdd:PRK14258 96 KPNLFP-MSVYDNVAYgvkivgwrPKLeIDDIVESAL--KDADLWD--EIKHKIHKSALDLSGGQQQRLCIARALAVKPK 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 931484041 162 IIFADEPTGNLDEENTNKLLDVFGS--LKSEgRTIILVTHSV 201
Cdd:PRK14258 171 VLLMDEPCFGLDPIASMKVESLIQSlrLRSE-LTMVIVSHNL 211
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
24-202 |
1.20e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 74.88 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 24 VNLLVSKGSFVVILGPSGSGKSTLLNILSSLdRPTDGKVVFDSVDVFSHDdtrLSEIRnKKMGFVFQFHHLLAEfTCLEN 103
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELD---PESWR-KHLSWVGQNPQLPHG-TLRDN 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 104 VALpALVNGSAQnkayrRAQDLLDKFDIGDKKNRLPL-----------EISGGERQRVAIARAMINDPLIIFADEPTGNL 172
Cdd:PRK11174 443 VLL-GNPDASDE-----QLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASL 516
|
170 180 190
....*....|....*....|....*....|..
gi 931484041 173 DEENTNKlldVFGSLK--SEGRTIILVTHSVD 202
Cdd:PRK11174 517 DAHSEQL---VMQALNaaSRRQTTLMVTHQLE 545
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
21-202 |
2.16e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 74.20 E-value: 2.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 21 LQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLdRPT---DGKVVFDSvdvfshDDTRLSEIRN---KKMGFVFQFHHL 94
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEG------EELQASNIRDterAGIAIIHQELAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 95 LAEFTCLENVALPA-LVNGSAQN--KAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGN 171
Cdd:PRK13549 94 VKELSVLENIFLGNeITPGGIMDydAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTAS 173
|
170 180 190
....*....|....*....|....*....|.
gi 931484041 172 LDEENTNKLLDVFGSLKSEGRTIILVTHSVD 202
Cdd:PRK13549 174 LTESETAVLLDIIRDLKAHGIACIYISHKLN 204
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
21-199 |
2.35e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 74.06 E-value: 2.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 21 LQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLdRPT---DGKVVFDSvDVFSHDDTRLSEirnkKMGFVFqFHHLLA- 96
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHgsyEGEILFDG-EVCRFKDIRDSE----ALGIVI-IHQELAl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 97 --EFTCLENVALpalvnGSAQ--------NKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFAD 166
Cdd:NF040905 90 ipYLSIAENIFL-----GNERakrgvidwNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILD 164
|
170 180 190
....*....|....*....|....*....|...
gi 931484041 167 EPTGNLDEENTNKLLDVFGSLKSEGRTIILVTH 199
Cdd:NF040905 165 EPTAALNEEDSAALLDLLLELKAQGITSIIISH 197
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
7-201 |
4.03e-15 |
|
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: 71.21 E-value: 4.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 7 VSKTYFLENETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLSEIRNKKMG 86
Cdd:cd03290 3 VTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 87 FVFQFHHLLAEfTCLENVALpalvnGSAQNKAYRRAQ----------DLL---DKFDIGDKKnrlpLEISGGERQRVAIA 153
Cdd:cd03290 83 YAAQKPWLLNA-TVEENITF-----GSPFNKQRYKAVtdacslqpdiDLLpfgDQTEIGERG----INLSGGQRQRICVA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 931484041 154 RAMINDPLIIFADEPTGNLDEENTNKLLD--VFGSLKSEGRTIILVTHSV 201
Cdd:cd03290 153 RALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKL 202
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-199 |
4.14e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 73.35 E-value: 4.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSKTYFLENETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDS----------VDVF 70
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 71 SHDDTRLSEIRNKKMGFVFQ--FHHLLAEFTCLENVALPA-LVNGSAQNKAYRRAQDLLDKFDIGDKK---NRLPLEISG 144
Cdd:PRK10261 92 EQSAAQMRHVRGADMAMIFQepMTSLNPVFTVGEQIAESIrLHQGASREEAMVEAKRMLDQVRIPEAQtilSRYPHQLSG 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 931484041 145 GERQRVAIARAMINDPLIIFADEPTGNLDEENTNKLLDVFGSLKSE-GRTIILVTH 199
Cdd:PRK10261 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITH 227
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
25-199 |
4.17e-15 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 72.83 E-value: 4.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 25 NLLVSKGSFVVILGPSGSGKS----TLLNILSSLDRpTDGKVVFDSVDVFSHDDTRLSEIRNKKMGFVFQ---------- 90
Cdd:PRK09473 36 NFSLRAGETLGIVGESGSGKSqtafALMGLLAANGR-IGGSATFNGREILNLPEKELNKLRAEQISMIFQdpmtslnpym 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 91 -FHHLLAEFTCLENvalpalvnGSAQNKAYRRAQDLLDKFDIGDKKNRL---PLEISGGERQRVAIARAMINDPLIIFAD 166
Cdd:PRK09473 115 rVGEQLMEVLMLHK--------GMSKAEAFEESVRMLDAVKMPEARKRMkmyPHEFSGGMRQRVMIAMALLCRPKLLIAD 186
|
170 180 190
....*....|....*....|....*....|....
gi 931484041 167 EPTGNLDEENTNKLLDVFGSLKSEGRT-IILVTH 199
Cdd:PRK09473 187 EPTTALDVTVQAQIMTLLNELKREFNTaIIMITH 220
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-205 |
4.36e-15 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 73.62 E-value: 4.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 2 LQASTVSKTYFLENEtieVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLSEIR 81
Cdd:TIGR01193 474 IVINDVSYSYGYGSN---ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFI 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 82 NkkmgFVFQFHHLLAEfTCLENVALPALVNGSAQN--KAYRRAQ--DLLDKFDIGdKKNRLPLE---ISGGERQRVAIAR 154
Cdd:TIGR01193 551 N----YLPQEPYIFSG-SILENLLLGAKENVSQDEiwAACEIAEikDDIENMPLG-YQTELSEEgssISGGQKQRIALAR 624
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 931484041 155 AMINDPLIIFADEPTGNLDEENTNKLLDVFgsLKSEGRTIILVTHSVDISK 205
Cdd:TIGR01193 625 ALLTDSKVLILDESTSNLDTITEKKIVNNL--LNLQDKTIIFVAHRLSVAK 673
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
20-220 |
4.92e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 71.94 E-value: 4.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 20 VLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLSeirnKKMGFVFQFHHLLAEFT 99
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA----RRIGLLAQNATTPGDIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 100 CLENVA------LPALV-----NGSAQNKAYRRAqdlldkfDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEP 168
Cdd:PRK10253 98 VQELVArgryphQPLFTrwrkeDEEAVTKAMQAT-------GITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 931484041 169 TGNLDEENTNKLLDVFGSL-KSEGRTIILVTHSVDIS-KFGSHVYKLKERELHA 220
Cdd:PRK10253 171 TTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQAcRYASHLIALREGKIVA 224
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
19-202 |
6.68e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 72.75 E-value: 6.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 19 EVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfshddTRLS--EIRNKKMGFVFQ--FHH- 93
Cdd:COG3845 272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDI-----TGLSprERRRLGVAYIPEdrLGRg 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 94 LLAEFTCLENVAL-----PALVNGSAQN--KAYRRAQDLLDKFDIgdkknRLP--------LeiSGGERQRVAIARAMIN 158
Cdd:COG3845 347 LVPDMSVAENLILgryrrPPFSRGGFLDrkAIRAFAEELIEEFDV-----RTPgpdtparsL--SGGNQQKVILARELSR 419
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 931484041 159 DPLIIFADEPTGNLDEENT----NKLLDvfgsLKSEGRTIILVthSVD 202
Cdd:COG3845 420 DPKLLIAAQPTRGLDVGAIefihQRLLE----LRDAGAAVLLI--SED 461
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
20-202 |
7.43e-15 |
|
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: 70.60 E-value: 7.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 20 VLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfshDDTRLSEIRnKKMGFVFQFHHLLA--- 96
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDI---SKIGLHDLR-SRISIIPQDPVLFSgti 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 97 --------EFT------CLENVALPALVNGSAqnkayrraqDLLDKFDIGDKKNrlpleISGGERQRVAIARAMINDPLI 162
Cdd:cd03244 95 rsnldpfgEYSdeelwqALERVGLKEFVESLP---------GGLDTVVEEGGEN-----LSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 931484041 163 IFADEPTGNLDEENTNKLLDVfgsLKSE--GRTIILVTHSVD 202
Cdd:cd03244 161 LVLDEATASVDPETDALIQKT---IREAfkDCTVLTIAHRLD 199
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
13-199 |
8.95e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 70.88 E-value: 8.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 13 LENETIE----VLQGVNLLVSKGSFVVILGPSGSGKS----TLLNILSSLDRPTDGKVVFDSVDVfshddtRLSEIRNKK 84
Cdd:PRK10418 7 LRNIALQaaqpLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPV------APCALRGRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 85 MGFVFQfhHLLAEFTCLENVALPALVNGSAQNKAYRRAQ--DLLDKFDIGDKKNRL---PLEISGGERQRVAIARAMIND 159
Cdd:PRK10418 81 IATIMQ--NPRSAFNPLHTMHTHARETCLALGKPADDATltAALEAVGLENAARVLklyPFEMSGGMLQRMMIALALLCE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 931484041 160 PLIIFADEPTGNLDEENTNKLLDVFGSL-KSEGRTIILVTH 199
Cdd:PRK10418 159 APFIIADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTH 199
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
20-203 |
1.09e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 72.05 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 20 VLQGVNLLVSKGSFVVILGPSGSGKST----LLNILSSldrptDGKVVFDSVDVFSHDDTRLSEIRnKKMGFVFQ--FHH 93
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQPLHNLNRRQLLPVR-HRIQVVFQdpNSS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 94 LLAEFTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIG---DKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTG 170
Cdd:PRK15134 375 LNPRLNVLQIIEEGLRVHQPTLSAAQREQQVIAVMEEVGldpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
|
170 180 190
....*....|....*....|....*....|....
gi 931484041 171 NLDEENTNKLLDVFGSLKSEGR-TIILVTHSVDI 203
Cdd:PRK15134 455 SLDKTVQAQILALLKSLQQKHQlAYLFISHDLHV 488
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
17-205 |
1.13e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 71.66 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 17 TIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLSEIRnKKMGFVFQ--FHHL 94
Cdd:PRK15079 33 TLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVR-SDIQMIFQdpLASL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 95 LAEFTCLENVALPAlvngsaqnKAYR---RAQDLLDKFDIGDKK--------NRLPLEISGGERQRVAIARAMINDPLII 163
Cdd:PRK15079 112 NPRMTIGEIIAEPL--------RTYHpklSRQEVKDRVKAMMLKvgllpnliNRYPHEFSGGQCQRIGIARALILEPKLI 183
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 931484041 164 FADEPTGNLDEENTNKLLDVFGSLKSE-GRTIILVTHSVDISK 205
Cdd:PRK15079 184 ICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVK 226
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
19-199 |
1.54e-14 |
|
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: 71.77 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 19 EVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfshDDTRLSEIRnKKMGFVFQ----FHHl 94
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDI---RDVTQASLR-AAIGIVPQdtvlFND- 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 95 laefTCLENVALPALVNGSAQ-NKAYRRAQdlldkfdIGDKKNRLP-----------LEISGGERQRVAIARAMINDPLI 162
Cdd:COG5265 447 ----TIAYNIAYGRPDASEEEvEAAARAAQ-------IHDFIESLPdgydtrvgergLKLSGGEKQRVAIARTLLKNPPI 515
|
170 180 190
....*....|....*....|....*....|....*....
gi 931484041 163 IFADEPTGNLDEEnTNKllDVFGSLK--SEGRTIILVTH 199
Cdd:COG5265 516 LIFDEATSALDSR-TER--AIQAALRevARGRTTLVIAH 551
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-199 |
2.10e-14 |
|
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: 71.50 E-value: 2.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 7 VSKTYfleNETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGK------------------------- 61
Cdd:TIGR03719 10 VSKVV---PPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEarpqpgikvgylpqepqldptktvr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 62 -VVFDSVDVFSHDDTRLSEIRNKKMGFVFQFHHLLAEFTCLENVAlpalvngSAQNkayrrAQDLLDKFDIGDKKNRLP- 139
Cdd:TIGR03719 87 eNVEEGVAEIKDALDRFNEISAKYAEPDADFDKLAAEQAELQEII-------DAAD-----AWDLDSQLEIAMDALRCPp 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 931484041 140 -----LEISGGERQRVAIARAMINDPLIIFADEPTGNLDEENT----NKLLDVFGslksegrTIILVTH 199
Cdd:TIGR03719 155 wdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVawleRHLQEYPG-------TVVAVTH 216
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-199 |
2.19e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 71.19 E-value: 2.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSKTYflenETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfSHDDTRLSEi 80
Cdd:PRK10762 4 LLQLKGIDKAF----PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEV-TFNGPKSSQ- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 81 rNKKMGFVFQFHHLLAEFTCLENVALP-ALVN--GSAQ-NKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAM 156
Cdd:PRK10762 78 -EAGIGIIHQELNLIPQLTIAENIFLGrEFVNrfGRIDwKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 931484041 157 INDPLIIFADEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTH 199
Cdd:PRK10762 157 SFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISH 199
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
2-205 |
6.25e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 68.71 E-value: 6.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 2 LQASTVSKTY-----FLENETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDV-FSHDDT 75
Cdd:COG4167 5 LEVRNLSKTFkyrtgLFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLeYGDYKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 76 RLSEIRnkkMgfVFQFhhllaeftclENVAL-PALVNGSAQNKAYRRAQDLLDK------FDI-------GDKKNRLPLE 141
Cdd:COG4167 85 RCKHIR---M--IFQD----------PNTSLnPRLNIGQILEEPLRLNTDLTAEereeriFATlrlvgllPEHANFYPHM 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 931484041 142 ISGGERQRVAIARAMINDPLIIFADEPTGNLDEENTNKLLDVFGSLKSE-GRTIILVTHSVDISK 205
Cdd:COG4167 150 LSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKlGISYIYVSQHLGIVK 214
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-201 |
6.80e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 68.97 E-value: 6.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 20 VLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDG-----KVVFDSVDVFSHDDtrLSEIRnKKMGFVFQFHHL 94
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRD--VLEFR-RRVGMLFQRPNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 95 LAeFTCLENVALPALVNGSAQNKAYRR-AQDLLDKFDIGDK-KNRL---PLEISGGERQRVAIARAMINDPLIIFADEPT 169
Cdd:PRK14271 113 FP-MSIMDNVLAGVRAHKLVPRKEFRGvAQARLTEVGLWDAvKDRLsdsPFRLSGGQQQLLCLARTLAVNPEVLLLDEPT 191
|
170 180 190
....*....|....*....|....*....|..
gi 931484041 170 GNLDEENTNKLLDVFGSLkSEGRTIILVTHSV 201
Cdd:PRK14271 192 SALDPTTTEKIEEFIRSL-ADRLTVIIVTHNL 222
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
14-203 |
2.25e-13 |
|
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: 66.11 E-value: 2.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 14 ENETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSslDRPTDGKVVFDSvdvfSHDDTRLSEIRNKKMGFVFQFHH 93
Cdd:cd03232 16 KGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLA--GRKTAGVITGEI----LINGRPLDKNFQRSTGYVEQQDV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 94 LLAEFTCLENVALPALVNGsaqnkayrraqdlldkfdigdkknrlpleISGGERQRVAIARAMINDPLIIFADEPTGNLD 173
Cdd:cd03232 90 HSPNLTVREALRFSALLRG-----------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
170 180 190
....*....|....*....|....*....|..
gi 931484041 174 EENTNKLLDVFGSLKSEGRTIILVTH--SVDI 203
Cdd:cd03232 141 SQAAYNIVRFLKKLADSGQAILCTIHqpSASI 172
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
18-202 |
3.65e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.83 E-value: 3.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 18 IEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfshDDTRLSEIRNKKMGFVFQFHHLLAE 97
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI---DFKSSKEALENGISMVHQELNLVLQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 98 FTCLENVAL---PALVNGSAQNKAYRRAQDLLDKFDIG-DKKNRLPlEISGGERQRVAIARAMINDPLIIFADEPTGNLD 173
Cdd:PRK10982 88 RSVMDNMWLgryPTKGMFVDQDKMYRDTKAIFDELDIDiDPRAKVA-TLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLT 166
|
170 180
....*....|....*....|....*....
gi 931484041 174 EENTNKLLDVFGSLKSEGRTIILVTHSVD 202
Cdd:PRK10982 167 EKEVNHLFTIIRKLKERGCGIVYISHKME 195
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
15-199 |
6.69e-13 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 66.47 E-value: 6.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 15 NETIEVLQGVNLLVSKGSFVVILGPSGSGKS----TLLNILSSLDRPTDGKVVFDSVDVfshddTRLS-----EIRNKKM 85
Cdd:COG4170 17 QGRVKAVDRVSLTLNEGEIRGLVGESGSGKSliakAICGITKDNWHVTADRFRWNGIDL-----LKLSprerrKIIGREI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 86 GFVFQfhhllAEFTCLENVA------LPALVNGSAQNK-------AYRRAQDLLDKFDIGDKK---NRLPLEISGGERQR 149
Cdd:COG4170 92 AMIFQ-----EPSSCLDPSAkigdqlIEAIPSWTFKGKwwqrfkwRKKRAIELLHRVGIKDHKdimNSYPHELTEGECQK 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 931484041 150 VAIARAMINDPLIIFADEPTGNLDEENTNKLLDVFGSL-KSEGRTIILVTH 199
Cdd:COG4170 167 VMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLnQLQGTSILLISH 217
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-175 |
6.94e-13 |
|
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: 65.51 E-value: 6.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 26 LLVSKGSF-----VVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfshdDTRLSEIRNKKMGFVFQFhhllaeftc 100
Cdd:cd03237 15 LEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV----SYKPQYIKADYEGTVRDL--------- 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 931484041 101 lenvaLPALVNGSAQNKAYRraQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLDEE 175
Cdd:cd03237 82 -----LSSITKDFYTHPYFK--TEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVE 149
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
31-209 |
8.52e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 66.80 E-value: 8.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 31 GSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLSEIRnKKMGFVFQ--FHHLLAEFTCLENVALPA 108
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALR-RDIQFIFQdpYASLDPRQTVGDSIMEPL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 109 LVNGSAQNK-AYRRAQDLLDKfdIGDKKN---RLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLDEENTNKLLDVF 184
Cdd:PRK10261 429 RVHGLLPGKaAAARVAWLLER--VGLLPEhawRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLL 506
|
170 180
....*....|....*....|....*.
gi 931484041 185 GSLKSE-GRTIILVTHSVDISKFGSH 209
Cdd:PRK10261 507 LDLQRDfGIAYLFISHDMAVVERISH 532
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
20-199 |
9.14e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 65.14 E-value: 9.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 20 VLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVfdsvdvfshddtRLSEIRnkkMGFVFQFHHLlaeft 99
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK------------RNGKLR---IGYVPQKLYL----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 100 cleNVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRL--PLE-ISGGERQRVAIARAMINDPLIIFADEPTGNLDEEN 176
Cdd:PRK09544 79 ---DTTLPLTVNRFLRLRPGTKKEDILPALKRVQAGHLIdaPMQkLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNG 155
|
170 180
....*....|....*....|....
gi 931484041 177 TNKLLDVFGSLKSE-GRTIILVTH 199
Cdd:PRK09544 156 QVALYDLIDQLRRElDCAVLMVSH 179
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
18-217 |
2.62e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 65.44 E-value: 2.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 18 IEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDsvDVFSHDDTRLSEIRNKkMGFVFQfHHLLAE 97
Cdd:PTZ00265 398 VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKDINLKWWRSK-IGVVSQ-DPLLFS 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 98 FTCLENVA--------LPALVNGSAQN--------------------------------------KAYRRAQD------- 124
Cdd:PTZ00265 474 NSIKNNIKyslyslkdLEALSNYYNEDgndsqenknkrnscrakcagdlndmsnttdsneliemrKNYQTIKDsevvdvs 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 125 -----------LLDKFD--IGDKKNRLpleiSGGERQRVAIARAMINDPLIIFADEPTGNLDEENTNKLLDVFGSLK-SE 190
Cdd:PTZ00265 554 kkvlihdfvsaLPDKYEtlVGSNASKL----SGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNE 629
|
250 260
....*....|....*....|....*..
gi 931484041 191 GRTIILVTHSVDISKFGSHVYKLKERE 217
Cdd:PTZ00265 630 NRITIIIAHRLSTIRYANTIFVLSNRE 656
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
19-199 |
2.72e-12 |
|
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: 63.20 E-value: 2.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 19 EVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLSEirnkKMGFVFQFhhllaef 98
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS----SLTIIPQD------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 99 tclenvalPALVNGSAQNKayrraqdlLDKFD-IGDKKNRLPLEISG-------GERQRVAIARAMINDPLIIFADEPTG 170
Cdd:cd03369 91 --------PTLFSGTIRSN--------LDPFDeYSDEEIYGALRVSEgglnlsqGQRQLLCLARALLKRPRVLVLDEATA 154
|
170 180
....*....|....*....|....*....
gi 931484041 171 NLDEENTNKLLDVFGSLKSeGRTIILVTH 199
Cdd:cd03369 155 SIDYATDALIQKTIREEFT-NSTILTIAH 182
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
21-201 |
2.76e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 64.13 E-value: 2.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 21 LQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfshddtrLSEIRNKKMGFVFQFHHLLAEFTC 100
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT-------RQALQKNLVAYVPQSEEVDWSFPV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 101 L-ENVALPA-------LVNGSAQNKAyrRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNL 172
Cdd:PRK15056 96 LvEDVVMMGryghmgwLRRAKKRDRQ--IVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGV 173
|
170 180
....*....|....*....|....*....
gi 931484041 173 DEENTNKLLDVFGSLKSEGRTIILVTHSV 201
Cdd:PRK15056 174 DVKTEARIISLLRELRDEGKTMLVSTHNL 202
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
22-214 |
2.87e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 63.28 E-value: 2.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 22 QGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDtrlseirnkkmgfvfQFHHLLA----- 96
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRD---------------EYHQDLLylghq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 97 -----EFTCLENVAlpalvngsaqnkAYRRAQDLLDKFDIGDKKNRLPLE---------ISGGERQRVAIARAMINDPLI 162
Cdd:PRK13538 83 pgiktELTALENLR------------FYQRLHGPGDDEALWEALAQVGLAgfedvpvrqLSAGQQRRVALARLWLTRAPL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 931484041 163 IFADEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTHSvDISKFGSHVYKLK 214
Cdd:PRK13538 151 WILDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTHQ-DLPVASDKVRKLR 201
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-205 |
4.79e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 63.66 E-value: 4.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSKTY-----FLENETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFdsvdvfshDDT 75
Cdd:PRK15112 4 LLEVRNLSKTFryrtgWFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLI--------DDH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 76 RLS----EIRNKKMGFVFQ-----------FHHLLaEFTCLENVALPALVNGSAQNKAYRRAQDLldkfdiGDKKNRLPL 140
Cdd:PRK15112 76 PLHfgdySYRSQRIRMIFQdpstslnprqrISQIL-DFPLRLNTDLEPEQREKQIIETLRQVGLL------PDHASYYPH 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 931484041 141 EISGGERQRVAIARAMINDPLIIFADEPTGNLDEENTNKLLDVFGSLKSE-GRTIILVTHSVDISK 205
Cdd:PRK15112 149 MLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMK 214
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
12-217 |
5.54e-12 |
|
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: 62.24 E-value: 5.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 12 FLENETIEVLQGVNLLVskgsfvvilGPSGSGKSTLLN-ILSSL--DRPTDGKVVFDSVDVFSHDDTR------LSEIRN 82
Cdd:cd03240 12 FHERSEIEFFSPLTLIV---------GQNGAGKTTIIEaLKYALtgELPPNSKGGAHDPKLIREGEVRaqvklaFENANG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 83 KKMgfvfqfhHLLAEFTCLENVAlpalvngsaqnkaYRRaQDLLDKFdigdkknrLPLEI---SGGERQ------RVAIA 153
Cdd:cd03240 83 KKY-------TITRSLAILENVI-------------FCH-QGESNWP--------LLDMRgrcSGGEKVlasliiRLALA 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 931484041 154 RAMINDPLIIFADEPTGNLDEEN-TNKLLDVFGSLKSEG-RTIILVTHSVDISKFGSHVYKLKERE 217
Cdd:cd03240 134 ETFGSNCGILALDEPTTNLDEENiEESLAEIIEERKSQKnFQLIVITHDEELVDAADHIYRVEKDG 199
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
98-216 |
5.89e-12 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 63.99 E-value: 5.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 98 FTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLDEENT 177
Cdd:NF000106 101 FSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTR 180
|
90 100 110
....*....|....*....|....*....|....*....
gi 931484041 178 NKLLDVFGSLKSEGRTIILVTHSVDISKFGSHVYKLKER 216
Cdd:NF000106 181 NEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDR 219
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
28-202 |
6.90e-12 |
|
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: 64.26 E-value: 6.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 28 VSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFshddTRLSEIrNKKMGFVFQFHHLLAEFTCLENVALP 107
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL----TNISDV-HQNMGYCPQFDAIDDLLTGREHLYLY 2036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 108 ALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLDEENTNKLLDVFGSL 187
Cdd:TIGR01257 2037 ARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSI 2116
|
170
....*....|....*
gi 931484041 188 KSEGRTIILVTHSVD 202
Cdd:TIGR01257 2117 IREGRAVVLTSHSME 2131
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-199 |
7.01e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.98 E-value: 7.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 7 VSKTYfleNETIEVLQGVNLlvskgSF-----VVILGPSGSGKSTLLNILSSLDRPTDGkvvfdsvdvfshdDTRLSEir 81
Cdd:PRK11819 12 VSKVV---PPKKQILKDISL-----SFfpgakIGVLGLNGAGKSTLLRIMAGVDKEFEG-------------EARPAP-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 82 NKKMGFVFQFHHLLAEFTCLENV--ALPALVNGSAQ----NKAYR--------------RAQDLLDKFDIGDKKNRLplE 141
Cdd:PRK11819 69 GIKVGYLPQEPQLDPEKTVRENVeeGVAEVKAALDRfneiYAAYAepdadfdalaaeqgELQEIIDAADAWDLDSQL--E 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 931484041 142 I-----------------SGGERQRVAIARAMINDPLIIFADEPTGNLDEENTNkLLDVFgsLKSEGRTIILVTH 199
Cdd:PRK11819 147 IamdalrcppwdakvtklSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVA-WLEQF--LHDYPGTVVAVTH 218
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
24-199 |
2.12e-11 |
|
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: 62.51 E-value: 2.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 24 VNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfshDDTRLSEIRNKkmgF--VFQFHHLLAEFTCL 101
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV---TADNREAYRQL---FsaVFSDFHLFDRLLGL 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 102 ENVALPAlvngsaqnkayrRAQDLLDKFDIGDK----KNRL-PLEISGGERQRVAIARAMIND-PLIIFaDE------PT 169
Cdd:COG4615 425 DGEADPA------------RARELLERLELDHKvsveDGRFsTTDLSQGQRKRLALLVALLEDrPILVF-DEwaadqdPE 491
|
170 180 190
....*....|....*....|....*....|....*
gi 931484041 170 gnldeentnkLLDVF-----GSLKSEGRTIILVTH 199
Cdd:COG4615 492 ----------FRRVFytellPELKARGKTVIAISH 516
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
19-198 |
2.88e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 61.96 E-value: 2.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 19 EVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfSHDDTR---------LSEIRnKKMGfvf 89
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPV-RIRSPRdairagiayVPEDR-KGEG--- 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 90 qfhhLLAEFTCLENVALPALVNGSA-----QNKAYRRAQDLLDKFDIgdKKNRLPLEI---SGGERQRVAIARAMINDPL 161
Cdd:COG1129 341 ----LVLDLSIRENITLASLDRLSRgglldRRRERALAEEYIKRLRI--KTPSPEQPVgnlSGGNQQKVVLAKWLATDPK 414
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 931484041 162 IIFADEPTGNLD----EEntnkLLDVFGSLKSEGRTIILVT 198
Cdd:COG1129 415 VLILDEPTRGIDvgakAE----IYRLIRELAAEGKAVIVIS 451
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
20-173 |
2.93e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 62.04 E-value: 2.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 20 VLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFD--SVDVFSHDDTRlseirnKKMGFVFQFHHLLAE 97
Cdd:PRK10790 356 VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDgrPLSSLSHSVLR------QGVAMVQQDPVVLAD 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 98 fTCLENVALPALVNGSAQNKAYRRAQ--DLLDKFD------IGDKKNRLpleiSGGERQRVAIARAMINDPLIIFADEPT 169
Cdd:PRK10790 430 -TFLANVTLGRDISEEQVWQALETVQlaELARSLPdglytpLGEQGNNL----SVGQKQLLALARVLVQTPQILILDEAT 504
|
....
gi 931484041 170 GNLD 173
Cdd:PRK10790 505 ANID 508
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
21-201 |
3.03e-11 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 62.22 E-value: 3.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 21 LQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVvfdsvdvfshdDTRLSEirnkkmGFVFQFHHLLAEFTC 100
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----------DIKGSA------ALIAISSGLNGQLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 101 LENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLDEENTNKL 180
Cdd:PRK13545 103 IENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKC 182
|
170 180
....*....|....*....|.
gi 931484041 181 LDVFGSLKSEGRTIILVTHSV 201
Cdd:PRK13545 183 LDKMNEFKEQGKTIFFISHSL 203
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1-220 |
3.69e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 60.96 E-value: 3.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 1 MLQASTVSKTYF-LENETIEV-----LQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDsvdvfshdD 74
Cdd:PRK10575 1 MQEYTNHSDTTFaLRNVSFRVpgrtlLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLD--------A 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 75 TRLSEIRNKkmGFVFQFHHLLAEFTCLENVALPALVN----------GSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISG 144
Cdd:PRK10575 73 QPLESWSSK--AFARKVAYLPQQLPAAEGMTVRELVAigrypwhgalGRFGAADREKVEEAISLVGLKPLAHRLVDSLSG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 931484041 145 GERQRVAIARAMINDPLIIFADEPTGNLDEENTNKLLDVFGSLKSE-GRTIILVTHSVDI-SKFGSHVYKLKERELHA 220
Cdd:PRK10575 151 GERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMaARYCDYLVALRGGEMIA 228
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
28-199 |
6.03e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 59.86 E-value: 6.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 28 VSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDsvdvfSHDDTRLSeiRNKKMGFVFQFHHLLAEFTCLENValp 107
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQID-----GKTATRGD--RSRFMAYLGHLPGLKADLSTLENL--- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 108 ALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLDEENTNKLLDVFGS- 186
Cdd:PRK13543 104 HFLCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAh 183
|
170
....*....|...
gi 931484041 187 LKSEGRTiILVTH 199
Cdd:PRK13543 184 LRGGGAA-LVTTH 195
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
21-205 |
7.31e-11 |
|
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: 58.87 E-value: 7.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 21 LQGVNLLVSKGSFVVILGPSGSGKSTLLN-ILSSLDRptdgKVVFDSVDVFSHDDTrlseIRNKKMGFvfqfhhllaeft 99
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNeGLYASGK----ARLISFLPKFSRNKL----IFIDQLQF------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 100 cLENVALPALVNGsaqnkayRRAQDLldkfdigdkknrlpleiSGGERQRVAIARAMINDP---LIIFaDEPTGNLDEEN 176
Cdd:cd03238 71 -LIDVGLGYLTLG-------QKLSTL-----------------SGGELQRVKLASELFSEPpgtLFIL-DEPSTGLHQQD 124
|
170 180
....*....|....*....|....*....
gi 931484041 177 TNKLLDVFGSLKSEGRTIILVTHSVDISK 205
Cdd:cd03238 125 INQLLEVIKGLIDLGNTVILIEHNLDVLS 153
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
4-173 |
1.10e-10 |
|
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: 58.81 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 4 ASTVSKTYFLENETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPT---DGKVVFDSVDvfshddtrlsei 80
Cdd:cd03233 6 WRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIP------------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 81 rNKKMgfvFQFHHLLAEFTCLENVALPALVngsaqnkayrrAQDLLDkFDIGDKKNRLPLEISGGERQRVAIARAMINDP 160
Cdd:cd03233 74 -YKEF---AEKYPGEIIYVSEEDVHFPTLT-----------VRETLD-FALRCKGNEFVRGISGGERKRVSIAEALVSRA 137
|
170
....*....|...
gi 931484041 161 LIIFADEPTGNLD 173
Cdd:cd03233 138 SVLCWDNSTRGLD 150
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-203 |
1.28e-10 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 59.30 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 31 GSFVVILGPSGSGKSTLLNILSSLDRPTDGKvvFDSVDVFshdDTRLSEIRnkkmGFVFQ--FHHLL-AEFTCLENVA-- 105
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGK--FDDPPDW---DEILDEFR----GSELQnyFTKLLeGDVKVIVKPQyv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 106 --LPALVNGSAQ---NKAYRRAQ--DLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLDEENTN 178
Cdd:cd03236 97 dlIPKAVKGKVGellKKKDERGKldELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRL 176
|
170 180
....*....|....*....|....*
gi 931484041 179 KLLDVFGSLKSEGRTIILVTHSVDI 203
Cdd:cd03236 177 NAARLIRELAEDDNYVLVVEHDLAV 201
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
20-199 |
1.57e-10 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 60.11 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 20 VLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfshDDTRLSEIRNkKMGFVFQFHHLLAEfT 99
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPL---TKLQLDSWRS-RLAVVSQTPFLFSD-T 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 100 CLENVAL--PalvNGSAQN--KAYRRA---QDLLdkfdigdkknRLP-----------LEISGGERQRVAIARAMINDPL 161
Cdd:PRK10789 405 VANNIALgrP---DATQQEieHVARLAsvhDDIL----------RLPqgydtevgergVMLSGGQKQRISIARALLLNAE 471
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 931484041 162 IIFADEPTGNLD---EENTNKLLDVFGslksEGRTIILVTH 199
Cdd:PRK10789 472 ILILDDALSAVDgrtEHQILHNLRQWG----EGRTVIISAH 508
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
13-199 |
3.99e-10 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 58.28 E-value: 3.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 13 LENETIEVLQG---------VNLLVSKGSFVVILGPSGSGKSTLLNILSSLD----RPTDGKVVFDSVDVFshddtRLSE 79
Cdd:PRK15093 6 IRNLTIEFKTSdgwvkavdrVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTkdnwRVTADRMRFDDIDLL-----RLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 80 IRNKK-----MGFVFQFHHllaefTCL---ENV------ALPALVNGSAQNKAY----RRAQDLLDKFDIGDKKNRL--- 138
Cdd:PRK15093 81 RERRKlvghnVSMIFQEPQ-----SCLdpsERVgrqlmqNIPGWTYKGRWWQRFgwrkRRAIELLHRVGIKDHKDAMrsf 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 931484041 139 PLEISGGERQRVAIARAMINDPLIIFADEPTGNLDEENTNKLLDVFGSL-KSEGRTIILVTH 199
Cdd:PRK15093 156 PYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISH 217
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-199 |
4.44e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 58.67 E-value: 4.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 28 VSKGSFVVILGPSGSGKSTLLNILSSLDRP----TDGKVVFDSV-DVFSHDD--TRLSEIRNKKMGFVF--QFHHLLaef 98
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPnlgdYEEEPSWDEVlKRFRGTElqNYFKKLYNGEIKVVHkpQYVDLI--- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 99 tclenvalPALVNGSAQ---NKAYRR--AQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLD 173
Cdd:PRK13409 173 --------PKVFKGKVRellKKVDERgkLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
170 180
....*....|....*....|....*.
gi 931484041 174 EENTNKLLDVFGSLkSEGRTIILVTH 199
Cdd:PRK13409 245 IRQRLNVARLIREL-AEGKYVLVVEH 269
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-201 |
5.14e-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: 58.80 E-value: 5.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 21 LQGVNLLVSKGSFVVILGPSGSGKSTLLN-ILSSLDRpTDGKVVFD-SVDVFSHDdtrlSEIRNKKMGFVFQFHHLLAE- 97
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDK-VEGHVHMKgSVAYVPQQ----AWIQNDSLRENILFGKALNEk 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 98 --FTCLENVALPA----LVNGsaqnkayrraqdllDKFDIGDKKnrlpLEISGGERQRVAIARAMINDPLIIFADEPTGN 171
Cdd:TIGR00957 729 yyQQVLEACALLPdleiLPSG--------------DRTEIGEKG----VNLSGGQKQRVSLARAVYSNADIYLFDDPLSA 790
|
170 180 190
....*....|....*....|....*....|....
gi 931484041 172 LDEENTNKLLDVF----GSLKseGRTIILVTHSV 201
Cdd:TIGR00957 791 VDAHVGKHIFEHVigpeGVLK--NKTRILVTHGI 822
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
16-199 |
7.83e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 57.11 E-value: 7.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 16 ETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLD--RPTDGKVVFDSVDVFSHDDtrlSEIRNKKMGFVFQFhh 93
Cdd:PRK09580 12 EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSP---EDRAGEGIFMAFQY-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 94 llaeftcleNVALPALVN----GSAQNKAYR-RAQDLLDKFDIGD------KKNRLPLEI---------SGGERQRVAIA 153
Cdd:PRK09580 87 ---------PVEIPGVSNqfflQTALNAVRSyRGQEPLDRFDFQDlmeekiALLKMPEDLltrsvnvgfSGGEKKRNDIL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 931484041 154 RAMINDPLIIFADEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTH 199
Cdd:PRK09580 158 QMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
17-199 |
1.60e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 56.19 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 17 TIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSldRP----TDGKVVFDSVDVFSHDdtrlSEIRNKKMGFV-FQF 91
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPaykiLEGDILFKGESILDLE----PEERAHLGIFLaFQY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 92 hhllaeftcleNVALPALVNGSAQNKAY--RRAQDLLDKFD-------IGDKKNRLPLE-----------ISGGERQRVA 151
Cdd:CHL00131 93 -----------PIEIPGVSNADFLRLAYnsKRKFQGLPELDplefleiINEKLKLVGMDpsflsrnvnegFSGGEKKRNE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 931484041 152 IARAMINDPLIIFADEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTH 199
Cdd:CHL00131 162 ILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH 209
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
3-206 |
1.72e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 55.73 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 3 QASTVSKTYFLENETIE--VLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTRLSEi 80
Cdd:COG2401 26 RVAIVLEAFGVELRVVEryVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGREASLID- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 81 rnkkmgfvfqfhHLLAEFTCLENVALPALVnGSAQNKAYRRaqdlldKFDigdkknrlplEISGGERQRVAIARAMINDP 160
Cdd:COG2401 105 ------------AIGRKGDFKDAVELLNAV-GLSDAVLWLR------RFK----------ELSTGQKFRFRLALLLAERP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 931484041 161 LIIFADEPTGNLDEENTNKLLDVFGSL-KSEGRTIILVTHSVDISKF 206
Cdd:COG2401 156 KLLVIDEFCSHLDRQTAKRVARNLQKLaRRAGITLVVATHHYDVIDD 202
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
37-169 |
1.74e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 57.06 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 37 LGPSGSGKSTLLNILSSLDRPTDGKV-VFD-SVDvfSHD-DTRlseirnKKMGFVFQFHHLLAEFTCLENVALPALVNGS 113
Cdd:NF033858 298 LGSNGCGKSTTMKMLTGLLPASEGEAwLFGqPVD--AGDiATR------RRVGYMSQAFSLYGELTVRQNLELHARLFHL 369
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 931484041 114 AQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPT 169
Cdd:NF033858 370 PAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
21-199 |
1.87e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.88 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 21 LQGVNLLVSKGSFVVILGPSGSGKSTLLNILS---SLDrptDGKVVFDSVDVFShddtRLSE--IRNKKmGFVF------ 89
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNgevLLD---DGRIIYEQDLIVA----RLQQdpPRNVE-GTVYdfvaeg 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 90 ---------QFHHLLAEftcLENVALPALVNGSAqnkayrRAQDLLD-----KFD--IGDKKNRLPL-------EISGGE 146
Cdd:PRK11147 91 ieeqaeylkRYHDISHL---VETDPSEKNLNELA------KLQEQLDhhnlwQLEnrINEVLAQLGLdpdaalsSLSGGW 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 931484041 147 RQRVAIARAMINDPLIIFADEPTGNLDEEnTNKLLDVFgsLKSEGRTIILVTH 199
Cdd:PRK11147 162 LRKAALGRALVSNPDVLLLDEPTNHLDIE-TIEWLEGF--LKTFQGSIIFISH 211
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-199 |
4.27e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 55.56 E-value: 4.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 30 KGSFVVILGPSGSGKSTLLNILSSLDRP----TDGKVVFDSV-------DVFSHddtrLSEIRNKKMGFVF--QFHHLLa 96
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPnlgdYDEEPSWDEVlkrfrgtELQDY----FKKLANGEIKVAHkpQYVDLI- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 97 eftclenvalPALVNGSAQ---NKAYRR--AQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGN 171
Cdd:COG1245 173 ----------PKVFKGTVRellEKVDERgkLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSY 242
|
170 180
....*....|....*....|....*...
gi 931484041 172 LDEENTNKLLDVFGSLKSEGRTIILVTH 199
Cdd:COG1245 243 LDIYQRLNVARLIRELAEEGKYVLVVEH 270
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-213 |
6.58e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 55.51 E-value: 6.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 2 LQASTVSKTYFLENETIE--VLQGVNLLVSKGSFVVILGPSGSGKSTLLN-ILSSLDRPTDGKVVfdsvdvfshddtrls 78
Cdd:PLN03130 612 LPAISIKNGYFSWDSKAErpTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVV--------------- 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 79 eIRNKkMGFVFQFHHLLAEfTCLENVALPALVNGSAQNKAYR-----RAQDLL---DKFDIGDKKnrlpLEISGGERQRV 150
Cdd:PLN03130 677 -IRGT-VAYVPQVSWIFNA-TVRDNILFGSPFDPERYERAIDvtalqHDLDLLpggDLTEIGERG----VNISGGQKQRV 749
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 931484041 151 AIARAMINDPLIIFADEPTGNLDEENTNKLLDvfGSLKSE--GRTIILVTHSVdisKFGSHVYKL 213
Cdd:PLN03130 750 SMARAVYSNSDVYIFDDPLSALDAHVGRQVFD--KCIKDElrGKTRVLVTNQL---HFLSQVDRI 809
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
4-173 |
1.12e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 54.73 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 4 ASTVSKTYFLENETIEV--LQGVNLLVSKGSFVVILGPSGSGKSTLLNILSS----LDRPTDGKVVFDSVDvfshddtrL 77
Cdd:TIGR00956 58 LTRGFRKLKKFRDTKTFdiLKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASntdgFHIGVEGVITYDGIT--------P 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 78 SEIRNKKMGFVF-------QFHHLLAEFTcLENVAL---PAL-VNG-SAQNKAYRRAQDLLDKFDIGDKK-----NRLPL 140
Cdd:TIGR00956 130 EEIKKHYRGDVVynaetdvHFPHLTVGET-LDFAARcktPQNrPDGvSREEYAKHIADVYMATYGLSHTRntkvgNDFVR 208
|
170 180 190
....*....|....*....|....*....|...
gi 931484041 141 EISGGERQRVAIARAMINDPLIIFADEPTGNLD 173
Cdd:TIGR00956 209 GVSGGERKRVSIAEASLGGAKIQCWDNATRGLD 241
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
28-175 |
1.98e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 53.79 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 28 VSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVF-DSVdvfshddtrlseirnkKMGFVFQFH-HLLAEFTCLENVA 105
Cdd:TIGR03719 345 LPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETV----------------KLAYVDQSRdALDPNKTVWEEIS 408
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 931484041 106 --LPALVNGSAQ--NKAYrraqdlLDKFDI--GDKKNRLPlEISGGERQRVAIARAMINDPLIIFADEPTGNLDEE 175
Cdd:TIGR03719 409 ggLDIIKLGKREipSRAY------VGRFNFkgSDQQKKVG-QLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVE 477
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
142-213 |
2.39e-08 |
|
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: 53.48 E-value: 2.39e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 931484041 142 ISGGERQRVAIARAM---INDPLIIFADEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTHSVDISKFGSHVYKL 213
Cdd:TIGR00630 830 LSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVIKTADYIIDL 904
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
28-199 |
2.40e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 52.63 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 28 VSKGSFVVILGPSGSGKSTLLNILSSLdRPTDGKVVFDSVDVFSHDDTRLSEIR-----NKKMGF---VFQFHHLlaeft 99
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELARHRaylsqQQTPPFampVFQYLTL----- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 100 clenvALPALVNGSAQNKAYRraqDLLDKFDIGDKKNRLPLEISGGERQRVAIARAM------INdP---LIIFaDEPTG 170
Cdd:PRK03695 93 -----HQPDKTRTEAVASALN---EVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpdIN-PagqLLLL-DEPMN 162
|
170 180
....*....|....*....|....*....
gi 931484041 171 NLDEENTNKLLDVFGSLKSEGRTIILVTH 199
Cdd:PRK03695 163 SLDVAQQAALDRLLSELCQQGIAVVMSSH 191
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
4-201 |
5.01e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 52.67 E-value: 5.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 4 ASTVSKTYF-----LENETievLQGVNLLVSKGSFVVILGPSGSGKSTLLNILssldrptdgkvvfdsVDVFSHDDTRLS 78
Cdd:PLN03232 614 AISIKNGYFswdskTSKPT---LSDINLEIPVGSLVAIVGGTGEGKTSLISAM---------------LGELSHAETSSV 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 79 EIRNKkMGFVFQFHHLLAEfTCLENValpaLVNGSAQNKAYRRAQDL------LDKF------DIGDKKnrlpLEISGGE 146
Cdd:PLN03232 676 VIRGS-VAYVPQVSWIFNA-TVRENI----LFGSDFESERYWRAIDVtalqhdLDLLpgrdltEIGERG----VNISGGQ 745
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 931484041 147 RQRVAIARAMINDPLIIFADEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTHSV 201
Cdd:PLN03232 746 KQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQL 800
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-199 |
5.56e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.20 E-value: 5.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 2 LQASTVSKTYflENETIevLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVvfdsvdvfshddtRLSEir 81
Cdd:PRK15064 320 LEVENLTKGF--DNGPL--FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV-------------KWSE-- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 82 NKKMGFVFQFHHllAEFTCLENvalpaLVNGSAQnkaYRRAQD------------LLDKFDIGdKKNRLpleISGGERQR 149
Cdd:PRK15064 381 NANIGYYAQDHA--YDFENDLT-----LFDWMSQ---WRQEGDdeqavrgtlgrlLFSQDDIK-KSVKV---LSGGEKGR 446
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 931484041 150 VAIARAMINDPLIIFADEPTGNLDEENTNKL---LDVFgslksEGrTIILVTH 199
Cdd:PRK15064 447 MLFGKLMMQKPNVLVMDEPTNHMDMESIESLnmaLEKY-----EG-TLIFVSH 493
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
20-214 |
8.91e-08 |
|
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: 52.06 E-value: 8.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 20 VLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSL--------DRPTDGKVVF-------------------DSVDVFSH 72
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELwpvyggrlTKPAKGKLFYvpqrpymtlgtlrdqiiypDSSEDMKR 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 73 DDTRLSEIrnKKMGFVFQFHHLLAeftclENVALPALvngsaqnkayrraQDLLDkfdigdkknrlplEISGGERQRVAI 152
Cdd:TIGR00954 547 RGLSDKDL--EQILDNVQLTHILE-----REGGWSAV-------------QDWMD-------------VLSGGEKQRIAM 593
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 931484041 153 ARAMINDPLIIFADEPTGNLDEENTNKLldvFGSLKSEGRTIILVTHSVDISKFgsHVYKLK 214
Cdd:TIGR00954 594 ARLFYHKPQFAILDECTSAVSVDVEGYM---YRLCREFGITLFSVSHRKSLWKY--HEYLLY 650
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
24-199 |
1.05e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 51.51 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 24 VNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfshDDTRLSEIRnKKMGFVFQFHHLLAEFTCLEN 103
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV---TAEQPEDYR-KLFSAVFTDFHLFDQLLGPEG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 104 -VALPALVngsaqnkayrraQDLLDKFDIGDK----KNRLP-LEISGGERQRVAIARAMINDPLIIFADEPTGNLD---- 173
Cdd:PRK10522 418 kPANPALV------------EKWLERLKMAHKleleDGRISnLKLSKGQKKRLALLLALAEERDILLLDEWAADQDphfr 485
|
170 180
....*....|....*....|....*.
gi 931484041 174 EENTNKLLDVfgsLKSEGRTIILVTH 199
Cdd:PRK10522 486 REFYQVLLPL---LQEMGKTIFAISH 508
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
142-201 |
1.11e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.95 E-value: 1.11e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 931484041 142 ISGGERQRVAIARAMINDPLIIFADEPTGNLDeENTNKLLD-VFGSLKSEG-RTIILVTHSV 201
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLD-SNSEKLIEkTIVDIKDKAdKTIITIAHRI 1419
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
29-216 |
1.52e-07 |
|
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: 49.28 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 29 SKGSFVVILGPSGSGKSTLLnilssldrptdgkvvfdsvdvfshDDTRLseirnkkmGFVFQFHHLLaeftclenvalPA 108
Cdd:cd03227 19 GEGSLTIITGPNGSGKSTIL------------------------DAIGL--------ALGGAQSATR-----------RR 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 109 LVNGSAQNKAYRRAQDLLdkfdigdkknrLPLEISGGERQRVAIARAMIN-----DPLIIFaDEPTGNLDEENTNKLLDV 183
Cdd:cd03227 56 SGVKAGCIVAAVSAELIF-----------TRLQLSGGEKELSALALILALaslkpRPLYIL-DEIDRGLDPRDGQALAEA 123
|
170 180 190
....*....|....*....|....*....|...
gi 931484041 184 FGSLKSEGRTIILVTHSVDISKFGSHVYKLKER 216
Cdd:cd03227 124 ILEHLVKGAQVIVITHLPELAELADKLIHIKKV 156
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-204 |
1.55e-07 |
|
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: 49.29 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 30 KGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVFshddtrlseirnkkmgfvfqfhhllaeftclenvalpal 109
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDI--------------------------------------- 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 110 vngsaqnkayrraQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLDEENTNKLLD------V 183
Cdd:smart00382 42 -------------LEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrlL 108
|
170 180
....*....|....*....|.
gi 931484041 184 FGSLKSEGRTIILVTHSVDIS 204
Cdd:smart00382 109 LLLKSEKNLTVILTTNDEKDL 129
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-175 |
1.56e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.96 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 28 VSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDsvdvfshddTRLS----EIRNKKMGFVFQFhhllaeftcLEN 103
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE---------LKISykpqYIKPDYDGTVEDL---------LRS 423
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 931484041 104 VAlPALvnGSAQNKayrraQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLDEE 175
Cdd:PRK13409 424 IT-DDL--GSSYYK-----SEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE 487
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-203 |
1.63e-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: 50.94 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 28 VSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVvfdsvdvfsHDDTRLS----EIRNKKMGFVFQFhhllaeftcLEN 103
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV---------DEDLKISykpqYISPDYDGTVEEF---------LRS 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 104 VALPALVNGSAQNKAYRRAQ--DLLDKfdigdkknRLPlEISGGERQRVAIARAMINDPLIIFADEPTGNLDEE---NTN 178
Cdd:COG1245 425 ANTDDFGSSYYKTEIIKPLGleKLLDK--------NVK-DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEqrlAVA 495
|
170 180
....*....|....*....|....*
gi 931484041 179 KLLDVFgsLKSEGRTIILVTHsvDI 203
Cdd:COG1245 496 KAIRRF--AENRGKTAMVVDH--DI 516
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
14-201 |
1.72e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 50.20 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 14 ENETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVfdsvdvfshddtrlseiRNKKMGFVFQFHH 93
Cdd:PRK13546 33 KNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD-----------------RNGEVSVIAISAG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 94 LLAEFTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLD 173
Cdd:PRK13546 96 LSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGD 175
|
170 180
....*....|....*....|....*...
gi 931484041 174 EENTNKLLDVFGSLKSEGRTIILVTHSV 201
Cdd:PRK13546 176 QTFAQKCLDKIYEFKEQNKTIFFVSHNL 203
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
12-213 |
2.17e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.93 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 12 FLENETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKV-------------------VFDSVDVFSH 72
Cdd:PTZ00243 667 FFELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVwaersiayvpqqawimnatVRGNILFFDE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 73 DDT-RLSE-IRnkkmgfVFQfhhllaeftcLEnvALPALVNGSAQNkayrraqdlldkfDIGDKKNRLpleiSGGERQRV 150
Cdd:PTZ00243 747 EDAaRLADaVR------VSQ----------LE--ADLAQLGGGLET-------------EIGEKGVNL----SGGQKARV 791
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 931484041 151 AIARAMINDPLIIFADEPTGNLDEENTNKLL-DVF-GSLKseGRTIILVTHSVDISKFGSHVYKL 213
Cdd:PTZ00243 792 SLARAVYANRDVYLLDDPLSALDAHVGERVVeECFlGALA--GKTRVLATHQVHVVPRADYVVAL 854
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
21-210 |
2.91e-07 |
|
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: 49.56 E-value: 2.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 21 LQGVNLLVSKGSFVVILGPSGSGKSTL-------------LNILSSLDRPTDGKVVFDSVD-------VFSHDDTRLSEI 80
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqrryVESLSAYARQFLGQMDKPDVDsieglspAIAIDQKTTSRN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 81 RNKKMGFVFQFHHLLA------------EFtcLENVALPALvngsaqnKAYRRAQDLldkfdigdkknrlpleiSGGERQ 148
Cdd:cd03270 91 PRSTVGTVTEIYDYLRllfarvgirerlGF--LVDVGLGYL-------TLSRSAPTL-----------------SGGEAQ 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 931484041 149 RVAIARaMINDPL--IIFA-DEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTHSVDISKFGSHV 210
Cdd:cd03270 145 RIRLAT-QIGSGLtgVLYVlDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHV 208
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
28-199 |
4.59e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.56 E-value: 4.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 28 VSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVvfdsvdvfsHDDTRLsEIrnkkmGFVFQFHHLL-AEFTCLENVA- 105
Cdd:PRK11147 342 VQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI---------HCGTKL-EV-----AYFDQHRAELdPEKTVMDNLAe 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 106 --LPALVNGSAqnkayRRAQDLLDKFDIGDKKNRLPLE-ISGGERQRVAIARAMINDPLIIFADEPTGNLDEEnTNKLLD 182
Cdd:PRK11147 407 gkQEVMVNGRP-----RHVLGYLQDFLFHPKRAMTPVKaLSGGERNRLLLARLFLKPSNLLILDEPTNDLDVE-TLELLE 480
|
170
....*....|....*..
gi 931484041 183 VFgsLKSEGRTIILVTH 199
Cdd:PRK11147 481 EL--LDSYQGTVLLVSH 495
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
28-201 |
8.15e-07 |
|
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: 47.57 E-value: 8.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 28 VSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfshddtrlseirnkkmgfvfqfhhllaeftclenvalp 107
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITP-------------------------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 108 alvngsaqnkAYRRAQdlldkfdigdkknrlpLEISGGERQRVAIARAMINDPLIIFADEPTGNLDEENTNKLLDVFGSL 187
Cdd:cd03222 64 ----------VYKPQY----------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRL 117
|
170
....*....|....*
gi 931484041 188 KSEG-RTIILVTHSV 201
Cdd:cd03222 118 SEEGkKTALVVEHDL 132
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-173 |
1.17e-06 |
|
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: 48.75 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 20 VLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVvfdsvdvfSHddtrlseirNKKMGFVFQFHHLLAEfT 99
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI--------KH---------SGRISFSPQTSWIMPG-T 502
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 931484041 100 CLENVaLPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPL-----EISGGERQRVAIARAMINDPLIIFADEPTGNLD 173
Cdd:TIGR01271 503 IKDNI-IFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
32-200 |
1.17e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.17 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 32 SFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfshddtrlSEIRNKKMGFVFQFHHLLAEFTCLENVALPALVN 111
Cdd:PRK13541 27 AITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNI--------NNIAKPYCTYIGHNLGLKLEMTVFENLKFWSEIY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 112 GSAQNK----AYRRAQDLLDKfdigdKKNRLpleiSGGERQRVAIARAMINDPLIIFADEPTGNLDEENTNKLLDVFGSL 187
Cdd:PRK13541 99 NSAETLyaaiHYFKLHDLLDE-----KCYSL----SSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMK 169
|
170
....*....|...
gi 931484041 188 KSEGRTIILVTHS 200
Cdd:PRK13541 170 ANSGGIVLLSSHL 182
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
22-198 |
1.72e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 47.86 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 22 QGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfsHDDTRLSEIRnKKMGFVFQ-------FHHl 94
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDI--SPRSPLDAVK-KGMAYITEsrrdngfFPN- 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 95 laeFTCLENVAlpalVNGSAQNKAYRRAQDLLDKFD----IGDKKNRLPL----------EISGGERQRVAIARAMINDP 160
Cdd:PRK09700 356 ---FSIAQNMA----ISRSLKDGGYKGAMGLFHEVDeqrtAENQRELLALkchsvnqnitELSGGNQQKVLISKWLCCCP 428
|
170 180 190
....*....|....*....|....*....|....*...
gi 931484041 161 LIIFADEPTGNLDEENTNKLLDVFGSLKSEGRTIILVT 198
Cdd:PRK09700 429 EVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVS 466
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
21-213 |
2.01e-06 |
|
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: 47.22 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 21 LQGVNLLVSKGSFVVILGPSGSGKSTLLN--ILSSLDRPTDGKVV----FDSVDVFSHDD------------TRLS---- 78
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINdtLYPALARRLHLKKEqpgnHDRIEGLEHIDkvividqspigrTPRSnpat 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 79 ------EIRNkkmgfVF-------QFHHLLAEFT--------CLENVALPALVNGSAQNKAYRRAQDL----LDKFDIGD 133
Cdd:cd03271 91 ytgvfdEIRE-----LFcevckgkRYNRETLEVRykgksiadVLDMTVEEALEFFENIPKIARKLQTLcdvgLGYIKLGQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 134 KKNRLpleiSGGERQRVAIARAMIN----DPLIIFaDEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTHSVDISKFGSH 209
Cdd:cd03271 166 PATTL----SGGEAQRIKLAKELSKrstgKTLYIL-DEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADW 240
|
....
gi 931484041 210 VYKL 213
Cdd:cd03271 241 IIDL 244
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-173 |
2.04e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.05 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 20 VLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDV--FSHDDTR--LSEIRNKKMGFVFQFHHLL 95
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVakFGLTDLRrvLSIIPQSPVLFSGTVRFNI 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 96 AEFTCLENVALPALVNGSAQNKAYRRAQDLLDK--FDIGDKknrlpleISGGERQRVAIARAMINDPLIIFADEPTGNLD 173
Cdd:PLN03232 1331 DPFSEHNDADLWEALERAHIKDVIDRNPFGLDAevSEGGEN-------FSVGQRQLLSLARALLRRSKILVLDEATASVD 1403
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
36-198 |
2.28e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 47.69 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 36 ILGPSG---SGKSTLLNILSSLDRPTDGKVVFDSVDVFSHDDTR--------LSEIRnKKMGFVFqfhhllaEFTCLENV 104
Cdd:PRK10762 280 ILGVSGlmgAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDglangivyISEDR-KRDGLVL-------GMSVKENM 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 105 ALPAL-----VNGSAQNKAYRRA-QDLLDKFDIGDKKNRLPL-EISGGERQRVAIARAMINDPLIIFADEPTGNLDEENT 177
Cdd:PRK10762 352 SLTALryfsrAGGSLKHADEQQAvSDFIRLFNIKTPSMEQAIgLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAK 431
|
170 180
....*....|....*....|.
gi 931484041 178 NKLLDVFGSLKSEGRTIILVT 198
Cdd:PRK10762 432 KEIYQLINQFKAEGLSIILVS 452
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
14-201 |
2.84e-06 |
|
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: 46.83 E-value: 2.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 14 ENETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDV----FSHDDTRLSEIRNKKMGFVF 89
Cdd:cd03288 30 ENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDIsklpLHTLRSRLSIILQDPILFSG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 90 QFH-HLLAEFTCLENVALPALVNGSAQNKAyRRAQDLLDKFDIGDKKNrlpleISGGERQRVAIARAMINDPLIIFADEP 168
Cdd:cd03288 110 SIRfNLDPECKCTDDRLWEALEIAQLKNMV-KSLPGGLDAVVTEGGEN-----FSVGQRQLFCLARAFVRKSSILIMDEA 183
|
170 180 190
....*....|....*....|....*....|...
gi 931484041 169 TGNLDEENTNKLLDVFGSLKSEgRTIILVTHSV 201
Cdd:cd03288 184 TASIDMATENILQKVVMTAFAD-RTVVTIAHRV 215
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
12-216 |
2.92e-06 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 46.49 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 12 FLENETIEVLQgvnllVSKGSFVVILGPSGSGKSTLLNILS-SL--DRPTDGKVVFDSvDVFSHDDTRLS-----EIRNK 83
Cdd:cd03279 14 FREEQVIDFTG-----LDNNGLFLICGPTGAGKSTILDAITyALygKTPRYGRQENLR-SVFAPGEDTAEvsftfQLGGK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 84 KMGFVFQFHHLLAEFTclENVALPalvngsaQNKAyrraqdllDKFDIGDKKNrlpleISGGERQRVAIARAMINDPLI- 162
Cdd:cd03279 88 KYRVERSRGLDYDQFT--RIVLLP-------QGEF--------DRFLARPVST-----LSGGETFLASLSLALALSEVLq 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 931484041 163 ---------IFADEPTGNLDEENTNKLLDVFGSLKSEGRTIILVthsvdiskfgSHVYKLKER 216
Cdd:cd03279 146 nrggarleaLFIDEGFGTLDPEALEAVATALELIRTENRMVGVI----------SHVEELKER 198
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
32-173 |
3.40e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.16 E-value: 3.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 32 SFVVILGPSGSGKSTLLNILSSLDRPTDGkVVFDSVDVfshddtRLSeirnkkmgfVFQFHH----------LLAEFTCL 101
Cdd:PLN03073 536 SRIAMVGPNGIGKSTILKLISGELQPSSG-TVFRSAKV------RMA---------VFSQHHvdgldlssnpLLYMMRCF 599
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 931484041 102 ENVALPALvngsaqnkayrRAQdlLDKFDIGDKKNRLPL-EISGGERQRVAIARAMINDPLIIFADEPTGNLD 173
Cdd:PLN03073 600 PGVPEQKL-----------RAH--LGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
136-199 |
3.45e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.13 E-value: 3.45e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 931484041 136 NRLPLEISGGERQRVAIARAMINDPLII--FADEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTH 199
Cdd:PRK00635 471 ERALATLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEH 536
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
12-199 |
3.77e-06 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 45.77 E-value: 3.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 12 FLENETIEVLQGVNLLVskgsfvvilGPSGSGKSTLLNIL--------SSLDRPTDGKVVFDSVD-----VFSHDDTRL- 77
Cdd:COG0419 13 YRDTETIDFDDGLNLIV---------GPNGAGKSTILEAIryalygkaRSRSKLRSDLINVGSEEasvelEFEHGGKRYr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 78 ---------------SEIRNKKMGFVFQFHHLLAEFTCLENVALPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLplei 142
Cdd:COG0419 84 ierrqgefaefleakPSERKEALKRLLGLEIYEELKERLKELEEALESALEELAELQKLKQEILAQLSGLDPIETL---- 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 931484041 143 SGGERQRVAIARAMindPLIIfaDepTGNLDEENTNKLLDVFGSLKsegrtiiLVTH 199
Cdd:COG0419 160 SGGERLRLALADLL---SLIL--D--FGSLDEERLERLLDALEELA-------IITH 202
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
18-203 |
3.88e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.15 E-value: 3.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 18 IEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSldRPTDGKVvfdsvdvfsHDDTRLSEIRNKK------MGFVFQF 91
Cdd:PLN03140 893 LQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYI---------EGDIRISGFPKKQetfariSGYCEQN 961
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 92 HHLLAEFTCLENVA------LPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLP--LEISGGERQRVAIARAMINDPLII 163
Cdd:PLN03140 962 DIHSPQVTVRESLIysaflrLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPgvTGLSTEQRKRLTIAVELVANPSII 1041
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 931484041 164 FADEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTH--SVDI 203
Cdd:PLN03140 1042 FMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHqpSIDI 1083
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
138-213 |
4.67e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.75 E-value: 4.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 138 LPL-----EISGGERQRVAIARAMIN---DPLIIFADEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTHSVDISKFGSH 209
Cdd:PRK00635 801 LPLgrplsSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVKVADY 880
|
....
gi 931484041 210 VYKL 213
Cdd:PRK00635 881 VLEL 884
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
20-199 |
7.01e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 45.33 E-value: 7.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 20 VLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDVfshDDTRLSeiRNKKMGFVFQFHHLLAEFT 99
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI---KKDLCT--YQKQLCFVGHRSGINPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 100 CLENVALPALVNGSAQNkayrrAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLDEENTNK 179
Cdd:PRK13540 91 LRENCLYDIHFSPGAVG-----ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLT 165
|
170 180
....*....|....*....|
gi 931484041 180 LLDVFGSLKSEGRTIILVTH 199
Cdd:PRK13540 166 IITKIQEHRAKGGAVLLTSH 185
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
13-202 |
8.01e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 45.81 E-value: 8.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 13 LENETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDvFSHDDTRlseIRNKKmGFVF--- 89
Cdd:PRK15439 271 VEDLTGEGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKE-INALSTA---QRLAR-GLVYlpe 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 90 --QFHHL-----LAEFTCLENVALPALVNGSAQNKA----YRRAQDLldKFDIGDKKNRlplEISGGERQRVAIARAMIN 158
Cdd:PRK15439 346 drQSSGLyldapLAWNVCALTHNRRGFWIKPARENAvlerYRRALNI--KFNHAEQAAR---TLSGGNQQKVLIAKCLEA 420
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 931484041 159 DPLIIFADEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTHSVD 202
Cdd:PRK15439 421 SPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLE 464
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
20-202 |
1.24e-05 |
|
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: 44.85 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 20 VLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVvfdsvdvfSHddtrlseirNKKMGFVFQFHHLLAEfT 99
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI--------KH---------SGRISFSSQFSWIMPG-T 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 100 CLENVaLPALVNGSAQNKAYRRAQDLLDKFDIGDKKNRLPL-----EISGGERQRVAIARAMINDPLIIFADEPTGNLDE 174
Cdd:cd03291 114 IKENI-IFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
170 180
....*....|....*....|....*...
gi 931484041 175 ENTNKLLDVFGSLKSEGRTIILVTHSVD 202
Cdd:cd03291 193 FTEKEIFESCVCKLMANKTRILVTSKME 220
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
20-187 |
1.48e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.16 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 20 VLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDsvdvfshddtrlseiRNKKMGFVFQfHHLlaEFT 99
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLA---------------KGIKLGYFAQ-HQL--EFL 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 100 CLENVALPALVNgSAQNKAYRRAQDLLDKFDI-GDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLD----E 174
Cdd:PRK10636 389 RADESPLQHLAR-LAPQELEQKLRDYLGGFGFqGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDldmrQ 467
|
170
....*....|...
gi 931484041 175 ENTNKLLDVFGSL 187
Cdd:PRK10636 468 ALTEALIDFEGAL 480
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
30-175 |
3.64e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 43.95 E-value: 3.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 30 KGSFVVILGPSGSGKSTLLNILSSLDRPTDGKV-VFDSVdvfshddtrlseirnkKMGFVFQFH-HLLAEFTCLENVA-- 105
Cdd:PRK11819 349 PGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIkIGETV----------------KLAYVDQSRdALDPNKTVWEEISgg 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 106 ----------LP--ALV-----NGSAQNKayrRAQDLldkfdigdkknrlpleiSGGERQRVAIARAMINDPLIIFADEP 168
Cdd:PRK11819 413 ldiikvgnreIPsrAYVgrfnfKGGDQQK---KVGVL-----------------SGGERNRLHLAKTLKQGGNVLLLDEP 472
|
....*..
gi 931484041 169 TGNLDEE 175
Cdd:PRK11819 473 TNDLDVE 479
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
142-216 |
4.03e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.12 E-value: 4.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 142 ISGGERQ------RVAIARAMINDPLIIFADEPTGNLDEENTNKLLDVFG-SLKSEG--RTIILVTHSVDISKFGSHVYK 212
Cdd:PRK01156 802 LSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEySLKDSSdiPQVIMISHHRELLSVADVAYE 881
|
....
gi 931484041 213 LKER 216
Cdd:PRK01156 882 VKKS 885
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
121-218 |
4.09e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.85 E-value: 4.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 121 RAQDLLDKFDIGDKKNRLPLEISGGERQRVAIARAMINDPLIIFADEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTHS 200
Cdd:PRK10938 115 RCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNR 194
|
90
....*....|....*....
gi 931484041 201 V-DISKFGSHVYKLKEREL 218
Cdd:PRK10938 195 FdEIPDFVQFAGVLADCTL 213
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
13-51 |
4.92e-05 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 43.38 E-value: 4.92e-05
10 20 30
....*....|....*....|....*....|....*....
gi 931484041 13 LENETIEVLQGVnllVSKGSFVVILGPSGSGKSTLLNIL 51
Cdd:PRK01889 180 LDGEGLDVLAAW---LSGGKTVALLGSSGVGKSTLVNAL 215
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-173 |
5.11e-05 |
|
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: 43.75 E-value: 5.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 20 VLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLdRPTDGKVVFDSVdvfSHDDTRLSEIRnKKMG------FVFQ--F 91
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGV---SWNSVTLQTWR-KAFGvipqkvFIFSgtF 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 92 HHLLAEFTCLENVALPALVNGSAQNKAYRRAQDLLDkFDIGDKKNRLpleiSGGERQRVAIARAMINDPLIIFADEPTGN 171
Cdd:TIGR01271 1309 RKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLD-FVLVDGGYVL----SNGHKQLMCLARSILSKAKILLLDEPSAH 1383
|
..
gi 931484041 172 LD 173
Cdd:TIGR01271 1384 LD 1385
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
38-199 |
9.60e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.57 E-value: 9.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 38 GPSGSGKSTLLNILSSLDRPTDGKVVFDSvdvfshddtrlseirNKKMGFVFQFHHLLAEFTCLENV------------- 104
Cdd:PRK15064 34 GANGCGKSTFMKILGGDLEPSAGNVSLDP---------------NERLGKLRQDQFAFEEFTVLDTVimghtelwevkqe 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 105 -----ALP-----------------ALVNGSAqnkAYRRAQDLLDKFDIGDKKNRLPL-EISGGERQRVAIARAMINDPL 161
Cdd:PRK15064 99 rdriyALPemseedgmkvadlevkfAEMDGYT---AEARAGELLLGVGIPEEQHYGLMsEVAPGWKLRVLLAQALFSNPD 175
|
170 180 190
....*....|....*....|....*....|....*...
gi 931484041 162 IIFADEPTGNLDEENTNKLLDVFGSLKSegrTIILVTH 199
Cdd:PRK15064 176 ILLLDEPTNNLDINTIRWLEDVLNERNS---TMIIISH 210
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
143-205 |
1.19e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 42.32 E-value: 1.19e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 931484041 143 SGGERQRVAIARAMINDP----LIIFaDEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTHSVDISK 205
Cdd:COG0178 828 SGGEAQRVKLASELSKRStgktLYIL-DEPTTGLHFHDIRKLLEVLHRLVDKGNTVVVIEHNLDVIK 893
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
14-47 |
2.35e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.55 E-value: 2.35e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 931484041 14 ENETIEV-------LQGVNLLVSKGSFVVILGPSGSGKSTL 47
Cdd:COG0178 2 MMDKIRIrgarehnLKNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
20-173 |
3.49e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 41.26 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 20 VLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDGKVVFDSVDV--FSHDDTRlseirnKKMGFVFQfhhllae 97
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDIskFGLMDLR------KVLGIIPQ------- 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 98 ftclenvaLPALVNGSAQ---------NKAyrraqDL---LDKFDIGD--KKNRLPLE---------ISGGERQRVAIAR 154
Cdd:PLN03130 1321 --------APVLFSGTVRfnldpfnehNDA-----DLwesLERAHLKDviRRNSLGLDaevseagenFSVGQRQLLSLAR 1387
|
170
....*....|....*....
gi 931484041 155 AMINDPLIIFADEPTGNLD 173
Cdd:PLN03130 1388 ALLRRSKILVLDEATAAVD 1406
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
13-58 |
4.52e-04 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 40.07 E-value: 4.52e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 931484041 13 LENETIEVLQgvNLLvsKGSFVVILGPSGSGKSTLLN-ILSSLDRPT 58
Cdd:cd01854 71 KTGEGLDELR--ELL--KGKTSVLVGQSGVGKSTLLNaLLPELVLAT 113
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
20-173 |
5.65e-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: 39.84 E-value: 5.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 20 VLQGVNLLVSKGSFVVILGPSGSGKSTLLNILSSLdRPTDGKVVFDSVdvfSHDDTRLSEIRnKKMG------FVFQ--F 91
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGV---SWNSVPLQKWR-KAFGvipqkvFIFSgtF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 92 HHLLAEFTCLENVALPALVNGSAQNKAYRRAQDLLDkFDIGDKKNRLpleiSGGERQRVAIARAMINDPLIIFADEPTGN 171
Cdd:cd03289 94 RKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLD-FVLVDGGCVL----SHGHKQLMCLARSVLSKAKILLLDEPSAH 168
|
..
gi 931484041 172 LD 173
Cdd:cd03289 169 LD 170
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
112-216 |
5.68e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. 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: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 40.34 E-value: 5.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 112 GSAQNKAYRRAQDLLDkFDIGDKKNRLPLEISGGERQRVAIARAMINDPLI----------IFADEPTGNLDEENTNKLL 181
Cdd:TIGR00618 922 DSHVNARKYQGLALLV-ADAYTGSVRPSATLSGGETFLASLSLALALADLLstsggtvldsLFIDEGFGSLDEDSLDRAI 1000
|
90 100 110
....*....|....*....|....*....|....*
gi 931484041 182 DVFGSLKSEGRTIILVthsvdiskfgSHVYKLKER 216
Cdd:TIGR00618 1001 GILDAIREGSKMIGII----------SHVPEFRER 1025
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
21-49 |
8.43e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.06 E-value: 8.43e-04
10 20
....*....|....*....|....*....
gi 931484041 21 LQGVNLLVSKGSFVVILGPSGSGKSTLLN 49
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLIN 653
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
14-47 |
8.82e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.06 E-value: 8.82e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 931484041 14 ENETIEV-------LQGVNLLVSKGSFVVILGPSGSGKSTL 47
Cdd:PRK00349 2 MMDKIIIrgarehnLKNIDLDIPRDKLVVFTGLSGSGKSSL 42
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
143-200 |
1.19e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.46 E-value: 1.19e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 931484041 143 SGGERQRVAIARAMINDPLIIFADEPTGNLDeenTNKLLDVFGSLKSEGRTIILVTHS 200
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLD---LHAVLWLETYLLKWPKTFIVVSHA 400
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
21-51 |
1.26e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 39.24 E-value: 1.26e-03
10 20 30
....*....|....*....|....*....|..
gi 931484041 21 LQGVNLLVSKGSFVVILGPSGSGKSTLLN-IL 51
Cdd:COG0178 621 LKNVDVEIPLGVLTCVTGVSGSGKSTLVNdIL 652
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
142-216 |
1.48e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 39.40 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 142 ISGGERQRVAIARAMINDPLI--------IFADEPTGNLDEENTNKLLDVFGSLKSEGRTIILVthsvdiskfgSHVYKL 213
Cdd:PRK10246 950 LSGGESFLVSLALALALSDLVshktridsLFLDEGFGTLDSETLDTALDALDALNASGKTIGVI----------SHVEAM 1019
|
...
gi 931484041 214 KER 216
Cdd:PRK10246 1020 KER 1022
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
142-199 |
1.63e-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: 39.23 E-value: 1.63e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 931484041 142 ISGGERQRVAIArAMINDPLI---IFADEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTH 199
Cdd:TIGR00630 489 LSGGEAQRIRLA-TQIGSGLTgvlYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEH 548
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
30-58 |
2.11e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 37.52 E-value: 2.11e-03
10 20 30
....*....|....*....|....*....|
gi 931484041 30 KGSFVVILGPSGSGKSTLLN-ILSSLDRPT 58
Cdd:pfam03193 105 KGKTTVLAGQSGVGKSTLLNaLLPELDLRT 134
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
138-198 |
2.17e-03 |
|
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: 38.65 E-value: 2.17e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 931484041 138 LPL-EISGGERQRVAIARAMINDPLIIFADEPTGNLDEENTNKLLDVFGSLKSEGRTIILVT 198
Cdd:TIGR02633 399 LPIgRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVS 460
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
141-203 |
2.23e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.60 E-value: 2.23e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 931484041 141 EISGGER-Q-----RVAIARAMINDPLIIFADEPTGNLDEENTNKLLDVFGSLkSEGRTIILVTHSVDI 203
Cdd:COG4717 558 ELSRGTReQlylalRLALAELLAGEPLPLILDDAFVNFDDERLRAALELLAEL-AKGRQVIYFTCHEEL 625
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
143-205 |
2.50e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 38.52 E-value: 2.50e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 931484041 143 SGGERQRVAIA-----RAMINDPLIIfaDEPTGNLDEENTNKLLDVFGSLKSEGRTIILVTHSVDISK 205
Cdd:PRK00349 832 SGGEAQRVKLAkelskRSTGKTLYIL--DEPTTGLHFEDIRKLLEVLHRLVDKGNTVVVIEHNLDVIK 897
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
21-47 |
2.71e-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: 38.46 E-value: 2.71e-03
10 20
....*....|....*....|....*..
gi 931484041 21 LQGVNLLVSKGSFVVILGPSGSGKSTL 47
Cdd:TIGR00630 12 LKNIDVEIPRDKLVVITGLSGSGKSSL 38
|
|
| VirB11 |
COG0630 |
Type IV secretory pathway ATPase VirB11/Archaellum biosynthesis ATPase ArlI/FlaI [Cell ... |
26-63 |
4.16e-03 |
|
Type IV secretory pathway ATPase VirB11/Archaellum biosynthesis ATPase ArlI/FlaI [Cell motility, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440395 [Multi-domain] Cd Length: 462 Bit Score: 37.75 E-value: 4.16e-03
10 20 30
....*....|....*....|....*....|....*...
gi 931484041 26 LLVSKGSFVVILGPSGSGKSTLLNILSSLDRPTDgKVV 63
Cdd:COG0630 285 LLLENGKSVLVAGGTASGKTTLLNALLSFIPPDA-KIV 321
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
115-199 |
4.19e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 37.71 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 115 QNKAYRRAQdlLDkfdiGD------KKNRLPLE---ISGGERQ------RVAI----------ARAMinDPLIIfaDEPT 169
Cdd:PRK02224 752 QNDAYSHIE--LD----GEyeltvyQKDGEPLEpeqLSGGERAlfnlslRCAIyrllaegiegDAPL--PPLIL--DEPT 821
|
90 100 110
....*....|....*....|....*....|.
gi 931484041 170 GNLDEENTNKLLDVFGSLKSEG-RTIILVTH 199
Cdd:PRK02224 822 VFLDSGHVSQLVDLVESMRRLGvEQIVVVSH 852
|
|
| NACHT |
COG5635 |
Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; |
16-48 |
5.46e-03 |
|
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 37.48 E-value: 5.46e-03
10 20 30
....*....|....*....|....*....|...
gi 931484041 16 ETIEVLQGVNLLVSKGSFVVILGPSGSGKSTLL 48
Cdd:COG5635 165 ERIESLKRLELLEAKKKRLLILGEPGSGKTTLL 197
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
102-197 |
5.48e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 37.22 E-value: 5.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931484041 102 ENVALPAL---VNGSAQNKA--YRRAQDLLDKFDIGDKKNRLPLE-ISGGERQRVAIARAMINDPLIIFADEPTGNLDEE 175
Cdd:PRK13549 360 KNITLAALdrfTGGSRIDDAaeLKTILESIQRLKVKTASPELAIArLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVG 439
|
90 100
....*....|....*....|..
gi 931484041 176 NTNKLLDVFGSLKSEGRTIILV 197
Cdd:PRK13549 440 AKYEIYKLINQLVQQGVAIIVI 461
|
|
| Gmk |
COG0194 |
Guanylate kinase [Nucleotide transport and metabolism]; |
30-51 |
5.93e-03 |
|
Guanylate kinase [Nucleotide transport and metabolism];
Pssm-ID: 439964 Cd Length: 190 Bit Score: 36.59 E-value: 5.93e-03
|
| GMPK |
cd00071 |
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ... |
34-51 |
6.19e-03 |
|
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), catalyzes the reversible phosphoryl transfer from adenosine triphosphate (ATP) to guanosine monophosphate (GMP) to yield adenosine diphosphate (ADP) and guanosine diphosphate (GDP). It plays an essential role in the biosynthesis of guanosine triphosphate (GTP). This enzyme is also important for the activation of some antiviral and anticancer agents, such as acyclovir, ganciclovir, carbovir, and thiopurines.
Pssm-ID: 238026 Cd Length: 137 Bit Score: 35.59 E-value: 6.19e-03
|
| CpaF |
COG4962 |
Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and ... |
20-54 |
7.72e-03 |
|
Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 443988 [Multi-domain] Cd Length: 386 Bit Score: 36.68 E-value: 7.72e-03
10 20 30
....*....|....*....|....*....|....*
gi 931484041 20 VLQGVNLLVSkgsfvvilGPSGSGKSTLLNILSSL 54
Cdd:COG4962 179 VRARLNILVS--------GGTGSGKTTLLNALSGF 205
|
|
| COG3911 |
COG3911 |
Predicted ATPase [General function prediction only]; |
33-54 |
8.01e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443117 Cd Length: 180 Bit Score: 35.95 E-value: 8.01e-03
|
| VirB4 |
COG3451 |
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ... |
34-51 |
9.16e-03 |
|
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442674 [Multi-domain] Cd Length: 546 Bit Score: 36.46 E-value: 9.16e-03
|
| dNK |
pfam01712 |
Deoxynucleoside kinase; This family consists of various deoxynucleoside kinases cytidine EC:2. ... |
34-98 |
9.61e-03 |
|
Deoxynucleoside kinase; This family consists of various deoxynucleoside kinases cytidine EC:2.7.1.74, guanosine EC:2.7.1.113, adenosine EC:2.7.1.76 and thymidine kinase EC:2.7.1.21 (which also phosphorylates deoxyuridine and deoxycytosine.) These enzymes catalyze the production of deoxynucleotide 5'-monophosphate from a deoxynucleoside. Using ATP and yielding ADP in the process.
Pssm-ID: 396326 Cd Length: 201 Bit Score: 35.76 E-value: 9.61e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 931484041 34 VVILGPSGSGKSTLLNILSsldRPTDGKVVFDSVDVFSHDDTRLSEIRNKKMGFVFQFHHLLAEF 98
Cdd:pfam01712 1 ISIEGNIGAGKSTLTKILS---KRLGFKVFEEPVDRWTNPYLDKFYKDPSRWSFALQTYFLNSRF 62
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
143-184 |
9.89e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 34.13 E-value: 9.89e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 931484041 143 SGGERQR---VAIARAMI----------NDPLIIFADEPTGNLDEENTNKLLDVF 184
Cdd:pfam13558 34 SGGEKQLlayLPLAAALAaqygsaegrpPAPRLVFLDEAFAKLDEENIRTALELL 88
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