|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-228 |
8.93e-147 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 408.01 E-value: 8.93e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 1 MPAQNVIEVHHVAKRVGEGENQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEE 80
Cdd:PRK10584 1 MPAENIVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 81 GRAALRARDIGFVFQSFMLVPTLTALENVQLPALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARA 160
Cdd:PRK10584 81 ARAKLRAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502612564 161 FSARPQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAARCQRRLRLVDGTLREVA 228
Cdd:PRK10584 161 FNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQEEA 228
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-228 |
2.07e-129 |
|
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: 364.45 E-value: 2.07e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 2 PAQNVIEVHHVAKRVGEGENQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEG 81
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 82 RAALRARDIGFVFQSFMLVPTLTALENVQLPALLRGERehDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAF 161
Cdd:COG4181 84 RARLRARHVGFVFQSFQLLPTLTALENVMLPLELAGRR--DARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502612564 162 SARPQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAARCQRRLRLVDGTLREVA 228
Cdd:COG4181 162 ATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVEDT 228
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
4-226 |
2.56e-110 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 315.83 E-value: 2.56e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 4 QNVIEVHHVAKRVGEGENQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEGRA 83
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 84 ALRARDIGFVFQSFMLVPTLTALENVQLPALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSA 163
Cdd:COG1136 82 RLRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502612564 164 RPQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAARCQRRLRLVDGTLRE 226
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
7-224 |
8.89e-103 |
|
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: 296.32 E-value: 8.89e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGEGENQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEGRAALR 86
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 87 ARDIGFVFQSFMLVPTLTALENVQLPALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQ 166
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502612564 167 ILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAARCQRRLRLVDGTL 224
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
6-226 |
1.89e-81 |
|
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: 242.64 E-value: 1.89e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 6 VIEVHHVAKRVGEGENQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEGRAAL 85
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 86 RARDIGFVFQSFMLVPTLTALENVQLPALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARP 165
Cdd:TIGR02211 81 RNKKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502612564 166 QILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAARCQRRLRLVDGTLRE 226
Cdd:TIGR02211 161 SLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVLEMKDGQLFN 221
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
6-227 |
1.12e-76 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 230.32 E-value: 1.12e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 6 VIEVHHVAKRVGEGenqISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEGRAAL 85
Cdd:COG2884 1 MIRFENVSKRYPGG---REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 86 RaRDIGFVFQSFMLVPTLTALENVQLPALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARP 165
Cdd:COG2884 78 R-RRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502612564 166 QILFADEPTGNLDRQTGDRIADLLFELNQRQaTTLVMVTHDVQLAARCQRR-LRLVDGTLREV 227
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEINRRG-TTVLIATHDLELVDRMPKRvLELEDGRLVRD 218
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
4-226 |
1.79e-67 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 207.36 E-value: 1.79e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 4 QNVIEVHHVAKRVGEGENQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEGRA 83
Cdd:PRK11629 3 KILLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 84 ALRARDIGFVFQSFMLVPTLTALENVQLPALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSA 163
Cdd:PRK11629 83 ELRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502612564 164 RPQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAARCQRRLRLVDGTLRE 226
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTA 225
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
2-207 |
2.76e-67 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 207.63 E-value: 2.76e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 2 PAQNVIEVHHVAKRVGEGENQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDeeg 81
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 82 raalraRDIGFVFQSFMLVPTLTALENVQLPALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAF 161
Cdd:COG1116 80 ------PDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARAL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 502612564 162 SARPQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDV 207
Cdd:COG1116 154 ANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDV 199
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
6-222 |
4.27e-63 |
|
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: 195.54 E-value: 4.27e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 6 VIEVHHVAKRVGEGenqISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEGRAAL 85
Cdd:TIGR02673 1 MIEFHNVSKAYPGG---VAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 86 RaRDIGFVFQSFMLVPTLTALENVQLPALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARP 165
Cdd:TIGR02673 78 R-RRIGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502612564 166 QILFADEPTGNLDRQTGDRIADLLFELNQRqATTLVMVTHDVQLAARCQRR-LRLVDG 222
Cdd:TIGR02673 157 PLLLADEPTGNLDPDLSERILDLLKRLNKR-GTTVIVATHDLSLVDRVAHRvIILDDG 213
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
7-207 |
1.77e-62 |
|
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: 194.23 E-value: 1.77e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGEGENQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQldeegraalR 86
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG---------P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 87 ARDIGFVFQSFMLVPTLTALENVQLPALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQ 166
Cdd:cd03293 72 GPDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 502612564 167 ILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDV 207
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDI 192
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
6-215 |
3.22e-60 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 189.50 E-value: 3.22e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 6 VIEVHHVAKRVGEGENqisILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEGRAAL 85
Cdd:COG3638 2 MLELRNLSKRYPGGTP---ALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 86 RaRDIGFVFQSFMLVPTLTALENVQ---------LPALLRGEREHDsRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVA 156
Cdd:COG3638 79 R-RRIGMIFQQFNLVPRLSVLTNVLagrlgrtstWRSLLGLFPPED-RERALEALERVGLADKAYQRADQLSGGQQQRVA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 157 LARAFSARPQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAAR-CQR 215
Cdd:COG3638 157 IARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRyADR 216
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-210 |
1.48e-58 |
|
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: 184.80 E-value: 1.48e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 2 PAQNVIEVHHVAKRVGEGEnqisILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEG 81
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRV----VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 82 RAALRARdIGFVFQSFMLVPTLTALENVQLPalLRgerEHDS------RQRAAALLTQLGLGQRLRHLPAQLSGGEQQRV 155
Cdd:COG1127 77 LYELRRR-IGMLFQGGALFDSLTVFENVAFP--LR---EHTDlseaeiRELVLEKLELVGLPGAADKMPSELSGGMRKRV 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502612564 156 ALARAFSARPQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLA 210
Cdd:COG1127 151 ALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSA 205
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
6-225 |
1.12e-57 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 182.14 E-value: 1.12e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 6 VIEVHHVAKRVGEGENQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEGRAAL 85
Cdd:TIGR02982 1 VISIRNLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 86 RaRDIGFVFQSFMLVPTLTALENVQLPA-LLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSAR 164
Cdd:TIGR02982 81 R-RRIGYIFQAHNLLGFLTARQNVQMALeLQPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHH 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502612564 165 PQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAARCQRRLRLVDGTLR 225
Cdd:TIGR02982 160 PKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDNRILDVADRILQMEDGKLL 220
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
19-222 |
1.05e-56 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 190.32 E-value: 1.05e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 19 GENQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEGRAALRARDIGFVFQSFM 98
Cdd:PRK10535 17 GEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRREHFGFIFQRYH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 99 LVPTLTALENVQLPALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEPTGNLD 178
Cdd:PRK10535 97 LLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 502612564 179 RQTGDRIADLLFELNQrQATTLVMVTHDVQLAARCQRRLRLVDG 222
Cdd:PRK10535 177 SHSGEEVMAILHQLRD-RGHTVIIVTHDPQVAAQAERVIEIRDG 219
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
6-228 |
1.09e-56 |
|
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: 179.62 E-value: 1.09e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 6 VIEVHHVAKRVGEGENQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEGRAaL 85
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRK-I 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 86 RARDIGFVFQSFM--LVPTLTALENVQLPALLRGEREHDSRQRAAALLTQLGLG---QRLRHLPAQLSGGEQQRVALARA 160
Cdd:cd03257 80 RRKEIQMVFQDPMssLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGlpeEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502612564 161 FSARPQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAAR-CQRRLRLVDGTLREVA 228
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
7-228 |
2.18e-56 |
|
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: 179.61 E-value: 2.18e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGEGENQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQldeeGRAALR 86
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTR----RRRKAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 87 ARDIGFVFQSFM--LVPTLTALENVQLPALLRGEREHDsrQRAAALLTQLGLGQRLRH-LPAQLSGGEQQRVALARAFSA 163
Cdd:COG1124 78 RRRVQMVFQDPYasLHPRHTVDRILAEPLRIHGLPDRE--ERIAELLEQVGLPPSFLDrYPHQLSGGQRQRVAIARALIL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502612564 164 RPQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAAR-CQRRLRLVDGTLREVA 228
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEEL 221
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
7-224 |
1.42e-55 |
|
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: 176.92 E-value: 1.42e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGEGenqiSILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEGRAALR 86
Cdd:cd03261 1 IELRGLTKSFGGR----TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 87 ARdIGFVFQSFMLVPTLTALENVQLPalLRGER---EHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSA 163
Cdd:cd03261 77 RR-MGMLFQSGALFDSLTVFENVAFP--LREHTrlsEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502612564 164 RPQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAAR-CQRRLRLVDGTL 224
Cdd:cd03261 154 DPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKI 215
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
7-206 |
1.77e-55 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 180.29 E-value: 1.77e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGEgenqISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEgraalr 86
Cdd:COG3842 6 LELENVSKRYGD----VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 87 ARDIGFVFQSFMLVPTLTALENVQLPALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQ 166
Cdd:COG3842 76 KRNVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPR 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 502612564 167 ILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHD 206
Cdd:COG3842 156 VLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHD 195
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
7-216 |
3.33e-55 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 175.67 E-value: 3.33e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGegeNQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEGRAALR 86
Cdd:cd03292 1 IEFINVTKTYP---NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 87 aRDIGFVFQSFMLVPTLTALENVQLPALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQ 166
Cdd:cd03292 78 -RKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 502612564 167 ILFADEPTGNLDRQTGDRIADLLFELNQRqATTLVMVTHDVQLAARCQRR 216
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHR 205
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
11-219 |
7.92e-55 |
|
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: 174.34 E-value: 7.92e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 11 HVAKRVGEgenqISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEGRAALRARDI 90
Cdd:TIGR03608 3 NISKKFGD----KVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRREKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 91 GFVFQSFMLVPTLTALENVQLPALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQILFA 170
Cdd:TIGR03608 79 GYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 502612564 171 DEPTGNLDRQTGDRIADLLFELNqRQATTLVMVTHDVQLAARCQRRLRL 219
Cdd:TIGR03608 159 DEPTGSLDPKNRDEVLDLLLELN-DEGKTIIIVTHDPEVAKQADRVIEL 206
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6-205 |
2.95e-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: 173.54 E-value: 2.95e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 6 VIEVHHVAKRVGEGENQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEGRAAL 85
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 86 RaRDIGFVFQSFMLVPTLTALENVQLPALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARP 165
Cdd:cd03258 81 R-RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 502612564 166 QILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTH 205
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITH 199
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
6-210 |
1.12e-53 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 172.49 E-value: 1.12e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 6 VIEVHHVAKRVGEGEnqisILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSqLDEEGRAAL 85
Cdd:COG1126 1 MIEIENLHKSFGDLE----VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 86 RaRDIGFVFQSFMLVPTLTALENVQL-PALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSAR 164
Cdd:COG1126 76 R-RKVGMVFQQFNLFPHLTVLENVTLaPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAME 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 502612564 165 PQILFADEPTGNLD-RQTGDrIADLLFELnQRQATTLVMVTHDVQLA 210
Cdd:COG1126 155 PKVMLFDEPTSALDpELVGE-VLDVMRDL-AKEGMTMVVVTHEMGFA 199
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
7-212 |
2.31e-53 |
|
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: 170.78 E-value: 2.31e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGEgenqISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLdeegraALR 86
Cdd:cd03259 1 LELKGLSKTYGS----VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGV------PPE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 87 ARDIGFVFQSFMLVPTLTALENVQLPALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQ 166
Cdd:cd03259 71 RRNIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPS 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 502612564 167 ILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAAR 212
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALA 196
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-215 |
4.40e-53 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 178.17 E-value: 4.40e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 3 AQNVIEVHHVAKR-VGEGENQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEG 81
Cdd:COG1123 257 AEPLLEVRNLSKRyPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRS 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 82 RAALRaRDIGFVFQ--SFMLVPTLTALENVQLPALLRGE-REHDSRQRAAALLTQLGLGQRLRH-LPAQLSGGEQQRVAL 157
Cdd:COG1123 337 LRELR-RRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPPDLADrYPHELSGGQRQRVAI 415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502612564 158 ARAFSARPQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAAR-CQR 215
Cdd:COG1123 416 ARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYiADR 474
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
7-206 |
2.06e-52 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 172.18 E-value: 2.06e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGEGENQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEGRAALR 86
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 87 aRDIGFVFQSFMLVPTLTALENVQLPALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQ 166
Cdd:COG1135 82 -RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 502612564 167 ILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHD 206
Cdd:COG1135 161 VLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHE 200
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
7-224 |
2.20e-51 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 165.37 E-value: 2.20e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGEGEnqisILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEgraALR 86
Cdd:COG4619 1 LELEGLSFRVGGKP----ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPP---EWR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 87 aRDIGFVFQSFMLVPTlTALENVQLPALLRGERehDSRQRAAALLTQLGLGQRLRHLPA-QLSGGEQQRVALARAFSARP 165
Cdd:COG4619 74 -RQVAYVPQEPALWGG-TVRDNLPFPFQLRERK--FDRERALELLERLGLPPDILDKPVeRLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 166 QILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAAR-CQRRLRLVDGTL 224
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
7-222 |
5.83e-51 |
|
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: 165.43 E-value: 5.83e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGEGENqisILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLdeeGRAALR 86
Cdd:cd03256 1 IEVENLSKTYPNGKK---ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKL---KGKALR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 87 A--RDIGFVFQSFMLVPTLTALENV---------QLPALLRGEREHDsRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRV 155
Cdd:cd03256 75 QlrRQIGMIFQQFNLIERLSVLENVlsgrlgrrsTWRSLFGLFPKEE-KQRALAALERVGLLDKAYQRADQLSGGQQQRV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502612564 156 ALARAFSARPQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAAR-CQRRLRLVDG 222
Cdd:cd03256 154 AIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREyADRIVGLKDG 221
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
7-210 |
1.53e-50 |
|
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: 163.47 E-value: 1.53e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGEGEnqisILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQlDEEGRAALR 86
Cdd:cd03262 1 IEIKNLHKSFGDFH----VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 87 ARdIGFVFQSFMLVPTLTALENVQL-PALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARP 165
Cdd:cd03262 76 QK-VGMVFQQFNLFPHLTVLENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 502612564 166 QILFADEPTGNLDRQTGDRIADLLFELNQRQaTTLVMVTHDVQLA 210
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAEEG-MTMVVVTHEMGFA 198
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
7-206 |
3.52e-50 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 166.79 E-value: 3.52e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGEGEnqisILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEegraalR 86
Cdd:COG3839 4 LELENVSKSYGGVE----ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPP------K 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 87 ARDIGFVFQSFMLVPTLTALENVQLPALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQ 166
Cdd:COG3839 74 DRNIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPK 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 502612564 167 ILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHD 206
Cdd:COG3839 154 VFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHD 193
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
7-227 |
1.16e-49 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 161.77 E-value: 1.16e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGEGEnqisILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSqldeEGRAALR 86
Cdd:COG1131 1 IEVRGLTKRYGDKT----ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA----RDPAEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 87 ARdIGFVFQSFMLVPTLTALENVQLPALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQ 166
Cdd:COG1131 73 RR-IGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502612564 167 ILFADEPTGNLDRQTGDRIADLLFELNQRQaTTLVMVTHDVQLAAR-CQR-------RLrLVDGTLREV 227
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLRELAAEG-KTVLLSTHYLEEAERlCDRvaiidkgRI-VADGTPDEL 218
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
8-223 |
5.25e-49 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 159.55 E-value: 5.25e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 8 EVHHVAKRVGEGENQIsiLTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDeegrAALRA 87
Cdd:cd03225 1 ELKNLSFSYPDGARPA--LDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLS----LKELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 88 RDIGFVFQSF--MLVpTLTALENVQLPALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARP 165
Cdd:cd03225 75 RKVGLVFQNPddQFF-GPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502612564 166 QILFADEPTGNLDRQTGDRIADLLFELNQrQATTLVMVTHDVQLAAR-CQRRLRLVDGT 223
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKA-EGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
7-223 |
5.36e-49 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 158.50 E-value: 5.36e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGegenQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEGRAalR 86
Cdd:cd03229 1 LELKNVSKRYG----QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPP--L 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 87 ARDIGFVFQSFMLVPTLTALENVQLPallrgerehdsrqraaalltqlglgqrlrhlpaqLSGGEQQRVALARAFSARPQ 166
Cdd:cd03229 75 RRRIGMVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502612564 167 ILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAAR-CQRRLRLVDGT 223
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
6-222 |
1.73e-47 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 156.79 E-value: 1.73e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 6 VIEVHHVAKRVGegenQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGqpLSQLDEEGRAAL 85
Cdd:PRK09493 1 MIEFKNVSKHFG----PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG--LKVNDPKVDERL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 86 RARDIGFVFQSFMLVPTLTALENVQL-PALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSAR 164
Cdd:PRK09493 75 IRQEAGMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502612564 165 PQILFADEPTGNLD---RQTGDRIADLLFElnqrQATTLVMVTHDVQLAARCQRRLRLVDG 222
Cdd:PRK09493 155 PKLMLFDEPTSALDpelRHEVLKVMQDLAE----EGMTMVIVTHEIGFAEKVASRLIFIDK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
7-227 |
4.38e-47 |
|
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: 155.18 E-value: 4.38e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGEGENqisILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSqldEEGRAALR 86
Cdd:COG1122 1 IELENLSFSYPGGTP---ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDIT---KKNLRELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 87 aRDIGFVFQS-----FMLvptlTALENVQLPALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAF 161
Cdd:COG1122 75 -RKVGLVFQNpddqlFAP----TVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502612564 162 SARPQILFADEPTGNLDRQTGDRIADLLFELNQRQaTTLVMVTHDVQLAAR-CQRRL-----RLV-DGTLREV 227
Cdd:COG1122 150 AMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEG-KTVIIVTHDLDLVAElADRVIvlddgRIVaDGTPREV 221
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
7-215 |
7.51e-46 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 155.30 E-value: 7.51e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGegenQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQldeegRAALR 86
Cdd:COG1118 3 IEVRNISKRFG----SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFT-----NLPPR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 87 ARDIGFVFQSFMLVPTLTALENVQ--LPALLRGEREhdSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSAR 164
Cdd:COG1118 74 ERRVGFVFQHYALFPHMTVAENIAfgLRVRPPSKAE--IRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 502612564 165 PQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAAR-CQR 215
Cdd:COG1118 152 PEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALElADR 203
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
6-226 |
1.33e-45 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 154.57 E-value: 1.33e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 6 VIEVHHVAKRVGEGENQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEGRAAL 85
Cdd:PRK11153 1 MIELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 86 RaRDIGFVFQSFMLVPTLTALENVQLPALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARP 165
Cdd:PRK11153 81 R-RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502612564 166 QILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAAR-CQRRLRLVDGTLRE 226
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRiCDRVAVIDAGRLVE 221
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-215 |
2.31e-45 |
|
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: 153.29 E-value: 2.31e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 6 VIEVHHVAKRVGEGENQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDA---SAGEVRLLGQPLSQLDEEGR 82
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 83 AALRARDIGFVFQSFM--LVPTLTALENVQLPALL-RGEREHDSRQRAAALLTQLGL---GQRLRHLPAQLSGGEQQRVA 156
Cdd:COG0444 81 RKIRGREIQMIFQDPMtsLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 157 LARAFSARPQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAAR-CQR 215
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEiADR 220
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-226 |
2.73e-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: 157.76 E-value: 2.73e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 4 QNVIEVHHVAKRVGEGENQIsiLTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASA---GEVRLLGQPLSQLDEe 80
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVPA--VDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 81 graALRARDIGFVFQSFM--LVPtLTALENVQLPALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALA 158
Cdd:COG1123 79 ---ALRGRRIGMVFQDPMtqLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502612564 159 RAFSARPQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAAR-CQRRLRLVDGTLRE 226
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEiADRVVVMDDGRIVE 223
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
7-222 |
1.76e-44 |
|
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: 148.99 E-value: 1.76e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGEGENQISILTavdLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEgraALR 86
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLN---LEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPV---ELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 87 aRDIGFVFQSFMLVPTLTALENVQLPALLRGEREHDSRQRAAALLTQLGL--GQRLRHLPAQLSGGEQQRVALARAFSAR 164
Cdd:cd03295 75 -RKIGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502612564 165 PQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAARCQRRLRLVDG 222
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKN 211
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
29-212 |
1.78e-44 |
|
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: 149.72 E-value: 1.78e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 29 VDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEGRAALRARDIGFVFQSFMLVPTLTALEN 108
Cdd:cd03294 43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTVLEN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 109 VQLPALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEPTGNLDRQTGDRIADL 188
Cdd:cd03294 123 VAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDE 202
|
170 180
....*....|....*....|....
gi 502612564 189 LFELNQRQATTLVMVTHDVQLAAR 212
Cdd:cd03294 203 LLRLQAELQKTIVFITHDLDEALR 226
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
7-228 |
2.46e-44 |
|
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: 148.10 E-value: 2.46e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGEGEnqisILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDA-----SAGEVRLLGQPLSQLDEEg 81
Cdd:cd03260 1 IELRDLNVYYGDKH----ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVD- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 82 RAALRARdIGFVFQSFMLVPtLTALENVQLPALLRGEREHDSR-QRAAALLTQLGLGQRL--RHLPAQLSGGEQQRVALA 158
Cdd:cd03260 76 VLELRRR-VGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELdERVEEALRKAALWDEVkdRLHALGLSGGQQQRLCLA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502612564 159 RAFSARPQILFADEPTGNLDRQTGDRIADLLFELNQRqaTTLVMVTHDVQLAARCQRR-LRLVDGTLREVA 228
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRtAFLLNGRLVEFG 222
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
6-212 |
4.30e-44 |
|
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: 148.27 E-value: 4.30e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 6 VIEVHHVAKRVGEGEnqisILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLdeegRAAL 85
Cdd:COG1120 1 MLEAENLSVGYGGRP----VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASL----SRRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 86 RARDIGFVFQSFMLVPTLTALENVQL---P--ALLRGEREHDsRQRAAALLTQLGLGQrLRHLP-AQLSGGEQQRVALAR 159
Cdd:COG1120 73 LARRIAYVPQEPPAPFGLTVRELVALgryPhlGLFGRPSAED-REAVEEALERTGLEH-LADRPvDELSGGERQRVLIAR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502612564 160 AFSARPQILFADEPTGNLD--RQTgdRIADLLFELNQRQATTLVMVTHDVQLAAR 212
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHLDlaHQL--EVLELLRRLARERGRTVVMVLHDLNLAAR 203
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
7-206 |
4.58e-44 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 150.96 E-value: 4.58e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGegenQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSqldeegRAALR 86
Cdd:TIGR03265 5 LSIDNIRKRFG----AFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDIT------RLPPQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 87 ARDIGFVFQSFMLVPTLTALENVQLPALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQ 166
Cdd:TIGR03265 75 KRDYGIVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPG 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 502612564 167 ILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHD 206
Cdd:TIGR03265 155 LLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHD 194
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
7-206 |
3.26e-43 |
|
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: 145.46 E-value: 3.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGegenQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEgraalr 86
Cdd:cd03300 1 IELENVSKFYG----GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 87 ARDIGFVFQSFMLVPTLTALENVQLPALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQ 166
Cdd:cd03300 71 KRPVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 502612564 167 ILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHD 206
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHD 190
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-224 |
5.49e-43 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 145.23 E-value: 5.49e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 1 MPAQNVIEVHHVakRVGEGENQIsiLTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQldee 80
Cdd:COG1121 1 MMMMPAIELENL--TVSYGGRPV--LEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 81 graalRARDIGFVFQSFMLVPT--LTALENV------QLPALLRGEREHdsRQRAAALLTQLGLGQRLRHLPAQLSGGEQ 152
Cdd:COG1121 73 -----ARRRIGYVPQRAEVDWDfpITVRDVVlmgrygRRGLFRRPSRAD--REAVDEALERVGLEDLADRPIGELSGGQQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502612564 153 QRVALARAFSARPQILFADEPTGNLDRQTGDRIADLLFELNQRQaTTLVMVTHDVQLAARCQRRLRLVDGTL 224
Cdd:COG1121 146 QRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREG-KTILVVTHDLGAVREYFDRVLLLNRGL 216
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
6-219 |
2.19e-42 |
|
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: 142.23 E-value: 2.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 6 VIEVHHVAKRVGEGEnqisILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEGRaal 85
Cdd:COG4133 2 MLEAENLSCRRGERL----LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYR--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 86 raRDIGFVFQSFMLVPTLTALENVQLPALLRGERehDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARP 165
Cdd:COG4133 75 --RRLAYLGHADGLKPELTVRENLRFWAALYGLR--ADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502612564 166 QILFADEPTGNLDRQTGDRIADLLFELNQRQAtTLVMVTHDvQLAARCQRRLRL 219
Cdd:COG4133 151 PLWLLDEPFTALDAAGVALLAELIAAHLARGG-AVLLTTHQ-PLELAAARVLDL 202
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
7-208 |
3.25e-42 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 144.85 E-value: 3.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGEGEnqisilTAVD---LVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEgra 83
Cdd:COG1125 2 IEFENVTKRYPDGT------VAVDdlsLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPV--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 84 ALRaRDIGFVFQSFMLVPTLTALENVQLPALLRGEREHDSRQRAAALLTQLGL-GQRLRH-LPAQLSGGEQQRVALARAF 161
Cdd:COG1125 73 ELR-RRIGYVIQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdPEEYRDrYPHELSGGQQQRVGVARAL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 502612564 162 SARPQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQ 208
Cdd:COG1125 152 AADPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDID 198
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
7-210 |
3.52e-42 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 143.46 E-value: 3.52e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGEGENQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLsqldeEGRAALR 86
Cdd:COG4525 4 LTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV-----TGPGADR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 87 ardiGFVFQSFMLVPTLTALENVQLPALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQ 166
Cdd:COG4525 79 ----GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 502612564 167 ILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLA 210
Cdd:COG4525 155 FLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEA 198
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
6-222 |
3.83e-42 |
|
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: 142.82 E-value: 3.83e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 6 VIEVHHVAKRVGegeNQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEGRAAL 85
Cdd:TIGR02315 1 MLEVENLSKVYP---NGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 86 RARdIGFVFQSFMLVPTLTALENV---------QLPALLRGEREHDsRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVA 156
Cdd:TIGR02315 78 RRR-IGMIFQHYNLIERLTVLENVlhgrlgykpTWRSLLGRFSEED-KERALSALERVGLADKAYQRADQLSGGQQQRVA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502612564 157 LARAFSARPQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAAR-CQRRLRLVDG 222
Cdd:TIGR02315 156 IARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKyADRIVGLKAG 222
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
4-206 |
5.05e-42 |
|
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: 142.19 E-value: 5.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 4 QNVIEVHHVAKRV---GEGENQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLL--GQP--LSQ 76
Cdd:COG4778 2 TTLLEVENLSKTFtlhLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdGGWvdLAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 77 LDEEGRAALRARDIGFVFQSFMLVPTLTALENVQLPALLRGEREHDSRQRAAALLTQLGLGQRLRHL-PAQLSGGEQQRV 155
Cdd:COG4778 82 ASPREILALRRRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERLWDLpPATFSGGEQQRV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502612564 156 ALARAFSARPQILFADEPTGNLDRQTGDRIADLLFELnQRQATTLVMVTHD 206
Cdd:COG4778 162 NIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHD 211
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
7-210 |
1.63e-41 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 144.46 E-value: 1.63e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGEGEnqisILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEegraalR 86
Cdd:PRK10851 3 IEIANIKKSFGRTQ----VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHA------R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 87 ARDIGFVFQSFMLVPTLTALENVQ--LPALLRGER--EHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFS 162
Cdd:PRK10851 73 DRKVGFVFQHYALFRHMTVFDNIAfgLTVLPRRERpnAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502612564 163 ARPQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLA 210
Cdd:PRK10851 153 VEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEA 200
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
7-206 |
2.73e-41 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 140.71 E-value: 2.73e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGEgenqISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDeegraaLR 86
Cdd:TIGR00968 1 IEIANISKRFGS----FQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVH------AR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 87 ARDIGFVFQSFMLVPTLTALENVQLPALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQ 166
Cdd:TIGR00968 71 DRKIGFVFQHYALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQ 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 502612564 167 ILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHD 206
Cdd:TIGR00968 151 VLLLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHD 190
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
26-174 |
3.10e-41 |
|
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: 137.78 E-value: 3.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 26 LTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDeegRAALRARdIGFVFQSFMLVPTLTA 105
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDE---RKSLRKE-IGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502612564 106 LENVQLPALLRGEREHDSRQRAAALLTQLGLG----QRLRHLPAQLSGGEQQRVALARAFSARPQILFADEPT 174
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDARAEEALEKLGLGdladRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
7-222 |
6.33e-41 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 137.51 E-value: 6.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGEGENQIsiLTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDeegRAALR 86
Cdd:cd03228 1 IEFKNVSFSYPGRPKPV--LKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLD---LESLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 87 ARdIGFVFQSFMLVPTlTALENVqlpallrgerehdsrqraaalltqlglgqrlrhlpaqLSGGEQQRVALARAFSARPQ 166
Cdd:cd03228 76 KN-IAYVPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502612564 167 ILFADEPTGNLDRQTGDRIADLLFELnqRQATTLVMVTHDVQLAARCQRRLRLVDG 222
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRAL--AKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
26-224 |
9.65e-41 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 138.85 E-value: 9.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 26 LTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEGRAALRaRDIGFVFQSFMLVPTLTA 105
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLR-RQIGMIFQDHHLLMDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 106 LENVQLPALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEPTGNLDRQTGDRI 185
Cdd:PRK10908 97 YDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 502612564 186 ADLLFELNqRQATTLVMVTHDVQL-AARCQRRLRLVDGTL 224
Cdd:PRK10908 177 LRLFEEFN-RVGVTVLMATHDIGLiSRRSYRMLTLSDGHL 215
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
7-224 |
9.91e-41 |
|
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: 137.14 E-value: 9.91e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGEGEnqisILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEGRaalr 86
Cdd:cd03230 1 IEVRNLSKRYGKKT----ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVK---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 87 aRDIGFVFQSFMLVPTLTALENVqlpallrgerehdsrqraaalltqlglgqrlrhlpaQLSGGEQQRVALARAFSARPQ 166
Cdd:cd03230 73 -RRIGYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502612564 167 ILFADEPTGNLDRQTGDRIADLLFELNQRQaTTLVMVTHDVQLAAR-CQRRLRLVDGTL 224
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKEG-KTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-226 |
4.35e-40 |
|
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: 144.52 E-value: 4.35e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 2 PAQNVIEVHHVakRVGEGENQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEg 81
Cdd:COG4987 329 PGGPSLELEDV--SFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDED- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 82 raALRARdIGFVFQSFMLVPTlTALENVQLPallrgeREHDSRQRAAALLTQLGLGQRLRHLP-----------AQLSGG 150
Cdd:COG4987 406 --DLRRR-IAVVPQRPHLFDT-TLRENLRLA------RPDATDEELWAALERVGLGDWLAALPdgldtwlgeggRRLSGG 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502612564 151 EQQRVALARAFSARPQILFADEPTGNLDRQTGDRIADLLFELNQRQatTLVMVTHDVQLAARCQRRLRLVDGTLRE 226
Cdd:COG4987 476 ERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLAGLERMDRILVLEDGRIVE 549
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
6-215 |
7.73e-40 |
|
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: 137.48 E-value: 7.73e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 6 VIEVHHVAKRVGEgenqisiLTAVD---LVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEGR 82
Cdd:COG0411 4 LLEVRGLTKRFGG-------LVAVDdvsLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 83 AALRardIGFVFQSFMLVPTLTALENVQLPALLRG---------------EREHDSRQRAAALLTQLGLGQRLRHLPAQL 147
Cdd:COG0411 77 ARLG---IARTFQNPRLFPELTVLENVLVAAHARLgrgllaallrlprarREEREARERAEELLERVGLADRADEPAGNL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502612564 148 SGGEQQRVALARAFSARPQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAAR-CQR 215
Cdd:COG0411 154 SYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGlADR 222
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
7-206 |
1.19e-39 |
|
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: 136.31 E-value: 1.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGegenQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDeegraaLR 86
Cdd:cd03296 3 IEVRNVSKRFG----DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP------VQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 87 ARDIGFVFQSFMLVPTLTALENVQ--LPALLRGER--EHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFS 162
Cdd:cd03296 73 ERNVGFVFQHYALFRHMTVFDNVAfgLRVKPRSERppEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 502612564 163 ARPQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHD 206
Cdd:cd03296 153 VEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHD 196
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6-212 |
4.08e-39 |
|
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: 134.99 E-value: 4.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 6 VIEVHHVAKRVGEGEnqisILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEGRaal 85
Cdd:COG4555 1 MIEVENLSKKYGKVP----ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREAR--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 86 raRDIGFVFQSFMLVPTLTALENVQLPALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARP 165
Cdd:COG4555 74 --RQIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDP 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 502612564 166 QILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVmVTHDVQLAAR 212
Cdd:COG4555 152 KVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLF-SSHIMQEVEA 197
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
7-210 |
4.11e-39 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 135.14 E-value: 4.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGEGEnqisILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLS---QLDEEGRA 83
Cdd:COG4161 3 IQLKNINCFYGSHQ----ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsqKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 84 ALRaRDIGFVFQSFMLVPTLTALEN-VQLPALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFS 162
Cdd:COG4161 79 LLR-QKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502612564 163 ARPQILFADEPTGNLDRQTGDRIADLLFELNQrQATTLVMVTHDVQLA 210
Cdd:COG4161 158 MEPQVLLFDEPTAALDPEITAQVVEIIRELSQ-TGITQVIVTHEVEFA 204
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
7-206 |
3.17e-38 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 131.99 E-value: 3.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGEgenqISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEgraalr 86
Cdd:cd03301 1 VELENVTKRFGN----VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 87 ARDIGFVFQSFMLVPTLTALENVQLPALLRG--EREHDSRQRAAALLtqLGLGQRLRHLPAQLSGGEQQRVALARAFSAR 164
Cdd:cd03301 71 DRDIAMVFQNYALYPHMTVYDNIAFGLKLRKvpKDEIDERVREVAEL--LQIEHLLDRKPKQLSGGQRQRVALGRAIVRE 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 502612564 165 PQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHD 206
Cdd:cd03301 149 PKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHD 190
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
7-228 |
4.44e-38 |
|
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: 132.18 E-value: 4.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGEgenqISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEGRAALR 86
Cdd:cd03219 1 LEVRGLTKRFGG----LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 87 ardIGFVFQSFMLVPTLTALENVQLPALLRG----------EREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVA 156
Cdd:cd03219 77 ---IGRTFQIPRLFPELTVLENVMVAAQARTgsglllararREEREARERAEELLERVGLADLADRPAGELSYGQQRRLE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 157 LARAFSARPQILFADEPTGNLDRQTGDRIADLLFELNQRqATTLVMVTHDVQLAAR-CQR-------RLrLVDGTLREVA 228
Cdd:cd03219 154 IARALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSlADRvtvldqgRV-IAEGTPDEVR 231
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
8-223 |
2.15e-37 |
|
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: 128.13 E-value: 2.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 8 EVHHVAKRVGEGEnqisILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEgraaLRA 87
Cdd:cd00267 1 EIENLSFRYGGRT----ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLE----ELR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 88 RDIGFVFQsfmlvptltalenvqlpallrgerehdsrqraaalltqlglgqrlrhlpaqLSGGEQQRVALARAFSARPQI 167
Cdd:cd00267 73 RRIGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502612564 168 LFADEPTGNLDRQTGDRIADLLFELNQRQAtTLVMVTHDVQLAAR-CQRRLRLVDGT 223
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEEGR-TVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-212 |
2.52e-37 |
|
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: 136.35 E-value: 2.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 1 MPAQNVIEVHHVAKRVGEGENQISILTAVDLVVKRGQSLALIGESGSGKS-TLLGILAGLDDASA---GEVRLLGQPLSQ 76
Cdd:COG4172 1 MMSMPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPAAhpsGSILFDGQDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 77 LDEEGRAALRARDIGFVFQSFMlvptlTAL-----------ENVQLPALLRGErehDSRQRAAALLTQLGL---GQRLRH 142
Cdd:COG4172 81 LSERELRRIRGNRIAMIFQEPM-----TSLnplhtigkqiaEVLRLHRGLSGA---AARARALELLERVGIpdpERRLDA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 143 LPAQLSGGEQQRVALARAFSARPQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAAR 212
Cdd:COG4172 153 YPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRR 222
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
30-221 |
4.16e-37 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 129.49 E-value: 4.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 30 DLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEgraalrARDIGFVFQSFMLVPTLTALENV 109
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA------ERPVSMLFQENNLFPHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 110 QL---PALLRGEREhdsRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAF-SARPqILFADEPTGNLD---RQtg 182
Cdd:COG3840 93 GLglrPGLKLTAEQ---RAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLvRKRP-ILLLDEPFSALDpalRQ-- 166
|
170 180 190
....*....|....*....|....*....|....*....
gi 502612564 183 dRIADLLFELNQRQATTLVMVTHDVQLAARCQRRLRLVD 221
Cdd:COG3840 167 -EMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVA 204
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
26-210 |
5.50e-37 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 129.12 E-value: 5.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 26 LTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQplsQLDEEGRaalrarDIGFVFQSFMLVPTLTA 105
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGK---QITEPGP------DRMVVFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 106 LENVQLP--ALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEPTGNLDRQTGD 183
Cdd:TIGR01184 72 RENIALAvdRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180
....*....|....*....|....*..
gi 502612564 184 RIADLLFELNQRQATTLVMVTHDVQLA 210
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTHDVDEA 178
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
7-226 |
6.52e-37 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 136.50 E-value: 6.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGEGENQIsiLTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDeegRAALR 86
Cdd:COG2274 474 IELENVSFRYPGDSPPV--LDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQID---PASLR 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 87 aRDIGFVFQSFMLVPTlTALENvqlpalLRGEREHDSRQRAAALLTQLGLGQRLRHLP-----------AQLSGGEQQRV 155
Cdd:COG2274 549 -RQIGVVLQDVFLFSG-TIREN------ITLGDPDATDEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRL 620
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502612564 156 ALARAFSARPQILFADEPTGNLDRQTGDRIADLLFELNQRQatTLVMVTHDVQLAARCQRRLRLVDGTLRE 226
Cdd:COG2274 621 AIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGR--TVIIIAHRLSTIRLADRIIVLDKGRIVE 689
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
8-224 |
6.70e-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: 128.14 E-value: 6.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 8 EVHHVAKRVGEGenqISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDeegraalRA 87
Cdd:cd03226 1 RIENISFSYKKG---TEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE-------RR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 88 RDIGFV-----FQSFMlvptltalENVQLPALLRGEREHDSRQRAAALLTQLGL-GQRLRHlPAQLSGGEQQRVALARAF 161
Cdd:cd03226 71 KSIGYVmqdvdYQLFT--------DSVREELLLGLKELDAGNEQAETVLKDLDLyALKERH-PLSLSGGQKQRLAIAAAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502612564 162 SARPQILFADEPTGNLDRQTGDRIADLLFELnQRQATTLVMVTHDVQLAAR-CQRRLRLVDGTL 224
Cdd:cd03226 142 LSGKDLLIFDEPTSGLDYKNMERVGELIREL-AAQGKAVIVITHDYEFLAKvCDRVLLLANGAI 204
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
6-226 |
9.41e-37 |
|
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: 129.54 E-value: 9.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 6 VIEVHHVAKRVGEG-----ENQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEE 80
Cdd:TIGR02769 2 LLEVRDVTHTYRTGglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 81 GRAALRaRDIGFVFQSFM--LVPTLTALENVQLPaLLRGEREHDSRQ--RAAALLTQLGL-GQRLRHLPAQLSGGEQQRV 155
Cdd:TIGR02769 82 QRRAFR-RDVQLVFQDSPsaVNPRMTVRQIIGEP-LRHLTSLDESEQkaRIAELLDMVGLrSEDADKLPRQLSGGQLQRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502612564 156 ALARAFSARPQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAAR-CQRRLRLVDGTLRE 226
Cdd:TIGR02769 160 NIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVE 231
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
26-227 |
1.05e-36 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 131.74 E-value: 1.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 26 LTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEgraalrARDIGFVFQSFMLVPTLTA 105
Cdd:NF040840 16 LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPE------KRGIAYVYQNYMLFPHKTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 106 LENVQLPALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEPTGNLDRQTGDRI 185
Cdd:NF040840 90 FENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDEL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 502612564 186 ADLLFELNQRQATTLVMVTHD----VQLAARC--QRRLRLVD-GTLREV 227
Cdd:NF040840 170 IREMKRWHREFGFTAIHVTHNfeeaLSLADRVgiMLNGRLSQvGDVREV 218
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
19-210 |
1.26e-36 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 128.59 E-value: 1.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 19 GENQIsiLTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPL---SQLDEEGRAALRaRDIGFVFQ 95
Cdd:PRK11124 13 GAHQA--LFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAIRELR-RNVGMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 96 SFMLVPTLTALEN-VQLPALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEPT 174
Cdd:PRK11124 90 QYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPT 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 502612564 175 GNLDRQTGDRIADLLFELNQrQATTLVMVTHDVQLA 210
Cdd:PRK11124 170 AALDPEITAQIVSIIRELAE-TGITQVIVTHEVEVA 204
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
7-227 |
1.62e-36 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 128.22 E-value: 1.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGEGEnqisiLTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEgraalr 86
Cdd:cd03299 1 LKVENLSKDWKEFK-----LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 87 ARDIGFVFQSFMLVPTLTALENVQ--LPALLRGEREHDSRQRAAALLtqLGLGQRLRHLPAQLSGGEQQRVALARAFSAR 164
Cdd:cd03299 70 KRDISYVPQNYALFPHMTVYKNIAygLKKRKVDKKEIERKVLEIAEM--LGIDHLLNRKPETLSGGEQQRVAIARALVVN 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 165 PQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAARCQRRL------RLVD-GTLREV 227
Cdd:cd03299 148 PKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVaimlngKLIQvGKPEEV 217
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
5-226 |
2.06e-36 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 129.04 E-value: 2.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 5 NVIEVHHVAKR------VGEGENQiSILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLD 78
Cdd:PRK10419 2 TLLNVSGLSHHyahgglSGKHQHQ-TVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 79 EEGRAALRaRDIGFVFQ-SFMLV-PTLTALENVQLP-----ALLRGEREHdsrqRAAALLTQLGLG-QRLRHLPAQLSGG 150
Cdd:PRK10419 81 RAQRKAFR-RDIQMVFQdSISAVnPRKTVREIIREPlrhllSLDKAERLA----RASEMLRAVDLDdSVLDKRPPQLSGG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502612564 151 EQQRVALARAFSARPQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAAR-CQRRLRLVDGTLRE 226
Cdd:PRK10419 156 QLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
7-225 |
2.34e-36 |
|
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: 127.24 E-value: 2.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGEGENqisilTAVDLV---VKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQldeeGRA 83
Cdd:cd03263 1 LQIRNLTKTYKKGTK-----PAVDDLslnVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT----DRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 84 ALRaRDIGFVFQSFMLVPTLTALENVQLPALLRGEREHDSRQRAAALLTQLGLGQrLRHLPA-QLSGGEQQRVALARAFS 162
Cdd:cd03263 72 AAR-QSLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTD-KANKRArTLSGGMKRKLSLAIALI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502612564 163 ARPQILFADEPTGNLDRQTGDRIADLLfeLNQRQATTLVMVTHDVQLAAR-CQRRLRLVDGTLR 225
Cdd:cd03263 150 GGPSVLLLDEPTSGLDPASRRAIWDLI--LEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLR 211
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
12-210 |
1.17e-35 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 126.72 E-value: 1.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 12 VAKRVGEGEnqisILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEGRaalrardig 91
Cdd:PRK11247 18 VSKRYGERT----VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTR--------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 92 FVFQSFMLVPTLTALENVQLPalLRGerehDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQILFAD 171
Cdd:PRK11247 85 LMFQDARLLPWKKVIDNVGLG--LKG----QWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLD 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 502612564 172 EPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLA 210
Cdd:PRK11247 159 EPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEA 197
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
21-221 |
4.68e-35 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 123.75 E-value: 4.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 21 NQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAG-LDDA--SAGEVRLLGQPLSQLDEEgraalrARDIGFVFQSF 97
Cdd:COG4136 12 GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAfsASGEVLLNGRRLTALPAE------QRRIGILFQDD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 98 MLVPTLTALENVQL---PALLRGERehdsRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEPT 174
Cdd:COG4136 86 LLFPHLSVGENLAFalpPTIGRAQR----RARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPF 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 502612564 175 GNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAARCQRRLRLVD 221
Cdd:COG4136 162 SKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAAGRVLDLGN 208
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
2-178 |
5.03e-35 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 124.91 E-value: 5.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 2 PAQNVIEVHHVAKRVGEGEnqisILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLsQLDEEG 81
Cdd:COG4598 4 TAPPALEVRDLHKSFGDLE----VLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEI-RLKPDR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 82 RAALRARD----------IGFVFQSFMLVPTLTALENV-QLPALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGG 150
Cdd:COG4598 79 DGELVPADrrqlqrirtrLGMVFQSFNLWSHMTVLENViEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGG 158
|
170 180
....*....|....*....|....*...
gi 502612564 151 EQQRVALARAFSARPQILFADEPTGNLD 178
Cdd:COG4598 159 QQQRAAIARALAMEPEVMLFDEPTSALD 186
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4-222 |
5.24e-35 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 125.13 E-value: 5.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 4 QNVIEVHHVAKRVgegeNQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGL---DDASAGEVRLLGQPLSQldeE 80
Cdd:PRK09984 2 QTIIRVEKLAKTF----NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQR---E 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 81 GRAAlraRDI-------GFVFQSFMLVPTLTALENVQLPALlrGER----------EHDSRQRAAALLTQLGLGQRLRHL 143
Cdd:PRK09984 75 GRLA---RDIrksrantGYIFQQFNLVNRLSVLENVLIGAL--GSTpfwrtcfswfTREQKQRALQALTRVGMVHFAHQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 144 PAQLSGGEQQRVALARAFSARPQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAAR-CQRRLRLVDG 222
Cdd:PRK09984 150 VSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRyCERIVALRQG 229
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-228 |
6.76e-35 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 129.88 E-value: 6.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 2 PAQNVIEVHHVAKRVGEGENqisILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEeg 81
Cdd:COG4988 332 AGPPSIELEDVSFSYPGGRP---ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDP-- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 82 rAALRARdIGFVFQSFMLVPTlTALENvqlpalLRGEREHDSRQRAAALLTQLGLGQRLRHLP-----------AQLSGG 150
Cdd:COG4988 407 -ASWRRQ-IAWVPQNPYLFAG-TIREN------LRLGRPDASDEELEAALEAAGLDEFVAALPdgldtplgeggRGLSGG 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502612564 151 EQQRVALARAFSARPQILFADEPTGNLDRQTGDRIADLLFELNQRQatTLVMVTHDVQLAARCQRRLRLVDGTLREVA 228
Cdd:COG4988 478 QAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALLAQADRILVLDDGRIVEQG 553
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
29-225 |
7.32e-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: 123.17 E-value: 7.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 29 VDLVVKrGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLsqLDEEGRAAL--RARDIGFVFQSFMLVPTLTAL 106
Cdd:cd03297 17 IDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVL--FDSRKKINLppQQRKIGLVFQQYALFPHLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 107 ENVQLPalLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEPTGNLDRQTGDRIA 186
Cdd:cd03297 94 ENLAFG--LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 502612564 187 DLLFELNQRQATTLVMVTHDVQLAAR-CQRRLRLVDGTLR 225
Cdd:cd03297 172 PELKQIKKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQ 211
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
41-206 |
1.25e-34 |
|
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: 125.68 E-value: 1.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 41 LIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEGRAalrardIGFVFQSFMLVPTLTALENVQLPALLRGERE 120
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRH------INMVFQSYALFPHMTVEENVAFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 121 HDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEPTGNLDRQTGDRIADLLFELNQRQATTL 200
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITF 154
|
....*.
gi 502612564 201 VMVTHD 206
Cdd:TIGR01187 155 VFVTHD 160
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
25-222 |
1.59e-34 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 123.32 E-value: 1.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 25 ILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRL------LGQPLSQLDEEGRAaLRaRDIGFVFQSFM 98
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidTARSLSQQKGLIRQ-LR-QHVGFVFQNFN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 99 LVPTLTALENV-QLPALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEPTGNL 177
Cdd:PRK11264 96 LFPHRTVLENIiEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSAL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 502612564 178 DRQTGDRIADLLFELNQRQaTTLVMVTHDVQLAARCQRRLRLVDG 222
Cdd:PRK11264 176 DPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQ 219
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
8-213 |
9.67e-34 |
|
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: 119.46 E-value: 9.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 8 EVHHVAKRVGEGEnqisILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDeegrAALRA 87
Cdd:cd03214 1 EVENLSVGYGGRT----VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLS----PKELA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 88 RDIGFVFQsfmlvptltALENVQLPALLrgEREHDsrqraaalltqlglgqrlrhlpaQLSGGEQQRVALARAFSARPQI 167
Cdd:cd03214 73 RKIAYVPQ---------ALELLGLAHLA--DRPFN-----------------------ELSGGERQRVLLARALAQEPPI 118
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 502612564 168 LFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAARC 213
Cdd:cd03214 119 LLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARY 164
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
29-210 |
3.00e-33 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 123.02 E-value: 3.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 29 VDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEegraalRARDIGFVFQSFMLVPTLTALEN 108
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP------YQRPINMMFQSYALFPHMTVEQN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 109 VQL----PALLRGErehdSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEPTGNLDRQTGDR 184
Cdd:PRK11607 112 IAFglkqDKLPKAE----IASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDR 187
|
170 180
....*....|....*....|....*.
gi 502612564 185 IADLLFELNQRQATTLVMVTHDVQLA 210
Cdd:PRK11607 188 MQLEVVDILERVGVTCVMVTHDQEEA 213
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-206 |
4.24e-33 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 122.14 E-value: 4.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 1 MPAQNVIEVHHVAKRVGEGenqiSILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQldee 80
Cdd:PRK11432 1 MTQKNFVVLKNITKRFGSN----TVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 81 grAALRARDIGFVFQSFMLVPTLTALENVQ--LPALLRGEREHDSRQRAAALLTQL-GLGQRLRHlpaQLSGGEQQRVAL 157
Cdd:PRK11432 73 --RSIQQRDICMVFQSYALFPHMSLGENVGygLKMLGVPKEERKQRVKEALELVDLaGFEDRYVD---QISGGQQQRVAL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 502612564 158 ARAFSARPQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHD 206
Cdd:PRK11432 148 ARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHD 196
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
29-208 |
4.53e-33 |
|
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: 124.80 E-value: 4.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 29 VDLVVKRGQSLALIGESGSGKSTL-LGILaGLDDaSAGEVRLLGQPLSQLDEEGRAALRaRDIGFVFQ----SfmLVPTL 103
Cdd:COG4172 305 VSLTLRRGETLGLVGESGSGKSTLgLALL-RLIP-SEGEIRFDGQDLDGLSRRALRPLR-RRMQVVFQdpfgS--LSPRM 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 104 TALE------NVQLPALLRGERehdsRQRAAALLTQLGLGQRLRH-LPAQLSGGEQQRVALARAFSARPQILFADEPTGN 176
Cdd:COG4172 380 TVGQiiaeglRVHGPGLSAAER----RARVAEALEEVGLDPAARHrYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSA 455
|
170 180 190
....*....|....*....|....*....|..
gi 502612564 177 LDRQTGDRIADLLFELNQRQATTLVMVTHDVQ 208
Cdd:COG4172 456 LDVSVQAQILDLLRDLQREHGLAYLFISHDLA 487
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-205 |
5.12e-33 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 124.36 E-value: 5.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 3 AQNVIEVHHVAKRVGegenQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDeeGR 82
Cdd:COG1129 1 AEPLLEMRGISKSFG----GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRS--PR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 83 AALRARdIGFVFQSFMLVPTLTALENVQLPALLRGEREHDS---RQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALAR 159
Cdd:COG1129 75 DAQAAG-IAIIHQELNLVPNLSVAENIFLGREPRRGGLIDWramRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIAR 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 502612564 160 AFSARPQILFADEPTGNLDRQTGDRIADLLFELnQRQATTLVMVTH 205
Cdd:COG1129 154 ALSRDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISH 198
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
29-213 |
1.16e-32 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 118.24 E-value: 1.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 29 VDLVVKRGQSLALIGESGSGKST----LLGILAGLDDASAGEVRLLGQPLSQLdeegraALRARDIGFVFQSFM--LVPT 102
Cdd:TIGR02770 5 LNLSLKRGEVLALVGESGSGKSLtclaILGLLPPGLTQTSGEILLDGRPLLPL------SIRGRHIATIMQNPRtaFNPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 103 LTALENVQLPALLRGEREHDSRQRAAALLTQLGL--GQRLRHL-PAQLSGGEQQRVALARAFSARPQILFADEPTGNLDR 179
Cdd:TIGR02770 79 FTMGNHAIETLRSLGKLSKQARALILEALEAVGLpdPEEVLKKyPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDV 158
|
170 180 190
....*....|....*....|....*....|....
gi 502612564 180 QTGDRIADLLFELNQRQATTLVMVTHDVQLAARC 213
Cdd:TIGR02770 159 VNQARVLKLLRELRQLFGTGILLITHDLGVVARI 192
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
6-224 |
1.43e-32 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 118.34 E-value: 1.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 6 VIEVHHVAKRVGegenQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEGRAAL 85
Cdd:PRK13548 2 MLEARNLSVRLG----GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 86 RArdigfVF-QSFMLVPTLTALENVQLPALLRGEREHDSRQRAAALLTQLGLGQ-RLRHLPaQLSGGEQQRVALARAF-- 161
Cdd:PRK13548 78 RA-----VLpQHSSLSFPFTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHlAGRDYP-QLSGGEQQRVQLARVLaq 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502612564 162 ----SARPQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAAR-CQRRLRLVDGTL 224
Cdd:PRK13548 152 lwepDGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARyADRIVLLHQGRL 219
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
30-221 |
1.53e-32 |
|
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: 117.21 E-value: 1.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 30 DLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEgraalrARDIGFVFQSFMLVPTLTALENV 109
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA------DRPVSMLFQENNLFAHLTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 110 QLPALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEPTGNLDRQTGDRIADLL 189
Cdd:cd03298 92 GLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190
....*....|....*....|....*....|..
gi 502612564 190 FELNQRQATTLVMVTHDVQLAARCQRRLRLVD 221
Cdd:cd03298 172 LDLHAETKMTVLMVTHQPEDAKRLAQRVVFLD 203
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
25-224 |
1.98e-32 |
|
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: 116.86 E-value: 1.98e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 25 ILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDeegraalraRDIGFVFQSFMLVPT-- 102
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER---------KRIGYVPQRRSIDRDfp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 103 LTALENV------QLPALLRGEREHdsRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEPTGN 176
Cdd:cd03235 85 ISVRDVVlmglygHKGLFRRLSKAD--KAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502612564 177 LDRQTGDRIADLLFELNQRqATTLVMVTHDVQLAARCQRRLRLVDGTL 224
Cdd:cd03235 163 VDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRTV 209
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
6-216 |
2.56e-32 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 117.78 E-value: 2.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 6 VIEVHHVAKRVGEGEnqisILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDA-----SAGEVRLLGQPL--SQLD 78
Cdd:TIGR00972 1 AIEIENLNLFYGEKE----ALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDLvpgvrIEGKVLFDGQDIydKKID 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 79 EEgraALRARdIGFVFQSFMLVPtLTALENVQLPALLRGER-EHDSRQRAAALLTQLGL----GQRLRHLPAQLSGGEQQ 153
Cdd:TIGR00972 77 VV---ELRRR-VGMVFQKPNPFP-MSIYDNIAYGPRLHGIKdKKELDEIVEESLKKAALwdevKDRLHDSALGLSGGQQQ 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502612564 154 RVALARAFSARPQILFADEPTGNLDRQTGDRIADLLFELnqRQATTLVMVTHDVQLAARCQRR 216
Cdd:TIGR00972 152 RLCIARALAVEPEVLLLDEPTSALDPIATGKIEELIQEL--KKKYTIVIVTHNMQQAARISDR 212
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-206 |
6.01e-32 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 119.67 E-value: 6.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 4 QNVIEVHHVAKRVGEGEnqisILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEgra 83
Cdd:PRK09452 12 SPLVELRGISKSFDGKE----VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 84 alrARDIGFVFQSFMLVPTLTALENVQ--LPALLRGEREHDSRQRAAALLTQL-GLGQRLrhlPAQLSGGEQQRVALARA 160
Cdd:PRK09452 85 ---NRHVNTVFQSYALFPHMTVFENVAfgLRMQKTPAAEITPRVMEALRMVQLeEFAQRK---PHQLSGGQQQRVAIARA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 502612564 161 FSARPQILFADEPTGNLDRQTGDRIADLLFELnQRQ-ATTLVMVTHD 206
Cdd:PRK09452 159 VVNKPKVLLLDESLSALDYKLRKQMQNELKAL-QRKlGITFVFVTHD 204
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
29-212 |
8.99e-32 |
|
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: 118.66 E-value: 8.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 29 VDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLsqLDEEGRAALRA--RDIGFVFQSFMLVPTLTAL 106
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVL--QDSARGIFLPPhrRRIGYVFQEARLFPHLSVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 107 ENVQLPalLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEPTGNLDRQTGDRIA 186
Cdd:COG4148 96 GNLLYG--RKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEIL 173
|
170 180
....*....|....*....|....*.
gi 502612564 187 DLLFELNQRQATTLVMVTHDVQLAAR 212
Cdd:COG4148 174 PYLERLRDELDIPILYVSHSLDEVAR 199
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
7-227 |
9.55e-32 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 116.78 E-value: 9.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGEG-ENQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEGRAAL 85
Cdd:TIGR04521 1 IKLKNVSYIYQPGtPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 86 RaRDIGFVFQsFmlvP-----TLTALENVQLPALLRGEREHDSRQRAAALLTQLGLGQRLRHL-PAQLSGGEQQRVALAR 159
Cdd:TIGR04521 81 R-KKVGLVFQ-F---PehqlfEETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEEYLERsPFELSGGQMRRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502612564 160 AFSARPQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDV-QLAARCQRRL-----RLV-DGTLREV 227
Cdd:TIGR04521 156 VLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMeDVAEYADRVIvmhkgKIVlDGTPREV 230
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
7-212 |
1.76e-31 |
|
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: 114.84 E-value: 1.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVakRVGEGENQIsiLTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEGRAalr 86
Cdd:cd03224 1 LEVENL--NAGYGKSQI--LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 87 ARDIGFVFQSFMLVPTLTALENVQLPALLRGERE-HDSRQRAAALLTQlgLGQRLRHLPAQLSGGEQQRVALARAFSARP 165
Cdd:cd03224 74 RAGIGYVPEGRRIFPELTVEENLLLGAYARRRAKrKARLERVYELFPR--LKERRKQLAGTLSGGEQQMLAIARALMSRP 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 502612564 166 QILFADEPTGNLDRQTGDRIADLLFELNQRQaTTLVMVTHDVQLAAR 212
Cdd:cd03224 152 KLLLLDEPSEGLAPKIVEEIFEAIRELRDEG-VTILLVEQNARFALE 197
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-226 |
2.30e-31 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 115.88 E-value: 2.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 3 AQNVIEVHHVAKRVGEGENQIsiLTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSqldEEGR 82
Cdd:PRK13635 2 KEEIIRVEHISFRYPDAATYA--LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLS---EETV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 83 AALRARdIGFVFQS--FMLVPTLT------ALENVQLPALLRGEREHDSrqraaalLTQLGLGQRLRHLPAQLSGGEQQR 154
Cdd:PRK13635 77 WDVRRQ-VGMVFQNpdNQFVGATVqddvafGLENIGVPREEMVERVDQA-------LRQVGMEDFLNREPHRLSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502612564 155 VALARAFSARPQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAARCQRRLRLVDGTLRE 226
Cdd:PRK13635 149 VAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILE 220
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
25-210 |
2.47e-31 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 115.18 E-value: 2.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 25 ILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLsqldeEGRAALRardiGFVFQSFMLVPTLT 104
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV-----EGPGAER----GVVFQNEGLLPWRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 105 ALENVQLPALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEPTGNLDRQTGDR 184
Cdd:PRK11248 87 VQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQ 166
|
170 180
....*....|....*....|....*.
gi 502612564 185 IADLLFELNQRQATTLVMVTHDVQLA 210
Cdd:PRK11248 167 MQTLLLKLWQETGKQVLLITHDIEEA 192
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-206 |
2.56e-31 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 116.75 E-value: 2.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 1 MPAQNVIEVHHVAKR--VGEG--ENQISILTAVD---LVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQP 73
Cdd:COG4608 2 AMAEPLLEVRDLKKHfpVRGGlfGRTVGVVKAVDgvsFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 74 LSQLDEEGRAALRaRDIGFVFQ----SfmLVPTLTALENVQLPALLRGEREHDSRQ-RAAALLTQLGLGQR-LRHLPAQL 147
Cdd:COG4608 82 ITGLSGRELRPLR-RRMQMVFQdpyaS--LNPRMTVGDIIAEPLRIHGLASKAERReRVAELLELVGLRPEhADRYPHEF 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502612564 148 SGGEQQRVALARAFSARPQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHD 206
Cdd:COG4608 159 SGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHD 217
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
5-210 |
2.70e-31 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 115.45 E-value: 2.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 5 NVIEVHhvaKRVGEGEnqisILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLS-------QL 77
Cdd:PRK10619 7 NVIDLH---KRYGEHE----VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 78 ---DEEGRAALRARdIGFVFQSFMLVPTLTALENV-QLPALLRGEREHDSRQRAAALLTQLGLGQRLR-HLPAQLSGGEQ 152
Cdd:PRK10619 80 kvaDKNQLRLLRTR-LTMVFQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAQgKYPVHLSGGQQ 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502612564 153 QRVALARAFSARPQILFADEPTGNLDRQTGDRIADLLFELNQrQATTLVMVTHDVQLA 210
Cdd:PRK10619 159 QRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAE-EGKTMVVVTHEMGFA 215
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-205 |
4.37e-31 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 118.98 E-value: 4.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 3 AQNVIEVHHVAKRVGEgenqisiLTA---VDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDE 79
Cdd:COG3845 2 MPPALELRGITKRFGG-------VVAnddVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 80 egRAALRARdIGFVFQSFMLVPTLTALENVQL---PALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVA 156
Cdd:COG3845 75 --RDAIALG-IGMVHQHFMLVPNLTVAENIVLglePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 502612564 157 LARAFSARPQILFADEPTGNLDRQTgdriADLLFE-LNQ--RQATTLVMVTH 205
Cdd:COG3845 152 ILKALYRGARILILDEPTAVLTPQE----ADELFEiLRRlaAEGKSIIFITH 199
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-213 |
5.93e-31 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 114.36 E-value: 5.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 2 PAQNVIEVHHVakRVGEGENQIsiLTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDD-----ASAGEVRLLGQPLSQ 76
Cdd:COG1117 7 TLEPKIEVRNL--NVYYGDKQA--LKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDlipgaRVEGEILLDGEDIYD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 77 LDEEgRAALRARdIGFVFQSfmlvPT---LTALENVQLPALLRGERehdSRQRAAAL----LTQLGLGQ----RLRHLPA 145
Cdd:COG1117 83 PDVD-VVELRRR-VGMVFQK----PNpfpKSIYDNVAYGLRLHGIK---SKSELDEIveesLRKAALWDevkdRLKKSAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502612564 146 QLSGGEQQRVALARAFSARPQILFADEPTGNLDRQTGDRIADLLFELnqRQATTLVMVTHDVQLAARC 213
Cdd:COG1117 154 GLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILEL--KKDYTIVIVTHNMQQAARV 219
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-217 |
7.05e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 114.41 E-value: 7.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGEG-ENQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEGraal 85
Cdd:COG1101 2 LELKNLSKTFNPGtVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYK---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 86 RARDIGFVFQSFML--VPTLTALENVQLpALLRGER-------EHDSRQRAAALLTQLGLG--QRLRHLPAQLSGGEQQR 154
Cdd:COG1101 78 RAKYIGRVFQDPMMgtAPSMTIEENLAL-AYRRGKRrglrrglTKKRRELFRELLATLGLGleNRLDTKVGLLSGGQRQA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502612564 155 VALARAFSARPQILFADEPTGNLDRQTGDRIADLLFEL-NQRQATTLvMVTHDVQLAARCQRRL 217
Cdd:COG1101 157 LSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTL-MVTHNMEQALDYGNRL 219
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
7-221 |
7.81e-31 |
|
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: 112.85 E-value: 7.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGEGEnqisILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGqplsqLDEEGRAALR 86
Cdd:cd03265 1 IEVENLVKKYGDFE----AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAG-----HDVVREPREV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 87 ARDIGFVFQSFMLVPTLTALENVQLPALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQ 166
Cdd:cd03265 72 RRRIGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502612564 167 ILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAARCQRRLRLVD 221
Cdd:cd03265 152 VLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIID 206
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
7-227 |
2.09e-30 |
|
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: 113.29 E-value: 2.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGEGENQIsiLTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGqpLSQLDEEGRAALR 86
Cdd:TIGR04520 1 IEVENVSFSYPESEKPA--LKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENLWEIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 87 aRDIGFVFQ---------------SFmlvptltALENVQLPallRGErehdSRQRAAALLTQLGLGQRLRHLPAQLSGGE 151
Cdd:TIGR04520 77 -KKVGMVFQnpdnqfvgatveddvAF-------GLENLGVP---REE----MRKRVDEALKLVGMEDFRDREPHLLSGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 152 QQRVALARAFSARPQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAARCQRRL-----RLV-DGTLR 225
Cdd:TIGR04520 142 KQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIvmnkgKIVaEGTPR 221
|
..
gi 502612564 226 EV 227
Cdd:TIGR04520 222 EI 223
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-212 |
2.50e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 112.70 E-value: 2.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 4 QNVIEVHHVAKRVGegenQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGL-----DDASAGEVRLLGQPLSQLD 78
Cdd:PRK14247 1 MNKIEIRDLKVSFG----QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 79 eegRAALRARdIGFVFQSFMLVPTLTALENV----QLPALLRGEREHDSRQRAAALLTQL--GLGQRLRHLPAQLSGGEQ 152
Cdd:PRK14247 77 ---VIELRRR-VQMVFQIPNPIPNLSIFENValglKLNRLVKSKKELQERVRWALEKAQLwdEVKDRLDAPAGKLSGGQQ 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 153 QRVALARAFSARPQILFADEPTGNLDRQTGDRIADLLFELnqRQATTLVMVTHDVQLAAR 212
Cdd:PRK14247 153 QRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLEL--KKDMTIVLVTHFPQQAAR 210
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-222 |
3.33e-30 |
|
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: 112.10 E-value: 3.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 4 QNVIEVHHVakRVGEGENQIsiLTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAG-EVRLLGQPLsqldeeGR 82
Cdd:COG1119 1 DPLLELRNV--TVRRGGKTI--LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERR------GG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 83 ---AALRARdIGFVFQSFML-VPTLTALENVQLPAL-----LRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQ 153
Cdd:COG1119 71 edvWELRKR-IGLVSPALQLrFPRDETVLDVVLSGFfdsigLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 154 RVALARAFSARPQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAARC-QRRLRLVDG 222
Cdd:COG1119 150 RVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGiTHVLLLKDG 219
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
7-207 |
3.35e-30 |
|
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: 111.13 E-value: 3.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGEGEnqisILTAVDLVVKRGQsLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSqldeEGRAALR 86
Cdd:cd03264 1 LQLENLTKRYGKKR----ALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVL----KQPQKLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 87 ARdIGFVFQSFMLVPTLTALENVQLPALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQ 166
Cdd:cd03264 72 RR-IGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 502612564 167 ILFADEPTGNLDRQTGDRIADLLFELNqrqATTLVMV-THDV 207
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSELG---EDRIVILsTHIV 189
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-205 |
4.50e-30 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 116.80 E-value: 4.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 2 PAQNVIEVHHVAKRVGEGENqisILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDeeg 81
Cdd:COG1132 335 PVRGEIEFENVSFSYPGDRP---VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLT--- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 82 RAALRARdIGFVFQSFMLVpTLTALENVQLPallrgeREHDSRQRAAALLTQLGLGQRLRHLP-----------AQLSGG 150
Cdd:COG1132 409 LESLRRQ-IGVVPQDTFLF-SGTIRENIRYG------RPDATDEEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGG 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502612564 151 EQQRVALARAFSARPQILFADEPTGNLDRQTGDRIADLLFELnqRQATTLVMVTH 205
Cdd:COG1132 481 QRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERL--MKGRTTIVIAH 533
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-212 |
6.49e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 111.47 E-value: 6.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 15 RVGEGENQIsiLTAVDLVVKRGQSLALIGESGSGKSTLLGILAGL----DDASA-GEVRLLGQPLSQLDEEgraALRAR- 88
Cdd:PRK14267 11 RVYYGSNHV--IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelnEEARVeGEVRLFGRNIYSPDVD---PIEVRr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 89 DIGFVFQSFMLVPTLTALENV----QLPALLRGEREHDSRQR----AAALLTQLGlgQRLRHLPAQLSGGEQQRVALARA 160
Cdd:PRK14267 86 EVGMVFQYPNPFPHLTIYDNVaigvKLNGLVKSKKELDERVEwalkKAALWDEVK--DRLNDYPSNLSGGQRQRLVIARA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 502612564 161 FSARPQILFADEPTGNLDRQTGDRIADLLFELnqRQATTLVMVTHDVQLAAR 212
Cdd:PRK14267 164 LAMKPKILLMDEPTANIDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAAR 213
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
7-205 |
1.22e-29 |
|
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: 115.28 E-value: 1.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGEGEnqisILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLL---------------- 70
Cdd:TIGR03269 1 IEVKNLTKKFDGKE----VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPTSGRIIyhvalcekcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 71 --GQPLSQ--------------LDEEGRAALRARdIGFVFQ-SFMLVPTLTALENVqLPALLRGERE-HDSRQRAAALLT 132
Cdd:TIGR03269 77 kvGEPCPVcggtlepeevdfwnLSDKLRRRIRKR-IAIMLQrTFALYGDDTVLDNV-LEALEEIGYEgKEAVGRAVDLIE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502612564 133 QLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTH 205
Cdd:TIGR03269 155 MVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSH 227
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
30-222 |
1.32e-28 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 107.36 E-value: 1.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 30 DLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQ-----PLSQldeegraalraRDIGFVFQSFMLVPTLT 104
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhtttPPSR-----------RPVSMLFQENNLFSHLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 105 ALENVQL---PALlrgEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEPTGNLDRQT 181
Cdd:PRK10771 88 VAQNIGLglnPGL---KLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPAL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 502612564 182 GDRIADLLFELNQRQATTLVMVTHDVQLAAR-CQRRLRLVDG 222
Cdd:PRK10771 165 RQEMLTLVSQVCQERQLTLLMVSHSLEDAARiAPRSLVVADG 206
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
7-227 |
1.38e-28 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 108.28 E-value: 1.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGegenQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEGRAALR 86
Cdd:COG4559 2 LEAENLSVRLG----GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 87 ArdigfVF-QSFMLVPTLTALENVQLPALLRGEREHDSRQRAAALLTQLGL-GQRLRHLPaQLSGGEQQRVALARAF--- 161
Cdd:COG4559 78 A-----VLpQHSSLAFPFTVEEVVALGRAPHGSSAAQDRQIVREALALVGLaHLAGRSYQ-TLSGGEQQRVQLARVLaql 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502612564 162 ----SARPQILFADEPTGNLDRQTGDRIADLLFELNQRQAtTLVMVTHDVQLAARCQRRL------RLV-DGTLREV 227
Cdd:COG4559 152 wepvDGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGG-GVVAVLHDLNLAAQYADRIlllhqgRLVaQGTPEEV 227
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
28-217 |
2.14e-28 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 109.06 E-value: 2.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 28 AVDLV---VKRGQSLALIGESGSGKSTLLGILAGLDD----ASAGEVRLLGQPLSQLDEEGRAALRARDIGFVFQSFM-- 98
Cdd:PRK11022 22 AVDRIsysVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDLQRISEKERRNLVGAEVAMIFQDPMts 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 99 LVPTLTAleNVQLPALLR---GEREHDSRQRAAALLTQLGL---GQRLRHLPAQLSGGEQQRVALARAFSARPQILFADE 172
Cdd:PRK11022 102 LNPCYTV--GFQIMEAIKvhqGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 502612564 173 PTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAARCQRRL 217
Cdd:PRK11022 180 PTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKI 224
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
7-224 |
2.88e-28 |
|
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: 104.99 E-value: 2.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGEGENqiSILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDeegRAALR 86
Cdd:cd03246 1 LEVENVSFRYPGAEP--PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWD---PNELG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 87 ARdIGFVFQSFMLVPTlTALENVqlpallrgerehdsrqraaalltqlglgqrlrhlpaqLSGGEQQRVALARAFSARPQ 166
Cdd:cd03246 76 DH-VGYLPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPR 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502612564 167 ILFADEPTGNLDRQTGDRIADLLFELNQRQAtTLVMVTHDVQLAARCQRRLRLVDGTL 224
Cdd:cd03246 117 ILVLDEPNSHLDVEGERALNQAIAALKAAGA-TRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
7-222 |
5.68e-28 |
|
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: 105.44 E-value: 5.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGEgenqISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEgraalr 86
Cdd:cd03269 1 LEVENVTKRFGR----VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARN------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 87 arDIGFVFQSFMLVPTLTALENVQLPALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQ 166
Cdd:cd03269 71 --RIGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502612564 167 ILFADEPTGNLDRQTGDRIADLLFELnQRQATTLVMVTHDVQLAAR-CQRRLRLVDG 222
Cdd:cd03269 149 LLILDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEElCDRVLLLNKG 204
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
26-219 |
1.15e-27 |
|
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: 109.68 E-value: 1.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 26 LTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDeegrAALRARDIGFVFQSFMLVPTlTA 105
Cdd:TIGR02857 338 LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADAD----ADSWRDQIAWVPQHPFLFAG-TI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 106 LENVQLPAllRGEREHDSRQ--RAAALLTQL-----GLGQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEPTGNLD 178
Cdd:TIGR02857 413 AENIRLAR--PDASDAEIREalERAGLDEFVaalpqGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLD 490
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 502612564 179 RQTGDRIADLLFELNQRQatTLVMVTHDVQLAARCQRRLRL 219
Cdd:TIGR02857 491 AETEAEVLEALRALAQGR--TVLLVTHRLALAALADRIVVL 529
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
22-212 |
2.74e-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: 104.29 E-value: 2.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 22 QISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEGRAALRardIGFVFQSFMLVP 101
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLG---IGYVPEGRRIFP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 102 TLTALENVQLPALLRGERE--HDSRQRAAALLTQLGlgQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEPTgnldr 179
Cdd:COG0410 92 SLTVEENLLLGAYARRDRAevRADLERVYELFPRLK--ERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPS----- 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 502612564 180 qTG------DRIADLLFELNqRQATTLVMVTHDVQLAAR 212
Cdd:COG0410 165 -LGlaplivEEIFEIIRRLN-REGVTILLVEQNARFALE 201
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
30-220 |
3.67e-27 |
|
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: 103.40 E-value: 3.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 30 DLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSqldeegRAALRARDIGFVFQSFMLVPTLTALENV 109
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHT------GLAPYQRPVSMLFQENNLFAHLTVRQNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 110 QL---PALLRGEREhdsRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEPTGNLDRQTGDRIA 186
Cdd:TIGR01277 92 GLglhPGLKLNAEQ---QEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEML 168
|
170 180 190
....*....|....*....|....*....|....
gi 502612564 187 DLLFELNQRQATTLVMVTHDVQLAARCQRRLRLV 220
Cdd:TIGR01277 169 ALVKQLCSERQRTLLMVTHHLSDARAIASQIAVV 202
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
29-209 |
4.21e-27 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 104.53 E-value: 4.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 29 VDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLsqldEEGRAALRARDIGFVFQ--SFMLVPTLTA- 105
Cdd:COG4167 32 VSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKL----EYGDYKYRCKHIRMIFQdpNTSLNPRLNIg 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 106 --LE-----NVQLPALlrgEREhdsrQRAAALLTQLGLgqrLR-HL---PAQLSGGEQQRVALARAFSARPQILFADEPT 174
Cdd:COG4167 108 qiLEeplrlNTDLTAE---ERE----ERIFATLRLVGL---LPeHAnfyPHMLSSGQKQRVALARALILQPKIIIADEAL 177
|
170 180 190
....*....|....*....|....*....|....*
gi 502612564 175 GNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQL 209
Cdd:COG4167 178 AALDMSVRSQIINLMLELQEKLGISYIYVSQHLGI 212
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
25-205 |
6.53e-27 |
|
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: 102.24 E-value: 6.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 25 ILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASA--GEVRLLGQPLSqldeegRAALRARdIGFVFQSFMLVPT 102
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPLD------KRSFRKI-IGYVPQDDILHPT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 103 LTALENVQLPALLRGerehdsrqraaalltqlglgqrlrhlpaqLSGGEQQRVALARAFSARPQILFADEPTGNLDRQTG 182
Cdd:cd03213 97 LTVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180
....*....|....*....|...
gi 502612564 183 DRIADLLFELNQrQATTLVMVTH 205
Cdd:cd03213 148 LQVMSLLRRLAD-TGRTIICSIH 169
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
20-205 |
7.58e-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: 102.69 E-value: 7.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 20 ENQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDeegRAALRARdIGFVFQSFML 99
Cdd:cd03254 13 DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIS---RKSLRSM-IGVVLQDTFL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 100 VPTlTALENVQLpallrgEREHDSRQRAAALLTQLGLGQRLRHLP-----------AQLSGGEQQRVALARAFSARPQIL 168
Cdd:cd03254 89 FSG-TIMENIRL------GRPNATDEEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 502612564 169 FADEPTGNLDRQTGDRIADLLFELnqRQATTLVMVTH 205
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKL--MKGRTSIIIAH 196
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
19-206 |
1.73e-26 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 104.73 E-value: 1.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 19 GENQISilTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEGRAalrardIGFVFQSFM 98
Cdd:PRK11000 14 GDVVIS--KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERG------VGMVFQSYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 99 LVPTLTALENVQLPALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEPTGNLD 178
Cdd:PRK11000 86 LYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
170 180 190
....*....|....*....|....*....|..
gi 502612564 179 R----QTGDRIAdllfELNQRQATTLVMVTHD 206
Cdd:PRK11000 166 AalrvQMRIEIS----RLHKRLGRTMIYVTHD 193
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
3-206 |
2.79e-26 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 103.51 E-value: 2.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 3 AQNVIEVHHVAKRVGEGENQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEGR 82
Cdd:PRK11308 8 AIDLKKHYPVKRGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 83 AALRaRDIGFVFQS--FMLVPTLTA---LE-----NVQLPAllrGERehdsRQRAAALLTQLGLgqRLRH---LPAQLSG 149
Cdd:PRK11308 88 KLLR-QKIQIVFQNpyGSLNPRKKVgqiLEeplliNTSLSA---AER----REKALAMMAKVGL--RPEHydrYPHMFSG 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502612564 150 GEQQRVALARAFSARPQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHD 206
Cdd:PRK11308 158 GQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHD 214
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
29-211 |
4.09e-26 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 103.38 E-value: 4.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 29 VDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEegraalRARDIGFVFQSFMLVPTLTALEN 108
Cdd:PRK11650 23 IDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEP------ADRDIAMVFQNYALYPHMSVREN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 109 VQLPALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEPTGNLDrqtgdriADL 188
Cdd:PRK11650 97 MAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD-------AKL 169
|
170 180 190
....*....|....*....|....*....|
gi 502612564 189 -------LFELNQRQATTLVMVTHDvQLAA 211
Cdd:PRK11650 170 rvqmrleIQRLHRRLKTTSLYVTHD-QVEA 198
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-226 |
5.30e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 105.29 E-value: 5.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 20 ENQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEegrAALRARdIGFVFQSFML 99
Cdd:PRK11160 350 DQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSE---AALRQA-ISVVSQRVHL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 100 VPTlTALENVQLPAllrgEREHDSRQRAAalLTQLGLGQRLRHLPA----------QLSGGEQQRVALARAFSARPQILF 169
Cdd:PRK11160 426 FSA-TLRDNLLLAA----PNASDEALIEV--LQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGIARALLHDAPLLL 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502612564 170 ADEPTGNLDRQTGDRIADLLFELNQRQatTLVMVTHDVQLAARCQRRLRLVDGTLRE 226
Cdd:PRK11160 499 LDEPTEGLDAETERQILELLAEHAQNK--TVLMITHRLTGLEQFDRICVMDNGQIIE 553
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
9-206 |
5.36e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 104.76 E-value: 5.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 9 VHHVAKRVGEGEnqisILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLlgqplsqldeegRAALRar 88
Cdd:COG0488 1 LENLSKSFGGRP----LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI------------PKGLR-- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 89 dIGFVFQSFMLVPTLTALENVQ-----LPALLR---------------GER------------EHDSRQRAAALLTQLGL 136
Cdd:COG0488 63 -IGYLPQEPPLDDDLTVLDTVLdgdaeLRALEAeleeleaklaepdedLERlaelqeefealgGWEAEARAEEILSGLGF 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502612564 137 GQRLRHLP-AQLSGGEQQRVALARAFSARPQILFADEPTGNLDRQTGDRIADLLfelnQRQATTLVMVTHD 206
Cdd:COG0488 142 PEEDLDRPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFL----KNYPGTVLVVSHD 208
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-227 |
9.19e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 101.34 E-value: 9.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 6 VIEVHHVAKRVGEgenqisiLTAVD---LVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDeegr 82
Cdd:COG4152 1 MLELKGLTKRFGD-------KTAVDdvsFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 83 aalrARDIGfvfqsFM-----LVPTLTALENVQLPALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVAL 157
Cdd:COG4152 70 ----RRRIG-----YLpeergLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502612564 158 ARAFSARPQILFADEPTGNLDRQTGDRIADLLFELNqRQATTLVMVTHDVQLAAR-CQR-------RLRLvDGTLREV 227
Cdd:COG4152 141 IAALLHDPELLILDEPFSGLDPVNVELLKDVIRELA-AKGTTVIFSSHQMELVEElCDRiviinkgRKVL-SGSVDEI 216
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-210 |
9.60e-26 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 100.77 E-value: 9.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 1 MPAQNVIEVHHVAKRVGEGENqisiLTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQ-----PLS 75
Cdd:PRK11701 1 MMDQPLLSVRGLTKLYGPRKG----CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 76 QLDEEGRAALRARDIGFVFQSFM--LVPTLTALENVQLPALLRGEREH-DSRQRAAALLTQLGLGQ-RLRHLPAQLSGGE 151
Cdd:PRK11701 77 ALSEAERRRLLRTEWGFVHQHPRdgLRMQVSAGGNIGERLMAVGARHYgDIRATAGDWLERVEIDAaRIDDLPTTFSGGM 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502612564 152 QQRVALARAFSARPQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLA 210
Cdd:PRK11701 157 QQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVA 215
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
7-226 |
1.26e-25 |
|
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: 104.44 E-value: 1.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGEGENqisILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDeegRAALR 86
Cdd:TIGR01193 474 IVINDVSYSYGYGSN---ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDID---RHTLR 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 87 aRDIGFVFQS-FMLvpTLTALENvqlpaLLRGEREHDSRQRAAALLT-----------QLGLGQRLRHLPAQLSGGEQQR 154
Cdd:TIGR01193 548 -QFINYLPQEpYIF--SGSILEN-----LLLGAKENVSQDEIWAACEiaeikddienmPLGYQTELSEEGSSISGGQKQR 619
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502612564 155 VALARAFSARPQILFADEPTGNLDRQTGDRIADLLFELNQRqatTLVMVTHDVQLAARCQRRLRLVDGTLRE 226
Cdd:TIGR01193 620 IALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQSDKIIVLDHGKIIE 688
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
26-210 |
1.39e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 100.54 E-value: 1.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 26 LTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSqLDEEGRAALRaRDIGFVFQS---FMLVPT 102
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKSLLEVR-KTVGIVFQNpddQLFAPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 103 LtaLENVQLPALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEPTGNLDRQTG 182
Cdd:PRK13639 96 V--EEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGA 173
|
170 180
....*....|....*....|....*...
gi 502612564 183 DRIADLLFELNqRQATTLVMVTHDVQLA 210
Cdd:PRK13639 174 SQIMKLLYDLN-KEGITIIISTHDVDLV 200
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
31-220 |
1.42e-25 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 102.80 E-value: 1.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 31 LVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEGRAALRARDIGFVFQSFMLVPTLTALENVQ 110
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNTA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 111 LPALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEPTGNLDRQTGDRIADLLF 190
Cdd:PRK10070 129 FGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELV 208
|
170 180 190
....*....|....*....|....*....|
gi 502612564 191 ELNQRQATTLVMVTHDVQLAARCQRRLRLV 220
Cdd:PRK10070 209 KLQAKHQRTIVFISHDLDEAMRIGDRIAIM 238
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
40-228 |
1.79e-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: 101.73 E-value: 1.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 40 ALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEGRAALRARDIGFVFQSFMLVPTLTALENvqlpaLLRGER 119
Cdd:TIGR02142 27 AIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQEARLFPHLSVRGN-----LRYGMK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 120 EHDSRQRA---AALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEPTGNLDRQTGDRIADLLFELNQRQ 196
Cdd:TIGR02142 102 RARPSERRisfERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEF 181
|
170 180 190
....*....|....*....|....*....|....*....
gi 502612564 197 ATTLVMVTHDVQLAARCQRRLRLVD-------GTLREVA 228
Cdd:TIGR02142 182 GIPILYVSHSLQEVLRLADRVVVLEdgrvaaaGPIAEVW 220
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
20-205 |
1.93e-25 |
|
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: 98.82 E-value: 1.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 20 ENQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDeegRAALRaRDIGFVFQSFML 99
Cdd:cd03245 14 NQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLD---PADLR-RNIGYVPQDVTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 100 VPTlTALENVQLpallrGEREHDSRQ--RAAAL--LTQL------GLGQRLRHLPAQLSGGEQQRVALARAFSARPQILF 169
Cdd:cd03245 90 FYG-TLRDNITL-----GAPLADDERilRAAELagVTDFvnkhpnGLDLQIGERGRGLSGGQRQAVALARALLNDPPILL 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 502612564 170 ADEPTGNLDRQTGDRIADLLFELnqRQATTLVMVTH 205
Cdd:cd03245 164 LDEPTSAMDMNSEERLKERLRQL--LGDKTLIIITH 197
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-212 |
4.05e-25 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 102.48 E-value: 4.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 18 EGENQISILTAVDLVVKRGQSLALIGESGSGKS-TLLGILAGLDDASA----GEVRLLGQPLSQLDEEGRAALRARDIGF 92
Cdd:PRK15134 17 QQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPVvypsGDIRFHGESLLHASEQTLRGVRGNKIAM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 93 VFQSFMLvpTLTALENV--QLPALL---RGEREHDSRQRAAALLTQLGLGQ---RLRHLPAQLSGGEQQRVALARAFSAR 164
Cdd:PRK15134 97 IFQEPMV--SLNPLHTLekQLYEVLslhRGMRREAARGEILNCLDRVGIRQaakRLTDYPHQLSGGERQRVMIAMALLTR 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502612564 165 PQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAAR 212
Cdd:PRK15134 175 PELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRK 222
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
25-223 |
4.59e-25 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 102.58 E-value: 4.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 25 ILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLlgqPlsqldeegraalRARDIGFVFQ-SFMLVPTL 103
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR---P------------AGARVLFLPQrPYLPLGTL 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 104 TAlenvqlpALLR-GEREHDSRQRAAALLTQLGLGQRLRHL------PAQLSGGEQQRVALARAFSARPQILFADEPTGN 176
Cdd:COG4178 443 RE-------ALLYpATAEAFSDAELREALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSA 515
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 502612564 177 LDRQTGDRIADLLfeLNQRQATTLVMVTHDVQLAARCQRRLRLVDGT 223
Cdd:COG4178 516 LDEENEAALYQLL--REELPGTTVISVGHRSTLAAFHDRVLELTGDG 560
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
7-225 |
5.78e-25 |
|
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: 97.82 E-value: 5.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGEGENQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEGRaalr 86
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEAR---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 87 aRDIGFVFQSFMLVPTLTALENVQLPALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQ 166
Cdd:cd03266 78 -RRLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 167 ILFADEPTGNLDRQTGDRIADLLFELnQRQATTLVMVTHDVQLAAR-CQRRLRLVDGTLR 225
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERlCDRVVVLHRGRVV 215
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-226 |
6.21e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 101.68 E-value: 6.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 6 VIEVHHVAKRVGEGEnqisILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRlLGQPLSqldeegraal 85
Cdd:COG0488 315 VLELEGLSKSYGDKT----LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVK-LGETVK---------- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 86 rardIGFVFQSF-MLVPTLTALENvqlpalLRGEREHDSRQRAAALLTQLGL-GQRLRHLPAQLSGGEQQRVALARAFSA 163
Cdd:COG0488 380 ----IGYFDQHQeELDPDKTVLDE------LRDGAPGGTEQEVRGYLGRFLFsGDDAFKPVGVLSGGEKARLALAKLLLS 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502612564 164 RPQILFADEPTGNLDRQTGDRIADLL--FElnqrqaTTLVMVTHDVQLAAR-CQRRLRLVDGTLRE 226
Cdd:COG0488 450 PPNVLLLDEPTNHLDIETLEALEEALddFP------GTVLLVSHDRYFLDRvATRILEFEDGGVRE 509
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
24-208 |
7.14e-25 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 101.71 E-value: 7.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 24 SILTAVDLVVKRGQSLALIGESGSGKST----LLGILAglddaSAGEVRLLGQPLSQLDEEGRAALRARdIGFVFQ--SF 97
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNRRQLLPVRHR-IQVVFQdpNS 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 98 MLVPTLTALE------NVQLPALLRGEREhdsrQRAAALLTQLGLGQRLRH-LPAQLSGGEQQRVALARAFSARPQILFA 170
Cdd:PRK15134 374 SLNPRLNVLQiieeglRVHQPTLSAAQRE----QQVIAVMEEVGLDPETRHrYPAEFSGGQRQRIAIARALILKPSLIIL 449
|
170 180 190
....*....|....*....|....*....|....*...
gi 502612564 171 DEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQ 208
Cdd:PRK15134 450 DEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLH 487
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
7-201 |
8.14e-25 |
|
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: 96.90 E-value: 8.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGEGEnqisILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQplsqldEEGRAALR 86
Cdd:cd03268 1 LKTNDLTKTYGKKR----VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGK------SYQKNIEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 87 ARDIGFVFQSFMLVPTLTALENVQLPALLRGEREhdsrQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQ 166
Cdd:cd03268 71 LRRIGALIEAPGFYPNLTARENLRLLARLLGIRK----KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPD 146
|
170 180 190
....*....|....*....|....*....|....*
gi 502612564 167 ILFADEPTGNLDRQTGDRIADLLFELNQRQATTLV 201
Cdd:cd03268 147 LLILDEPTNGLDPDGIKELRELILSLRDQGITVLI 181
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
7-205 |
1.11e-24 |
|
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: 95.19 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGEGEnqisILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEegRAALR 86
Cdd:cd03216 1 LELRGITKRFGGVK----ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASP--RDARR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 87 ARdIGFVFqsfmlvptltalenvqlpallrgerehdsrqraaalltqlglgqrlrhlpaQLSGGEQQRVALARAFSARPQ 166
Cdd:cd03216 75 AG-IAMVY---------------------------------------------------QLSVGERQMVEIARALARNAR 102
|
170 180 190
....*....|....*....|....*....|....*....
gi 502612564 167 ILFADEPTGNLDRQTGDRIADLLFELnQRQATTLVMVTH 205
Cdd:cd03216 103 LLILDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISH 140
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
7-226 |
1.17e-24 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 95.84 E-value: 1.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGEGENQIsiLTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEGRAAlr 86
Cdd:cd03247 1 LSINNVSFSYPEQEQQV--LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSL-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 87 ardIGFVFQSFMLVPTlTALENVqlpallrGERehdsrqraaalltqlglgqrlrhlpaqLSGGEQQRVALARAFSARPQ 166
Cdd:cd03247 77 ---ISVLNQRPYLFDT-TLRNNL-------GRR---------------------------FSGGERQRLALARILLQDAP 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 167 ILFADEPTGNLDRQTGDRIADLLFElnQRQATTLVMVTHDVQLAARCQRRLRLVDGTLRE 226
Cdd:cd03247 119 IVLLDEPTVGLDPITERQLLSLIFE--VLKDKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
25-203 |
1.29e-24 |
|
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: 96.96 E-value: 1.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 25 ILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASA---GEVRLLGQPLSqldeegrAALRARDIGFVFQSFMLVP 101
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRK-------PDQFQKCVAYVRQDDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 102 TLTALENVQLPALLRGEREHDSRQR----AAALLTQLGLgQRLRH-LPAQLSGGEQQRVALARAFSARPQILFADEPTGN 176
Cdd:cd03234 95 GLTVRETLTYTAILRLPRKSSDAIRkkrvEDVLLRDLAL-TRIGGnLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180
....*....|....*....|....*..
gi 502612564 177 LDRQTGDRIADLLFELNQRQATTLVMV 203
Cdd:cd03234 174 LDSFTALNLVSTLSQLARRNRIVILTI 200
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
6-215 |
1.91e-24 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 100.97 E-value: 1.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 6 VIEVHHVAKRVGEgenqisiLTAVDLV---VKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEGR 82
Cdd:NF033858 266 AIEARGLTMRFGD-------FTAVDHVsfrIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 83 aalraRDIGFVFQSFMLVPTLTALENVQLPALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFS 162
Cdd:NF033858 339 -----RRVGYMSQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVI 413
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502612564 163 ARPQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAARCQR 215
Cdd:NF033858 414 HKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEAERCDR 466
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
21-205 |
2.42e-24 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 100.51 E-value: 2.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 21 NQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDAS---AGEVRLLGQPLsqldeeGRAALRARDiGFVFQSF 97
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPI------DAKEMRAIS-AYVQQDD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 98 MLVPTLTALENVQLPALLRGEREHDS---RQRAAALLTQLGL--------GQRLRHlpAQLSGGEQQRVALARAFSARPQ 166
Cdd:TIGR00955 109 LFIPTLTVREHLMFQAHLRMPRRVTKkekRERVDEVLQALGLrkcantriGVPGRV--KGLSGGERKRLAFASELLTDPP 186
|
170 180 190
....*....|....*....|....*....|....*....
gi 502612564 167 ILFADEPTGNLDRQTGDRIADLLFELNQRqATTLVMVTH 205
Cdd:TIGR00955 187 LLFCDEPTSGLDSFMAYSVVQVLKGLAQK-GKTIICTIH 224
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
29-213 |
4.47e-24 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 96.31 E-value: 4.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 29 VDLVVKRGQSLALIGESGSGKS----TLLGILAGLDDASAGEVRLLGQPLSQldeegrAALRARDIGFVFQ----SFMLV 100
Cdd:PRK10418 22 VSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAP------CALRGRKIATIMQnprsAFNPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 101 PTLTALENVQLPALLRgereHDSRQRAAALLTQLGLGQRLRHL---PAQLSGGEQQRVALARAFSARPQILFADEPTGNL 177
Cdd:PRK10418 96 HTMHTHARETCLALGK----PADDATLTAALEAVGLENAARVLklyPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDL 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 502612564 178 DRQTGDRIADLLFELNQRQATTLVMVTHDVQLAARC 213
Cdd:PRK10418 172 DVVAQARILDLLESIVQKRALGMLLVTHDMGVVARL 207
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
25-226 |
4.58e-24 |
|
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: 95.76 E-value: 4.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 25 ILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEgraALRaRDIGFVFQSFMLVPTlT 104
Cdd:cd03253 16 VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLD---SLR-RAIGVVPQDTVLFND-T 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 105 ALENVQLPALLRGEREhdsrQRAAALLTQLG-------------LGQR-LRhlpaqLSGGEQQRVALARAFSARPQILFA 170
Cdd:cd03253 91 IGYNIRYGRPDATDEE----VIEAAKAAQIHdkimrfpdgydtiVGERgLK-----LSGGEKQRVAIARAILKNPPILLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502612564 171 DEPTGNLDRQTGDRIADLLFELNQRQatTLVMVTHDVQLAARCQRRLRLVDGTLRE 226
Cdd:cd03253 162 DEATSALDTHTEREIQAALRDVSKGR--TTIVIAHRLSTIVNADKIIVLKDGRIVE 215
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-207 |
6.09e-24 |
|
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: 99.11 E-value: 6.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 6 VIEVHHVAKR---VGEGenQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVR-LLGQPLSQL---- 77
Cdd:TIGR03269 279 IIKVRNVSKRyisVDRG--VVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvRVGDEWVDMtkpg 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 78 -DEEGRAAlraRDIGFVFQSFMLVPTLTALEN------VQLPALLrgerehdSRQRAAALLTQLGLGQR-----LRHLPA 145
Cdd:TIGR03269 357 pDGRGRAK---RYIGILHQEYDLYPHRTVLDNlteaigLELPDEL-------ARMKAVITLKMVGFDEEkaeeiLDKYPD 426
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502612564 146 QLSGGEQQRVALARAFSARPQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDV 207
Cdd:TIGR03269 427 ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDM 488
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
26-212 |
1.07e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 95.86 E-value: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 26 LTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLS-QLDEEGRAALRARdIGFVFQsfmlVPTL- 103
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITaGKKNKKLKPLRKK-VGIVFQ----FPEHq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 104 ----TALENVQLPALLRGEREHDSRQRAAALLTQLGLGQRLR-HLPAQLSGGEQQRVALARAFSARPQILFADEPTGNLD 178
Cdd:PRK13634 98 lfeeTVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEELLaRSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
170 180 190
....*....|....*....|....*....|....
gi 502612564 179 RQTGDRIADLLFELNQRQATTLVMVTHDVQLAAR 212
Cdd:PRK13634 178 PKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAAR 211
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
36-217 |
1.12e-23 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 95.28 E-value: 1.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 36 GQSLALIGESGSGKSTLLGILAGLDDASAGEVRLL---GQP--LSQLDEEGRAALRARDIGFVFQSFM--LVPTLTALEN 108
Cdd:TIGR02323 29 GEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYImrsGAEleLYQLSEAERRRLMRTEWGFVHQNPRdgLRMRVSAGAN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 109 VQLPALLRGEREH-DSRQRAAALLTQLGLGQ-RLRHLPAQLSGGEQQRVALARAFSARPQILFADEPTGNLDRQTGDRIA 186
Cdd:TIGR02323 109 IGERLMAIGARHYgNIRATAQDWLEEVEIDPtRIDDLPRAFSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLL 188
|
170 180 190
....*....|....*....|....*....|.
gi 502612564 187 DLLFELNQRQATTLVMVTHDVQLAARCQRRL 217
Cdd:TIGR02323 189 DLLRGLVRDLGLAVIIVTHDLGVARLLAQRL 219
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
23-208 |
1.31e-23 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 96.51 E-value: 1.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 23 ISILTAVDLVVKRGQSLALIGESGSGKSTLL-GILAGLDD---ASAGEVRLLGQPLSQLDEEGRAALRARDIGFVFQ--S 96
Cdd:COG4170 20 VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAkAICGITKDnwhVTADRFRWNGIDLLKLSPRERRKIIGREIAMIFQepS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 97 FMLVPTLTALEnvQL----PA-LLRG---EREHDSRQRAAALLTQLGLGQR---LRHLPAQLSGGEQQRVALARAFSARP 165
Cdd:COG4170 100 SCLDPSAKIGD--QLieaiPSwTFKGkwwQRFKWRKKRAIELLHRVGIKDHkdiMNSYPHELTEGECQKVMIAMAIANQP 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 502612564 166 QILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQ 208
Cdd:COG4170 178 RLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLE 220
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
5-223 |
1.34e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 95.68 E-value: 1.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 5 NVIEVHHVAKRVGEGENQisiLTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSqLDEEGRAA 84
Cdd:PRK13636 4 YILKVEELNYNYSDGTHA---LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID-YSRKGLMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 85 LRaRDIGFVFQSfmlvP-----TLTALENVQLPALLRGEREHDSRQRAAALLTQLGLgQRLRHLPAQ-LSGGEQQRVALA 158
Cdd:PRK13636 80 LR-ESVGMVFQD----PdnqlfSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGI-EHLKDKPTHcLSFGQKKRVAIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502612564 159 RAFSARPQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAA-RCQRRLRLVDGT 223
Cdd:PRK13636 154 GVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPlYCDNVFVMKEGR 219
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
26-206 |
1.51e-23 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 96.31 E-value: 1.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 26 LTAVDLVVKR---GQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEGRAALRaRDIGFVFQSFM--LV 100
Cdd:PRK15079 34 LKAVDGVTLRlyeGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVR-SDIQMIFQDPLasLN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 101 PTLTALENVQLPalLRGEREHDSRQ----RAAALLTQLGLGQRL--RHlPAQLSGGEQQRVALARAFSARPQILFADEPT 174
Cdd:PRK15079 113 PRMTIGEIIAEP--LRTYHPKLSRQevkdRVKAMMLKVGLLPNLinRY-PHEFSGGQCQRIGIARALILEPKLIICDEPV 189
|
170 180 190
....*....|....*....|....*....|..
gi 502612564 175 GNLDRQTGDRIADLLFELNQRQATTLVMVTHD 206
Cdd:PRK15079 190 SALDVSIQAQVVNLLQQLQREMGLSLIFIAHD 221
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
22-221 |
2.46e-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: 93.94 E-value: 2.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 22 QISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQ-PLSQldeegRAALRARdIGFVF-QSFML 99
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLvPWKR-----RKKFLRR-IGVVFgQKTQL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 100 VPTLTALENVQLPALLRGEREHDSRQRAAALLTQLGLGqRLRHLPA-QLSGGEQQRVALARAFSARPQILFADEPTGNLD 178
Cdd:cd03267 107 WWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLE-ELLDTPVrQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD 185
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 502612564 179 RQTGDRIADLLFELNQRQATTLVMVTHDVQLAARCQRRLRLVD 221
Cdd:cd03267 186 VVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVID 228
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
25-226 |
2.50e-23 |
|
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: 93.37 E-value: 2.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 25 ILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEGraalrardiGFvfqsfmlVPTLT 104
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLGG---------GF-------NPELT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 105 ALENVQLPALLRGEREHDSRQRAAALLTQLGLGQRLrHLP-AQLSGGEQQRVALARAFSARPQILFADEPTGNLDRQTGD 183
Cdd:cd03220 101 GRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFI-DLPvKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 502612564 184 RIADLLFELnQRQATTLVMVTHDVQLAAR-CQRRLRLVDGTLRE 226
Cdd:cd03220 180 KCQRRLREL-LKQGKTVILVSHDPSSIKRlCDRALVLEKGKIRF 222
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
4-224 |
3.84e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 93.90 E-value: 3.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 4 QNVIEVHHVAKRVGEGENQIsiLTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQldeEGRA 83
Cdd:PRK13632 5 SVMIKVENVSFSYPNSENNA--LKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISK---ENLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 84 ALRaRDIGFVFQS----FMlvpTLTA-------LENVQLPallRGErehdSRQRAAALLTQLGLGQRLRHLPAQLSGGEQ 152
Cdd:PRK13632 80 EIR-KKIGIIFQNpdnqFI---GATVeddiafgLENKKVP---PKK----MKDIIDDLAKKVGMEDYLDKEPQNLSGGQK 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502612564 153 QRVALARAFSARPQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAARCQRRLRLVDGTL 224
Cdd:PRK13632 149 QRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKL 220
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-224 |
4.18e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 94.10 E-value: 4.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 2 PAQNVIEVHHVAKRVGEGENqiSILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGL---DDASAGEVRLLGqplSQLD 78
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPDSKK--PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDG---ITLT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 79 EEGRAALRARdIGFVFQS----FM--LVPTLTA--LENVQLPallRGEREHDSRQraaaLLTQLGLGQRLRHLPAQLSGG 150
Cdd:PRK13640 76 AKTVWDIREK-VGIVFQNpdnqFVgaTVGDDVAfgLENRAVP---RPEMIKIVRD----VLADVGMLDYIDSEPANLSGG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502612564 151 EQQRVALARAFSARPQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAARCQRRLRLVDGTL 224
Cdd:PRK13640 148 QKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKL 221
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
25-211 |
7.48e-23 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 94.41 E-value: 7.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 25 ILTAV-DL--VVKRGQSLALIGESGSGKS----TLLGILAGlDDASAGEVRLLGQPLSQLDEEGRAALRARDIGFVFQSF 97
Cdd:PRK09473 28 DVTAVnDLnfSLRAGETLGIVGESGSGKSqtafALMGLLAA-NGRIGGSATFNGREILNLPEKELNKLRAEQISMIFQDP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 98 M--LVPTLTALEnvQLPALL---RGEREHDSRQRAAALLTQLGLG---QRLRHLPAQLSGGEQQRVALARAFSARPQILF 169
Cdd:PRK09473 107 MtsLNPYMRVGE--QLMEVLmlhKGMSKAEAFEESVRMLDAVKMPearKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLI 184
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 502612564 170 ADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAA 211
Cdd:PRK09473 185 ADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVA 226
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
25-206 |
7.79e-23 |
|
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: 95.89 E-value: 7.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 25 ILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEgraALRARdIGFVFQSFMLVPTlT 104
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQD---EVRRR-VSVCAQDAHLFDT-T 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 105 ALENvqlpalLRGEREHDSRQRAAALLTQLGLGQRLRHLP-----------AQLSGGEQQRVALARAFSARPQILFADEP 173
Cdd:TIGR02868 425 VREN------LRLARPDATDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLDEP 498
|
170 180 190
....*....|....*....|....*....|...
gi 502612564 174 TGNLDRQTGDRIADLLFELNQRqaTTLVMVTHD 206
Cdd:TIGR02868 499 TEHLDAETADELLEDLLAALSG--RTVVLITHH 529
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
5-226 |
1.11e-22 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 92.07 E-value: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 5 NVIEVHHVAK--RVGEGENQ----------------ISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGE 66
Cdd:COG1134 3 SMIEVENVSKsyRLYHEPSRslkelllrrrrtrreeFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 67 VRLLGQPLSQLdeegraalrarDIGFVFQsfmlvPTLTALENVQLPALLRG--EREHDSRQRAAALLTQLG--LGQRLRH 142
Cdd:COG1134 83 VEVNGRVSALL-----------ELGAGFH-----PELTGRENIYLNGRLLGlsRKEIDEKFDEIVEFAELGdfIDQPVKT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 143 lpaqLSGGEQQRVALARAFSARPQILFADEPTGnldrqTGD-----RIADLLFELnQRQATTLVMVTHDVQLAAR-CQRR 216
Cdd:COG1134 147 ----YSSGMRARLAFAVATAVDPDILLVDEVLA-----VGDaafqkKCLARIREL-RESGRTVIFVSHSMGAVRRlCDRA 216
|
250
....*....|
gi 502612564 217 LRLVDGTLRE 226
Cdd:COG1134 217 IWLEKGRLVM 226
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
26-219 |
1.79e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 90.37 E-value: 1.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 26 LTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRllgqplsqldeegraALRARDIGFVFQSFMLVPTL-- 103
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR---------------RAGGARVAYVPQRSEVPDSLpl 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 104 TALENVQL-----PALLRGEREHDsRQRAAALLTQLGLgQRLRHLP-AQLSGGEQQRVALARAFSARPQILFADEPTGNL 177
Cdd:NF040873 73 TVRDLVAMgrwarRGLWRRLTRDD-RAAVDDALERVGL-ADLAGRQlGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 502612564 178 DRQTGDRIADLLFELNQRQAtTLVMVTHDVQLAARCQRRLRL 219
Cdd:NF040873 151 DAESRERIIALLAEEHARGA-TVVVVTHDLELVRRADPCVLL 191
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-212 |
1.91e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 92.03 E-value: 1.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 21 NQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDD------ASAGEVRLLGQPLSQLDeegraALRAR-DIGFV 93
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQID-----AIKLRkEVGMV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 94 FQSFMLVPTLTALENVQLPALLRGERE-HDSRQRAAALLTQLGLGQ----RLRHLPAQLSGGEQQRVALARAFSARPQIL 168
Cdd:PRK14246 96 FQQPNPFPHLSIYDNIAYPLKSHGIKEkREIKKIVEECLRKVGLWKevydRLNSPASQLSGGQQQRLTIARALALKPKVL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 502612564 169 FADEPTGNLDRQTGDRIADLLFELnqRQATTLVMVTHDVQLAAR 212
Cdd:PRK14246 176 LMDEPTSMIDIVNSQAIEKLITEL--KNEIAIVIVSHNPQQVAR 217
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
25-225 |
3.81e-22 |
|
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: 94.04 E-value: 3.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 25 ILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEgraaLRARDIGFVFQSFMLVPTlT 104
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDRE----ELGRHIGYLPQDVELFDG-T 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 105 ALENVqlpALLRgerEHDSRQ-RAAALL---------------TQLGLGqrlrhlPAQLSGGEQQRVALARAFSARPQIL 168
Cdd:COG4618 422 IAENI---ARFG---DADPEKvVAAAKLagvhemilrlpdgydTRIGEG------GARLSGGQRQRIGLARALYGDPRLV 489
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502612564 169 FADEPTGNLDRQTGDRIADLLFELNQRQATTlVMVTHDVQLAARCQRRLRLVDGTLR 225
Cdd:COG4618 490 VLDEPNSNLDDEGEAALAAAIRALKARGATV-VVITHRPSLLAAVDKLLVLRDGRVQ 545
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
6-222 |
5.03e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 91.79 E-value: 5.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 6 VIEVHHVAKRVGEGenqiSILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSqldeeGRAAL 85
Cdd:PRK13537 7 PIDFRNVEKRYGDK----LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVP-----SRARH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 86 RARDIGFVFQSFMLVPTLTALENVQLPALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARP 165
Cdd:PRK13537 78 ARQRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502612564 166 QILFADEPTGNLDRQTGDRIADLLFELNQRQATTLvMVTHDVQLAARCQRRLRLVDG 222
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARHLMWERLRSLLARGKTIL-LTTHFMEEAERLCDRLCVIEE 213
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
4-204 |
5.23e-22 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 91.00 E-value: 5.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 4 QNVIEVHHVAK----RVGEGENQ-ISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQld 78
Cdd:PRK15112 2 ETLLEVRNLSKtfryRTGWFRRQtVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHF-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 79 eeGRAALRARDIGFVFQ--SFMLVPTLTALENVQLPALLRGEREHDSR-QRAAALLTQLGL-GQRLRHLPAQLSGGEQQR 154
Cdd:PRK15112 80 --GDYSYRSQRIRMIFQdpSTSLNPRQRISQILDFPLRLNTDLEPEQReKQIIETLRQVGLlPDHASYYPHMLAPGQKQR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 502612564 155 VALARAFSARPQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVT 204
Cdd:PRK15112 158 LGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVT 207
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
4-227 |
1.02e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 90.53 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 4 QNVIEVHHVA---KRVGEGENQISiLTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGqpLSQLDEE 80
Cdd:PRK13633 2 NEMIKCKNVSykyESNEESTEKLA-LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 81 GRAALRARdIGFVFQS--FMLVPTLTAlENVQL-PALLrGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVAL 157
Cdd:PRK13633 79 NLWDIRNK-AGMVFQNpdNQIVATIVE-EDVAFgPENL-GIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502612564 158 ARAFSARPQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAARCQRRLRL------VDGTLREV 227
Cdd:PRK13633 156 AGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMdsgkvvMEGTPKEI 231
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
5-222 |
1.22e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 90.18 E-value: 1.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 5 NVIEVHHVAKRVGEGENQiSILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQplsQLDEEGRAA 84
Cdd:PRK13650 3 NIIEVKNLTFKYKEDQEK-YTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD---LLTEENVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 85 LRaRDIGFVFQS----FM--LVPTLTA--LENVQLPallrgerEHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVA 156
Cdd:PRK13650 79 IR-HKIGMVFQNpdnqFVgaTVEDDVAfgLENKGIP-------HEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502612564 157 LARAFSARPQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAARCQRRLRLVDG 222
Cdd:PRK13650 151 IAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNG 216
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-207 |
1.44e-21 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 89.82 E-value: 1.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 1 MPAQNVIEVHHVAKRVGEGenqiSILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEE 80
Cdd:PRK11831 2 QSVANLVDMRGVSFTRGNR----CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 81 GRAALRARdIGFVFQSFMLVPTLTALENVQLPAllrgeREHdSRQRAAAL-------LTQLGLGQRLRHLPAQLSGGEQQ 153
Cdd:PRK11831 78 RLYTVRKR-MSMLFQSGALFTDMNVFDNVAYPL-----REH-TQLPAPLLhstvmmkLEAVGLRGAAKLMPSELSGGMAR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502612564 154 RVALARAFSARPQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDV 207
Cdd:PRK11831 151 RAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDV 204
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
26-207 |
1.57e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 89.89 E-value: 1.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 26 LTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPL-SQLDEEGRAALRaRDIGFVFQsFMLVPTL- 103
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItPETGNKNLKKLR-KKVSLVFQ-FPEAQLFe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 104 -TALENVQLPALLRGEREHDSRQRAAALLTQLGLGQRL-RHLPAQLSGGEQQRVALARAFSARPQILFADEPTGNLDRQT 181
Cdd:PRK13641 101 nTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLiSKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEG 180
|
170 180
....*....|....*....|....*.
gi 502612564 182 GDRIADlLFELNQRQATTLVMVTHDV 207
Cdd:PRK13641 181 RKEMMQ-LFKDYQKAGHTVILVTHNM 205
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
7-223 |
1.58e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 92.15 E-value: 1.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGegenQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEGRAALr 86
Cdd:PRK09700 6 ISMAGIGKSFG----PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 87 arDIGFVFQSFMLVPTLTALENVQLPALLRGE-------REHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALAR 159
Cdd:PRK09700 81 --GIGIIYQELSVIDELTVLENLYIGRHLTKKvcgvniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502612564 160 AFSARPQILFADEPTGNLdrqTGDRIADLLFELNQ--RQATTLVMVTHDV-QLAARCQRRLRLVDGT 223
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSL---TNKEVDYLFLIMNQlrKEGTAIVYISHKLaEIRRICDRYTVMKDGS 222
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
5-211 |
1.70e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 89.79 E-value: 1.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 5 NVIEVHHVAKRVGEGENQisiLTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEgraA 84
Cdd:PRK13647 3 NIIEVEDLHFRYKDGTKA---LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEK---W 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 85 LRARdIGFVFQSfmlvP-----TLTALENVQLPALLRGEREHDSRQRAAALLTQLGLgQRLRH-LPAQLSGGEQQRVALA 158
Cdd:PRK13647 77 VRSK-VGLVFQD----PddqvfSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRM-WDFRDkPPYHLSYGQKKRVAIA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502612564 159 RAFSARPQILFADEPTGNLDRQTGDRIADLLFELNQrQATTLVMVTHDVQLAA 211
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHN-QGKTVIVATHDVDLAA 202
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
14-206 |
2.05e-21 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 88.62 E-value: 2.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 14 KRVGEGENQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEgraALRaRDIGFV 93
Cdd:PRK10247 11 QNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPE---IYR-QQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 94 FQSfmlvPTL---TALENVQLPALLRGEREhdSRQRAAALLTQLGLGQRLRHLP-AQLSGGEQQRVALARAFSARPQILF 169
Cdd:PRK10247 87 AQT----PTLfgdTVYDNLIFPWQIRNQQP--DPAIFLDDLERFALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLL 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 502612564 170 ADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHD 206
Cdd:PRK10247 161 LDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
29-226 |
2.25e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 90.15 E-value: 2.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 29 VDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLG-QPLSQldeegRAALrARDIGFVF-QSFMLVPTLTAL 106
Cdd:COG4586 41 ISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyVPFKR-----RKEF-ARRIGVVFgQRSQLWWDLPAI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 107 ENVQLPALLRGEREHDSRQRAAALLTQLGLGQRLrHLPA-QLSGGEQQRVALARAFSARPQILFADEPTGNLDRQTGDRI 185
Cdd:COG4586 115 DSFRLLKAIYRIPDAEYKKRLDELVELLDLGELL-DTPVrQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAI 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502612564 186 ADLLFELNQRQATTLVMVTHDVQ-LAARCQRRL-----RLV-DGTLRE 226
Cdd:COG4586 194 REFLKEYNRERGTTILLTSHDMDdIEALCDRVIvidhgRIIyDGSLEE 241
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
25-219 |
3.12e-21 |
|
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: 87.41 E-value: 3.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 25 ILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEgraalRARDIGFVFQSFMLVPTLT 104
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDE-----PHENILYLGHLPGLKPELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 105 ALENVQLPAllrgeREHDSRQRAA-ALLTQLGLgQRLRHLPA-QLSGGEQQRVALARAFSARPQILFADEPTGNLDRQTG 182
Cdd:TIGR01189 90 ALENLHFWA-----AIHGGAQRTIeDALAAVGL-TGFEDLPAaQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGV 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 502612564 183 DRIADLLFELNQRQATTLVMVTHDVQLAArcQRRLRL 219
Cdd:TIGR01189 164 ALLAGLLRAHLARGGIVLLTTHQDLGLVE--ARELRL 198
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
25-224 |
5.50e-21 |
|
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: 90.87 E-value: 5.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 25 ILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEgraaLRARDIGFVFQSFMLVPTlT 104
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRE----TFGKHIGYLPQDVELFPG-T 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 105 ALENVQlpallRGEREHDSRQ-RAAALLTqlGLGQRLRHLP-----------AQLSGGEQQRVALARAFSARPQILFADE 172
Cdd:TIGR01842 408 VAENIA-----RFGENADPEKiIEAAKLA--GVHELILRLPdgydtvigpggATLSGGQRQRIALARALYGDPKLVVLDE 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 502612564 173 PTGNLDRQTGDRIADLLFELNQRQATTLVmVTHDVQLAARCQRRLRLVDGTL 224
Cdd:TIGR01842 481 PNSNLDEEGEQALANAIKALKARGITVVV-ITHRPSLLGCVDKILVLQDGRI 531
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
25-205 |
9.28e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 86.08 E-value: 9.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 25 ILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPlsqlDEEGRAALRARDIGfvFQSFMlVPTLT 104
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD----IDDPDVAEACHYLG--HRNAM-KPALT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 105 ALENVQLPALLRGEREHDsrqrAAALLTQLGLgQRLRHLPAQ-LSGGEQQRVALARAFSARPQILFADEPTGNLDRQTGD 183
Cdd:PRK13539 90 VAENLEFWAAFLGGEELD----IAAALEAVGL-APLAHLPFGyLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVA 164
|
170 180
....*....|....*....|..
gi 502612564 184 RIADLLFElNQRQATTLVMVTH 205
Cdd:PRK13539 165 LFAELIRA-HLAQGGIVIAATH 185
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
27-219 |
1.19e-20 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 86.01 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 27 TAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEgraalrardigfvFQSFMLV------ 100
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE-------------YHQDLLYlghqpg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 101 --PTLTALENVQLPALLRGERehdSRQRAAALLTQLGLGQRLrHLPA-QLSGGEQQRVALARAFSARPQILFADEPTGNL 177
Cdd:PRK13538 85 ikTELTALENLRFYQRLHGPG---DDEALWEALAQVGLAGFE-DVPVrQLSAGQQRRVALARLWLTRAPLWILDEPFTAI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 502612564 178 DRQTGDRIADlLFELNQRQATTLVMVTH-DVQLAARCQRRLRL 219
Cdd:PRK13538 161 DKQGVARLEA-LLAQHAEQGGMVILTTHqDLPVASDKVRKLRL 202
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
40-227 |
1.49e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 86.75 E-value: 1.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 40 ALIGESGSGKSTLLGILAGLDDASAgEVRLLGQplsqLDEEGR---------AALRaRDIGFVFQSFMLVPtLTALENVQ 110
Cdd:PRK14239 35 ALIGPSGSGKSTLLRSINRMNDLNP-EVTITGS----IVYNGHniysprtdtVDLR-KEIGMVFQQPNPFP-MSIYENVV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 111 LPALLRGEREH-------DSRQRAAALLTQLGlgQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEPTGNLDRQTGD 183
Cdd:PRK14239 108 YGLRLKGIKDKqvldeavEKSLKGASIWDEVK--DRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAG 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 502612564 184 RIADLLFELnqRQATTLVMVTHDVQLAAR-CQRRLRLVDGTLREV 227
Cdd:PRK14239 186 KIEETLLGL--KDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEY 228
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-217 |
1.76e-20 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 89.53 E-value: 1.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 1 MPAQNVIEVHHVAKRVGEGENQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEV-------RLLGQP 73
Cdd:PRK10261 7 LDARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllRRRSRQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 74 LSQLDEEGRAAL---RARDIGFVFQSFM--LVPTLTALENV-QLPALLRGEREHDSRQRAAALLTQLGLGQR---LRHLP 144
Cdd:PRK10261 87 VIELSEQSAAQMrhvRGADMAMIFQEPMtsLNPVFTVGEQIaESIRLHQGASREEAMVEAKRMLDQVRIPEAqtiLSRYP 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502612564 145 AQLSGGEQQRVALARAFSARPQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAARCQRRL 217
Cdd:PRK10261 167 HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRV 239
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
23-211 |
2.18e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 86.78 E-value: 2.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 23 ISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLD-EEGRaalraRDIGFVFQS---FM 98
Cdd:PRK13652 17 KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENiREVR-----KFVGLVFQNpddQI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 99 LVPTLTalENVQLPALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEPTGNLD 178
Cdd:PRK13652 92 FSPTVE--QDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLD 169
|
170 180 190
....*....|....*....|....*....|...
gi 502612564 179 RQTGDRIADLLFELNQRQATTLVMVTHDVQLAA 211
Cdd:PRK13652 170 PQGVKELIDFLNDLPETYGMTVIFSTHQLDLVP 202
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
22-224 |
2.50e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 87.06 E-value: 2.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 22 QISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEGRA------------------ 83
Cdd:PRK13651 19 ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKekvleklviqktrfkkik 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 84 ---ALRARdIGFVFQ--SFMLVPTlTALENVQLPALLRGEREHDSRQRAAALLTQLGLGQR-LRHLPAQLSGGEQQRVAL 157
Cdd:PRK13651 99 kikEIRRR-VGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESyLQRSPFELSGGQKRRVAL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502612564 158 ARAFSARPQILFADEPTGNLDRQTGDRIADLLFELNQrQATTLVMVTHDVQLA-ARCQRRLRLVDGTL 224
Cdd:PRK13651 177 AGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNK-QGKTIILVTHDLDNVlEWTKRTIFFKDGKI 243
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
26-205 |
2.87e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 88.45 E-value: 2.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 26 LTAVDLVVKRGQSLALIGESGSGKSTLLGILAGL--DDASAGEVRLLGQPL--SQLDEEGRAAlrardIGFVFQSFMLVP 101
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEELqaSNIRDTERAG-----IAIIHQELALVK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 102 TLTALENVQLPA-LLRGEREHDSR--QRAAALLTQLGLG----QRLRHlpaqLSGGEQQRVALARAFSARPQILFADEPT 174
Cdd:PRK13549 96 ELSVLENIFLGNeITPGGIMDYDAmyLRAQKLLAQLKLDinpaTPVGN----LGLGQQQLVEIAKALNKQARLLILDEPT 171
|
170 180 190
....*....|....*....|....*....|.
gi 502612564 175 GNLDRQTGDRIADLLFELnQRQATTLVMVTH 205
Cdd:PRK13549 172 ASLTESETAVLLDIIRDL-KAHGIACIYISH 201
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
7-178 |
2.96e-20 |
|
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: 85.29 E-value: 2.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGEGEnqisILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEGRAALr 86
Cdd:cd03218 1 LRAENLSKRYGKRK----VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARL- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 87 arDIGFVFQSFMLVPTLTALENVQLPALLRGEREHDSRQRAAALLTQLGLgQRLRHLPA-QLSGGEQQRVALARAFSARP 165
Cdd:cd03218 76 --GIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHI-THLRKSKAsSLSGGERRRVEIARALATNP 152
|
170
....*....|...
gi 502612564 166 QILFADEPTGNLD 178
Cdd:cd03218 153 KFLLLDEPFAGVD 165
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
26-212 |
3.37e-20 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 85.66 E-value: 3.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 26 LTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLdDASAGEVRLLGQPLSQLDEEGRAALRArdigFVFQSFMLVPTLTA 105
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAELARHRA----YLSQQQSPPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 106 LENVQLpALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAF-------SARPQILFADEPTGNLD 178
Cdd:COG4138 87 FQYLAL-HQPAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwptiNPEGQLLLLDEPMNSLD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 502612564 179 rqtgdrIA------DLLFELNQRQATTlVMVTHDVQLAAR 212
Cdd:COG4138 166 ------VAqqaaldRLLRELCQQGITV-VMSSHDLNHTLR 198
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
26-224 |
3.47e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 85.96 E-value: 3.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 26 LTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEgraALRaRDIGFVFQ--------SF 97
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFE---KLR-KHIGIVFQnpdnqfvgSI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 98 MLVPTLTALENVQLPallrgereHDSRQR-AAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEPTGN 176
Cdd:PRK13648 101 VKYDVAFGLENHAVP--------YDEMHRrVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSM 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502612564 177 LDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAARCQRRLRLVDGTL 224
Cdd:PRK13648 173 LDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTV 220
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
26-181 |
4.20e-20 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 88.14 E-value: 4.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 26 LTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQldeEGRAALRARDIGFVFQSFMLVPTLTA 105
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTF---NGPKSSQEAGIGIIHQELNLIPQLTI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 106 LENVQLpallrgEREHDSR----------QRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEPTG 175
Cdd:PRK10762 97 AENIFL------GREFVNRfgridwkkmyAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTD 170
|
....*..
gi 502612564 176 NL-DRQT 181
Cdd:PRK10762 171 ALtDTET 177
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
29-205 |
4.75e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 85.94 E-value: 4.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 29 VDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEGRAALRARDIGFVFQ---SFMLVPTLta 105
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQfpeSQLFEETV-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 106 LENVQLPALLRGEREHDSRQRAAALLTQLGLGQRL-RHLPAQLSGGEQQRVALARAFSARPQILFADEPTGNLDRQTgdR 184
Cdd:PRK13643 103 LKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA--R 180
|
170 180
....*....|....*....|..
gi 502612564 185 IADL-LFELNQRQATTLVMVTH 205
Cdd:PRK13643 181 IEMMqLFESIHQSGQTVVLVTH 202
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
7-209 |
5.13e-20 |
|
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: 82.50 E-value: 5.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGEGEnqisILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVrllgqplsqldeegraalr 86
Cdd:cd03221 1 IELENLSKTYGGKL----LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 87 ardigfvfqsfmlvptltalenvqlpallrgerehdsrqraaalltQLGLGQRLRHLPaQLSGGEQQRVALARAFSARPQ 166
Cdd:cd03221 58 ----------------------------------------------TWGSTVKIGYFE-QLSGGEKMRLALAKLLLENPN 90
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 502612564 167 ILFADEPTGNLDRQTGDRIADLLFELNQrqatTLVMVTHDVQL 209
Cdd:cd03221 91 LLLLDEPTNHLDLESIEALEEALKEYPG----TVILVSHDRYF 129
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
20-205 |
6.49e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 86.06 E-value: 6.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 20 ENQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRL-----------LGQPLSQLDEEGRAALRAR 88
Cdd:PRK13631 36 ENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknnHELITNPYSKKIKNFKELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 89 D-IGFVFQ--SFMLVPTlTALENVQLPALLRGEREHDSRQRAAALLTQLGLGQR-LRHLPAQLSGGEQQRVALARAFSAR 164
Cdd:PRK13631 116 RrVSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSyLERSPFGLSGGQKRRVAIAGILAIQ 194
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 502612564 165 PQILFADEPTGNLDRQTGDRIADLLFElNQRQATTLVMVTH 205
Cdd:PRK13631 195 PEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITH 234
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
40-226 |
1.04e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 85.15 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 40 ALIGESGSGKSTLLGILAGLDDASAGeVRLLGQPLSQldeeGRAALRARDI-------GFVFQSFMLVPtLTALENVqlp 112
Cdd:PRK14271 51 SLMGPTGSGKTTFLRTLNRMNDKVSG-YRYSGDVLLG----GRSIFNYRDVlefrrrvGMLFQRPNPFP-MSIMDNV--- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 113 alLRGEREH------DSRQRAAALLTQLGL----GQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEPTGNLDRQTG 182
Cdd:PRK14271 122 --LAGVRAHklvprkEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTT 199
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 502612564 183 DRIADLLFELNQRqaTTLVMVTHDVQLAARCQRRLRL-VDGTLRE 226
Cdd:PRK14271 200 EKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALfFDGRLVE 242
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
25-219 |
1.04e-19 |
|
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: 83.31 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 25 ILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEgraalRARDIGFVFQSFMLVPTLT 104
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDS-----IARGLLYLGHAPGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 105 ALENVQLPAllrgeREHDSRQRAAALlTQLGLGQrLRHLP-AQLSGGEQQRVALARAFSARPQILFADEPTGNLDRQTGD 183
Cdd:cd03231 90 VLENLRFWH-----ADHSDEQVEEAL-ARVGLNG-FEDRPvAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVA 162
|
170 180 190
....*....|....*....|....*....|....*.
gi 502612564 184 RIADLLFELNQRQATTLVMVTHDVQLAARCQRRLRL 219
Cdd:cd03231 163 RFAEAMAGHCARGGMVVLTTHQDLGLSEAGARELDL 198
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
29-209 |
1.76e-19 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 83.89 E-value: 1.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 29 VDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLsqldeEGRAALRARDIGFV--FQSFMLVPTLTAL 106
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHI-----EGLPGHQIARMGVVrtFQHVRLFREMTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 107 ENV-----------------QLPALLRGEREhdSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQILF 169
Cdd:PRK11300 99 ENLlvaqhqqlktglfsgllKTPAFRRAESE--ALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILM 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 502612564 170 ADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQL 209
Cdd:PRK11300 177 LDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKL 216
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
22-205 |
2.39e-19 |
|
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: 83.36 E-value: 2.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 22 QISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEgraALRARdIGFVFQSFMLVP 101
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLR---WLRSQ-IGLVSQEPVLFD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 102 TlTALENVqlpALLRGEREHDSRQRAAALL--------------TQLGlgQRlrhlPAQLSGGEQQRVALARAFSARPQI 167
Cdd:cd03249 91 G-TIAENI---RYGKPDATDEEVEEAAKKAnihdfimslpdgydTLVG--ER----GSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 502612564 168 LFADEPTGNLDRQTGDRIADLLFELnqRQATTLVMVTH 205
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRA--MKGRTTIVIAH 196
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
29-212 |
2.50e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 83.68 E-value: 2.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 29 VDLVVKRGQSLALIGESGSGKSTLLGILAGLDD-----ASAGEVRLLGQPL--SQLDEegrAALRARdIGFVFQSFMLVP 101
Cdd:PRK14243 29 VWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLyaPDVDP---VEVRRR-IGMVFQKPNPFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 102 TlTALENVQLPALLRGER-------EHDSRQraAALLTQLGlgQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEPT 174
Cdd:PRK14243 105 K-SIYDNIAYGARINGYKgdmdelvERSLRQ--AALWDEVK--DKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPC 179
|
170 180 190
....*....|....*....|....*....|....*...
gi 502612564 175 GNLDRQTGDRIADLLFELNQRQatTLVMVTHDVQLAAR 212
Cdd:PRK14243 180 SALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAAR 215
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
7-201 |
2.76e-19 |
|
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: 83.05 E-value: 2.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVakRVGEGENQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDeegRAALR 86
Cdd:cd03251 1 VEFKNV--TFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYT---LASLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 87 aRDIGFVFQSFMLVPTlTALENVQLPAllRGEREHDSRQRA-AALLTQL------GLGQRLRHLPAQLSGGEQQRVALAR 159
Cdd:cd03251 76 -RQIGLVSQDVFLFND-TVAENIAYGR--PGATREEVEEAArAANAHEFimelpeGYDTVIGERGVKLSGGQRQRIAIAR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 502612564 160 AFSARPQILFADEPTGNLDRQTGDRIADLLFELNQRQaTTLV 201
Cdd:cd03251 152 ALLKDPPILILDEATSALDTESERLVQAALERLMKNR-TTFV 192
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
6-224 |
3.12e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 83.60 E-value: 3.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 6 VIEVHHVAKRVgEGENQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQplsQLDEEGRAAL 85
Cdd:PRK13642 4 ILEVENLVFKY-EKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE---LLTAENVWNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 86 RaRDIGFVFQ--------SFMLVPTLTALENVQLPallrgeREHDSRQRAAALLTQLGLGQRLRHlPAQLSGGEQQRVAL 157
Cdd:PRK13642 80 R-RKIGMVFQnpdnqfvgATVEDDVAFGMENQGIP------REEMIKRVDEALLAVNMLDFKTRE-PARLSGGQKQRVAV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502612564 158 ARAFSARPQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAARCQRRLRLVDGTL 224
Cdd:PRK13642 152 AGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEI 218
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
29-212 |
3.63e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 83.68 E-value: 3.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 29 VDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQL--DEEGRAaLRARdIGFVFQsfmlVPTLTAL 106
Cdd:PRK13646 26 VNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKtkDKYIRP-VRKR-IGMVFQ----FPESQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 107 ENVQLPALLRGERE-----HDSRQRAAALLTQLGLGQRLRHL-PAQLSGGEQQRVALARAFSARPQILFADEPTGNLDRQ 180
Cdd:PRK13646 100 EDTVEREIIFGPKNfkmnlDEVKNYAHRLLMDLGFSRDVMSQsPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQ 179
|
170 180 190
....*....|....*....|....*....|..
gi 502612564 181 TGDRIADLLFELNQRQATTLVMVTHDVQLAAR 212
Cdd:PRK13646 180 SKRQVMRLLKSLQTDENKTIILVSHDMNEVAR 211
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6-222 |
5.15e-19 |
|
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: 84.88 E-value: 5.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 6 VIEVHHVAKRVGEgenqISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASA--GEVRLLGQPL--SQLDEEG 81
Cdd:TIGR02633 1 LLEMKGIVKTFGG----VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLkaSNIRDTE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 82 RAAlrardIGFVFQSFMLVPTLTALENVQL--PALLRGEREHDSR--QRAAALLTQLGLGQRLRHLP-AQLSGGEQQRVA 156
Cdd:TIGR02633 77 RAG-----IVIIHQELTLVPELSVAENIFLgnEITLPGGRMAYNAmyLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502612564 157 LARAFSARPQILFADEPTGNLDRQTGDRIADLLFELnQRQATTLVMVTHDV-QLAARCQRRLRLVDG 222
Cdd:TIGR02633 152 IAKALNKQARLLILDEPSSSLTEKETEILLDIIRDL-KAHGVACVYISHKLnEVKAVCDTICVIRDG 217
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
6-178 |
5.27e-19 |
|
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: 82.32 E-value: 5.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 6 VIEVHHVAKRVGEGEnqisILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEGRAAL 85
Cdd:TIGR04406 1 TLVAENLIKSYKKRK----VVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 86 rarDIGFVFQSFMLVPTLTALENVQLPALLRGEREHDSR-QRAAALLTQLGLgQRLRHLPAQ-LSGGEQQRVALARAFSA 163
Cdd:TIGR04406 77 ---GIGYLPQEASIFRKLTVEENIMAVLEIRKDLDRAEReERLEALLEEFQI-SHLRDNKAMsLSGGERRRVEIARALAT 152
|
170
....*....|....*
gi 502612564 164 RPQILFADEPTGNLD 178
Cdd:TIGR04406 153 NPKFILLDEPFAGVD 167
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
7-223 |
5.52e-19 |
|
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: 81.36 E-value: 5.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGEGENQIS-ILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQplsqldeegraal 85
Cdd:cd03250 1 ISVEDASFTWDSGEQETSfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 86 rardIGFVFQSFMLVPTlTALENVqlpalLRGEREHDSRQ----RAAALLTQLGLgqrlrhLPAQ-----------LSGG 150
Cdd:cd03250 68 ----IAYVSQEPWIQNG-TIRENI-----LFGKPFDEERYekviKACALEPDLEI------LPDGdlteigekginLSGG 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502612564 151 EQQRVALARAFSARPQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAARCQRRLRLVDGT 223
Cdd:cd03250 132 QKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
25-189 |
5.74e-19 |
|
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: 81.14 E-value: 5.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 25 ILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDAS--AGEVRLLGQPlsqLDEEGRaalraRDIGFVFQSFMLVPT 102
Cdd:cd03232 22 LLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRP---LDKNFQ-----RSTGYVEQQDVHSPN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 103 LTALENVQLPALLRGerehdsrqraaalltqLGLGQRlrhlpaqlsggeqQRVALARAFSARPQILFADEPTGNLDRQTG 182
Cdd:cd03232 94 LTVREALRFSALLRG----------------LSVEQR-------------KRLTIGVELAAKPSILFLDEPTSGLDSQAA 144
|
....*..
gi 502612564 183 DRIADLL 189
Cdd:cd03232 145 YNIVRFL 151
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
26-205 |
7.49e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 82.48 E-value: 7.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 26 LTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEGRAALRARDIGFVFQ---SFMLVPT 102
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRKKVGLVFQfpeSQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 103 LtaLENVQLPALLRGEREHDSRQRAAALLTQLGLGQRLRHL-PAQLSGGEQQRVALARAFSARPQILFADEPTGNLDRQT 181
Cdd:PRK13649 103 V--LKDVAFGPQNFGVSQEEAEALAREKLALVGISESLFEKnPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180
|
170 180
....*....|....*....|....
gi 502612564 182 GDRIADLLFELNQrQATTLVMVTH 205
Cdd:PRK13649 181 RKELMTLFKKLHQ-SGMTIVLVTH 203
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
36-217 |
8.85e-19 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 84.52 E-value: 8.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 36 GQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEGRAALRaRDIGFVFQS--FMLVPTLTA----LENV 109
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALR-RDIQFIFQDpyASLDPRQTVgdsiMEPL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 110 QLPALLRGErehDSRQRAAALLTQLGL-GQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEPTGNLDRQTGDRIADL 188
Cdd:PRK10261 429 RVHGLLPGK---AAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINL 505
|
170 180
....*....|....*....|....*....
gi 502612564 189 LFELNQRQATTLVMVTHDVQLAARCQRRL 217
Cdd:PRK10261 506 LLDLQRDFGIAYLFISHDMAVVERISHRV 534
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
25-201 |
1.06e-18 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 84.10 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 25 ILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEegrAALRaRDIGfvfqsfmLVPTLT 104
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQ---ASLR-AAIG-------IVPQDT 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 105 ALENVQLPALLRGEREHDSRQ--RAAALLTQlgLGQRLRHLPAQ-----------LSGGEQQRVALARAFSARPQILFAD 171
Cdd:COG5265 442 VLFNDTIAYNIAYGRPDASEEevEAAARAAQ--IHDFIESLPDGydtrvgerglkLSGGEKQRVAIARTLLKNPPILIFD 519
|
170 180 190
....*....|....*....|....*....|
gi 502612564 172 EPTGNLDRQTGDRIADLLFELNQRQaTTLV 201
Cdd:COG5265 520 EATSALDSRTERAIQAALREVARGR-TTLV 548
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-212 |
1.21e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 82.01 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 25 ILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASaGEVRLLGQP--LSQLDEEGRAALRA--RDIGFVFQSFMLV 100
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGRVefFNQNIYERRVNLNRlrRQVSMVHPKPNLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 101 PtLTALENVQLPALLRGEREH-------DSRQRAAALLTQLGlgQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEP 173
Cdd:PRK14258 101 P-MSVYDNVAYGVKIVGWRPKleiddivESALKDADLWDEIK--HKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEP 177
|
170 180 190
....*....|....*....|....*....|....*....
gi 502612564 174 TGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAAR 212
Cdd:PRK14258 178 CFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSR 216
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
6-173 |
1.90e-18 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 80.84 E-value: 1.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 6 VIEVHHVAKRVGEGEnqisILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEGRAAL 85
Cdd:COG1137 3 TLEAENLVKSYGKRT----VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 86 rarDIGF------VFQSfmlvptLTALENVQLPALLRGEREHDSRQRAAALLTQLGLGqRLRHLPA-QLSGGEQQRVALA 158
Cdd:COG1137 79 ---GIGYlpqeasIFRK------LTVEDNILAVLELRKLSKKEREERLEELLEEFGIT-HLRKSKAySLSGGERRRVEIA 148
|
170
....*....|....*
gi 502612564 159 RAFSARPQILFADEP 173
Cdd:COG1137 149 RALATNPKFILLDEP 163
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
6-177 |
2.15e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 83.18 E-value: 2.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 6 VIEVHHVAKRVGegenQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLdeegrAAL 85
Cdd:PRK15439 11 LLCARSISKQYS----GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARL-----TPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 86 RARDIG--FVFQSFMLVPTLTALENVqlpaLLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSA 163
Cdd:PRK15439 82 KAHQLGiyLVPQEPLLFPNLSVKENI----LFGLPKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMR 157
|
170
....*....|....
gi 502612564 164 RPQILFADEPTGNL 177
Cdd:PRK15439 158 DSRILILDEPTASL 171
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
33-207 |
2.24e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 81.08 E-value: 2.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 33 VKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQldeegraALRARDIGFVFQSF-------MLVPTLTA 105
Cdd:PRK15056 30 VPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ-------ALQKNLVAYVPQSEevdwsfpVLVEDVVM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 106 LENVQLPALLRGEREHDsRQRAAALLTQLGLgQRLRHLP-AQLSGGEQQRVALARAFSARPQILFADEPTGNLDRQTGDR 184
Cdd:PRK15056 103 MGRYGHMGWLRRAKKRD-RQIVTAALARVDM-VEFRHRQiGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEAR 180
|
170 180
....*....|....*....|...
gi 502612564 185 IADLLFELNQRQATTLVMvTHDV 207
Cdd:PRK15056 181 IISLLRELRDEGKTMLVS-THNL 202
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
26-227 |
2.31e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 81.25 E-value: 2.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 26 LTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSqlDEEGRAALRARDIGFVFQsfmlVPTLTA 105
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDIT--DKKVKLSDIRKKVGLVFQ----YPEYQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 106 LE------------NVQLpallrGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEP 173
Cdd:PRK13637 97 FEetiekdiafgpiNLGL-----SEEEIENRVKRAMNIVGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502612564 174 TGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAARCQRRLRL-------VDGTLREV 227
Cdd:PRK13637 172 TAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVmnkgkceLQGTPREV 232
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
26-205 |
2.91e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 82.65 E-value: 2.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 26 LTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPlsQLDEEGRAALRArDIGFVFQSFMLVPTLTA 105
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQE--MRFASTTAALAA-GVAIIYQELHLVPEMTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 106 LENV---QLPALLRGEREHDSRQRAAALLTQLGL----GQRLRHlpaqLSGGEQQRVALARAFSARPQILFADEPTGNLD 178
Cdd:PRK11288 97 AENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVdidpDTPLKY----LSIGQRQMVEIAKALARNARVIAFDEPTSSLS 172
|
170 180
....*....|....*....|....*..
gi 502612564 179 RQTGDRIADLLFELnQRQATTLVMVTH 205
Cdd:PRK11288 173 AREIEQLFRVIREL-RAEGRVILYVSH 198
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
23-225 |
3.11e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 82.20 E-value: 3.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 23 ISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDeegrAALRARDIGFVFQSFMLVPT 102
Cdd:PRK09536 16 TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALS----ARAASRRVASVPQDTSLSFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 103 LTALENVQL---PALLRGEReHDSRQRAAA--LLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEPTGNL 177
Cdd:PRK09536 92 FDVRQVVEMgrtPHRSRFDT-WTETDRAAVerAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 502612564 178 DRQTGDRIADLLFELNQrQATTLVMVTHDVQLAAR-CQRRLRLVDGTLR 225
Cdd:PRK09536 171 DINHQVRTLELVRRLVD-DGKTAVAAIHDLDLAARyCDELVLLADGRVR 218
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
26-208 |
3.45e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 80.80 E-value: 3.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 26 LTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGqpLSQLDEEGRAALRaRDIGFVFQS----FMLVP 101
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG--IDTGDFSKLQGIR-KLVGIVFQNpetqFVGRT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 102 TLTAL----ENVQLPALlrgerehDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEPTGNL 177
Cdd:PRK13644 95 VEEDLafgpENLCLPPI-------EIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSML 167
|
170 180 190
....*....|....*....|....*....|.
gi 502612564 178 DRQTGDRIADLLFELNqRQATTLVMVTHDVQ 208
Cdd:PRK13644 168 DPDSGIAVLERIKKLH-EKGKTIVYITHNLE 197
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
29-174 |
4.81e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 81.99 E-value: 4.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 29 VDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEegRAALRARdIGFV---FQSFMLVPTLTA 105
Cdd:COG1129 271 VSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSP--RDAIRAG-IAYVpedRKGEGLVLDLSI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 106 LENVQLPAL--------LRGEREhdsRQRAAALLTQL-----GLGQRLRhlpaQLSGGEQQRVALARAFSARPQILFADE 172
Cdd:COG1129 348 RENITLASLdrlsrgglLDRRRE---RALAEEYIKRLriktpSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILDE 420
|
..
gi 502612564 173 PT 174
Cdd:COG1129 421 PT 422
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
25-205 |
5.30e-18 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 82.07 E-value: 5.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 25 ILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLdeeGRAALRaRDIGFVFQ-------SF 97
Cdd:PRK10790 356 VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSL---SHSVLR-QGVAMVQQdpvvladTF 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 98 MLVPTL----------TALENVQLPALLRGEREhdsrqraaalltqlGLGQRLRHLPAQLSGGEQQRVALARAFSARPQI 167
Cdd:PRK10790 432 LANVTLgrdiseeqvwQALETVQLAELARSLPD--------------GLYTPLGEQGNNLSVGQKQLLALARVLVQTPQI 497
|
170 180 190
....*....|....*....|....*....|....*...
gi 502612564 168 LFADEPTGNLDRQTGDRIADLLFELnqRQATTLVMVTH 205
Cdd:PRK10790 498 LILDEATANIDSGTEQAIQQALAAV--REHTTLVVIAH 533
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
7-221 |
6.12e-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: 77.58 E-value: 6.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGEGEnqiSILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQplsqldeegraalr 86
Cdd:cd03223 1 IELENLSLATPDGR---VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEG-------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 87 aRDIGFVFQ-SFMLVPTLtalenvqlpallrgeREhdsrqraaalltqlglgQRLRHLPAQLSGGEQQRVALARAFSARP 165
Cdd:cd03223 64 -EDLLFLPQrPYLPLGTL---------------RE-----------------QLIYPWDDVLSGGEQQRLAFARLLLHKP 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502612564 166 QILFADEPTGNLDRQTGDRIADLLfelnQRQATTLVMVTHDVQLAARCQRRLRLVD 221
Cdd:cd03223 111 KFVFLDEATSALDEESEDRLYQLL----KELGITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
40-178 |
6.46e-18 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 81.07 E-value: 6.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 40 ALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSqlDEEGRAALRA--RDIGFVFQSFMLVPTLTALENvqlpaLLRG 117
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLF--DAEKGICLPPekRRIGYVFQDARLFPHYKVRGN-----LRYG 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502612564 118 EREHDsRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEPTGNLD 178
Cdd:PRK11144 101 MAKSM-VAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
29-201 |
2.09e-17 |
|
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: 76.70 E-value: 2.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 29 VDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEegRAALRARdIGFV---FQSFMLVPTLTA 105
Cdd:cd03215 19 VSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSP--RDAIRAG-IAYVpedRKREGLVLDLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 106 LENVQLPALLrgerehdsrqraaalltqlglgqrlrhlpaqlSGGEQQRVALARAFSARPQILFADEPTGNLDRQTGDRI 185
Cdd:cd03215 96 AENIALSSLL--------------------------------SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEI 143
|
170
....*....|....*.
gi 502612564 186 ADLLFELNQRQATTLV 201
Cdd:cd03215 144 YRLIRELADAGKAVLL 159
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
24-212 |
2.14e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 78.29 E-value: 2.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 24 SILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEgraaLRARDIGFVFQSFMLVPTL 103
Cdd:PRK10575 25 TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK----AFARKVAYLPQQLPAAEGM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 104 TALENVQL------PALLRGEREhdSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEPTGNL 177
Cdd:PRK10575 101 TVRELVAIgrypwhGALGRFGAA--DREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSAL 178
|
170 180 190
....*....|....*....|....*....|....*
gi 502612564 178 DRQTGDRIADLLFELNQRQATTLVMVTHDVQLAAR 212
Cdd:PRK10575 179 DIAHQVDVLALVHRLSQERGLTVIAVLHDINMAAR 213
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
7-201 |
3.80e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 79.62 E-value: 3.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGegeNQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLdeeGRAALR 86
Cdd:PRK13657 335 VEFDDVSFSYD---NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTV---TRASLR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 87 aRDIGFVFQSFMLVpTLTALENVQLPALLRGERE-HDSRQRAAAL---LTQLG-----LGQRLRhlpaQLSGGEQQRVAL 157
Cdd:PRK13657 409 -RNIAVVFQDAGLF-NRSIEDNIRVGRPDATDEEmRAAAERAQAHdfiERKPDgydtvVGERGR----QLSGGERQRLAI 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 502612564 158 ARAFSARPQILFADEPTGNLDRQTGDRIADLLFELNQRQaTTLV 201
Cdd:PRK13657 483 ARALLKDPPILILDEATSALDVETEAKVKAALDELMKGR-TTFI 525
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
37-210 |
4.08e-17 |
|
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: 79.67 E-value: 4.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 37 QSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLsqldEEGRAALRaRDIGFVFQSFMLVPTLTALENVQLPALLR 116
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI----ETNLDAVR-QSLGMCPQHNILFHHLTVAEHILFYAQLK 1031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 117 GEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEPTGNLDRQTGDRIADLLfeLNQRQ 196
Cdd:TIGR01257 1032 GRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRS 1109
|
170
....*....|....
gi 502612564 197 ATTLVMVTHDVQLA 210
Cdd:TIGR01257 1110 GRTIIMSTHHMDEA 1123
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
29-217 |
4.28e-17 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 78.31 E-value: 4.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 29 VDLVVKRGQSLALIGESGSGKSTLLGILAGLDD----ASAGEVRLLGQPLSQLDEEGRAALRARDIGFVFQSfmlvPT-- 102
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrVTADRMRFDDIDLLRLSPRERRKLVGHNVSMIFQE----PQsc 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 103 LTALENV--QLPALLRG--------EREHDSRQRAAALLTQLGLGQR---LRHLPAQLSGGEQQRVALARAFSARPQILF 169
Cdd:PRK15093 102 LDPSERVgrQLMQNIPGwtykgrwwQRFGWRKRRAIELLHRVGIKDHkdaMRSFPYELTEGECQKVMIAIALANQPRLLI 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502612564 170 ADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAARCQRRL 217
Cdd:PRK15093 182 ADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKI 229
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
26-207 |
5.20e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 77.74 E-value: 5.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 26 LTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVrLLGQ-----PLSQLDEEGRaaLRaRDIGFVFQ--SFM 98
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQT-IVGDyaipaNLKKIKEVKR--LR-KEIGLVFQfpEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 99 LVPTlTALENVQLPALLRGEREHDSRQRAAALLTQLGLGQR-LRHLPAQLSGGEQQRVALARAFSARPQILFADEPTGNL 177
Cdd:PRK13645 103 LFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDyVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGL 181
|
170 180 190
....*....|....*....|....*....|
gi 502612564 178 DRQTGDRIADLLFELNQRQATTLVMVTHDV 207
Cdd:PRK13645 182 DPKGEEDFINLFERLNKEYKKRIIMVTHNM 211
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
7-226 |
1.01e-16 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 75.61 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGEGENQIsiLTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLdeeGRAALR 86
Cdd:cd03244 3 IEFKNVSLRYRPNLPPV--LKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKI---GLHDLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 87 ARdIGFVFQSfmlvPTL---------------------TALENVQLpallrgerehdsRQRAAALLTQLGLgqRLRHLPA 145
Cdd:cd03244 78 SR-ISIIPQD----PVLfsgtirsnldpfgeysdeelwQALERVGL------------KEFVESLPGGLDT--VVEEGGE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 146 QLSGGEQQRVALARAFSARPQILFADEPTGNLDRQTGDRIADLLFElnQRQATTLVMVTHDVQLAARCQRRLRLVDGTLR 225
Cdd:cd03244 139 NLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIRE--AFKDCTVLTIAHRLDTIIDSDRILVLDKGRVV 216
|
.
gi 502612564 226 E 226
Cdd:cd03244 217 E 217
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
24-212 |
1.05e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 76.21 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 24 SILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDeegrAALRARDIGFVFQSFMLVPTL 103
Cdd:PRK11231 16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLS----SRQLARRLALLPQHHLTPEGI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 104 TALENVQL---PAL-LRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEPTGNLDR 179
Cdd:PRK11231 92 TVRELVAYgrsPWLsLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDI 171
|
170 180 190
....*....|....*....|....*....|...
gi 502612564 180 QTGDRIADLLFELNQrQATTLVMVTHDVQLAAR 212
Cdd:PRK11231 172 NHQVELMRLMRELNT-QGKTVVTVLHDLNQASR 203
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
16-205 |
1.09e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 75.77 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 16 VGEGENQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAG--LDDASAGEVRLlgqPLSQLDEEgraalrardigfv 93
Cdd:COG2401 36 VELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDV---PDNQFGRE------------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 94 fqsfmlvptLTALENVqlpallrgEREHDSRQrAAALLTQLGLG--QRLRHLPAQLSGGEQQRVALARAFSARPQILFAD 171
Cdd:COG2401 100 ---------ASLIDAI--------GRKGDFKD-AVELLNAVGLSdaVLWLRRFKELSTGQKFRFRLALLLAERPKLLVID 161
|
170 180 190
....*....|....*....|....*....|....
gi 502612564 172 EPTGNLDRQTGDRIADLLFELNQRQATTLVMVTH 205
Cdd:COG2401 162 EFCSHLDRQTAKRVARNLQKLARRAGITLVVATH 195
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
21-178 |
1.64e-16 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 75.27 E-value: 1.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 21 NQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDeegraalRARDIGFVFQSFMLV 100
Cdd:PRK13543 22 NEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD-------RSRFMAYLGHLPGLK 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502612564 101 PTLTALENVQLPALLRGERehdSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEPTGNLD 178
Cdd:PRK13543 95 ADLSTLENLHFLCGLHGRR---AKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
36-224 |
2.85e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 77.19 E-value: 2.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 36 GQSLALIGESGSGKSTLLGILAGLDdASAGEVRLLGQPLSQLDEegrAALRaRDIGFVFQSFMLvPTLTALENVQLpall 115
Cdd:PRK11174 376 GQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDP---ESWR-KHLSWVGQNPQL-PHGTLRDNVLL---- 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 116 rgEREHDSRQRAAALLTQLGLGQRLRHLP-----------AQLSGGEQQRVALARAFSARPQILFADEPTGNLDRQTGDR 184
Cdd:PRK11174 446 --GNPDASDEQLQQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQL 523
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 502612564 185 IADLLFELNQRQatTLVMVTHDVQLAARCQRRLRLVDGTL 224
Cdd:PRK11174 524 VMQALNAASRRQ--TTLMVTHQLEDLAQWDQIWVMQDGQI 561
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
7-222 |
3.24e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 76.02 E-value: 3.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGEGenqiSILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPlsqldEEGRAALR 86
Cdd:PRK13536 42 IDLAGVSKSYGDK----AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVP-----VPARARLA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 87 ARDIGFVFQSFMLVPTLTALENVQLPALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQ 166
Cdd:PRK13536 113 RARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQ 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502612564 167 ILFADEPTGNLDRQTGDRIADLLFELNQRqATTLVMVTHDVQLAARCQRRLRLVDG 222
Cdd:PRK13536 193 LLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEA 247
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
25-226 |
4.85e-16 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 76.30 E-value: 4.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 25 ILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEgraALRaRDIGFVFQSFML----- 99
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHH---YLH-RQVALVGQEPVLfsgsv 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 100 ----VPTLTALENVQLPALLRGEREHDSRQRaaalLTQlGLGQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEPTG 175
Cdd:TIGR00958 572 reniAYGLTDTPDEEIMAAAKAANAHDFIME----FPN-GYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATS 646
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502612564 176 NLDRQtgdrIADLLFELNQRQATTLVMVTHDVQLAARCQRRLRLVDGTLRE 226
Cdd:TIGR00958 647 ALDAE----CEQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVE 693
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
7-212 |
7.40e-16 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 73.96 E-value: 7.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGEGEnqisILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDeegrAALR 86
Cdd:COG4604 2 IEIKNVSKRYGGKV----VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTP----SREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 87 ARDIGFVFQSFMLVPTLTALEnvqLPALLR----GER--EHDSRQRAAAlLTQLGLGQ-RLRHLpAQLSGGEQQRVALAR 159
Cdd:COG4604 74 AKRLAILRQENHINSRLTVRE---LVAFGRfpysKGRltAEDREIIDEA-IAYLDLEDlADRYL-DELSGGQRQRAFIAM 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502612564 160 AFSARPQILFADEPTGNLD----RQTGDRIADLLFELNQrqatTLVMVTHDVQLAAR 212
Cdd:COG4604 149 VLAQDTDYVLLDEPLNNLDmkhsVQMMKLLRRLADELGK----TVVIVLHDINFASC 201
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-206 |
2.88e-15 |
|
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: 74.20 E-value: 2.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 3 AQNVIEVHHVAKRVGEGENqisILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLlgQPlsqldeegr 82
Cdd:TIGR03719 1 AQYIYTMNRVSKVVPPKKE---ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP--QP--------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 83 aalrARDIGFVFQSFMLVPTLTALENVQ-----LPALLRgEREHDSRQRAA------ALLTQLG-------------LGQ 138
Cdd:TIGR03719 67 ----GIKVGYLPQEPQLDPTKTVRENVEegvaeIKDALD-RFNEISAKYAEpdadfdKLAAEQAelqeiidaadawdLDS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 139 RLR------HLP------AQLSGGEQQRVALARAFSARPQILFADEPTGNLDRQTGDRIADLLfelnQRQATTLVMVTHD 206
Cdd:TIGR03719 142 QLEiamdalRCPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL----QEYPGTVVAVTHD 217
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
25-209 |
2.96e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 72.45 E-value: 2.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 25 ILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVrllgqplsqldeEGRAALRardIGFVFQSFMLVPTLt 104
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------------KRNGKLR---IGYVPQKLYLDTTL- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 105 ALENVQLPALLRGEREHD-----SRQRAAALLTQlglgqrlrhlPAQ-LSGGEQQRVALARAFSARPQILFADEPTGNLD 178
Cdd:PRK09544 83 PLTVNRFLRLRPGTKKEDilpalKRVQAGHLIDA----------PMQkLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
170 180 190
....*....|....*....|....*....|.
gi 502612564 179 RQTGDRIADLLFELNQRQATTLVMVTHDVQL 209
Cdd:PRK09544 153 VNGQVALYDLIDQLRRELDCAVLMVSHDLHL 183
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
33-206 |
3.22e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 72.27 E-value: 3.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 33 VKRGQSLALIGESGSGKSTLLGILAGLDDASaGEVRLLGQPLSQLDEEGRAALRArdigFVFQSfmlVPTLTALENVQLP 112
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAGLLPGS-GSIQFAGQPLEAWSAAELARHRA----YLSQQ---QTPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 113 ALLR--GEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAF-----SARP--QILFADEPTGNLDrqtgd 183
Cdd:PRK03695 91 TLHQpdKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPagQLLLLDEPMNSLD----- 165
|
170 180
....*....|....*....|....*...
gi 502612564 184 rIA-----DLLFELNQRQATTLVMVTHD 206
Cdd:PRK03695 166 -VAqqaalDRLLSELCQQGIAVVMSSHD 192
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
25-181 |
4.02e-15 |
|
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: 71.75 E-value: 4.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 25 ILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDeegRAALRaRDIGFVFQSFMLVpTLT 104
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALAD---PAWLR-RQVGVVLQENVLF-NRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 105 ALENVQL--PALLRGEREHDSRQRAA-ALLTQL--GLGQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEPTGNLDR 179
Cdd:cd03252 92 IRDNIALadPGMSMERVIEAAKLAGAhDFISELpeGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDY 171
|
..
gi 502612564 180 QT 181
Cdd:cd03252 172 ES 173
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
25-224 |
4.82e-15 |
|
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: 71.35 E-value: 4.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 25 ILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEgraALRaRDIGFVFQSFMLVPT-- 102
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK---YLH-SKVSLVGQEPVLFARsl 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 103 -------LTALENVQLPALLRGEREHDSRQRAAaLLTQLGLGQRlrhlPAQLSGGEQQRVALARAFSARPQILFADEPTG 175
Cdd:cd03248 105 qdniaygLQSCSFECVKEAAQKAHAHSFISELA-SGYDTEVGEK----GSQLSGGQKQRVAIARALIRNPQVLILDEATS 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 502612564 176 NLDRQTGDRIADLLFELNQRQatTLVMVTHDVQLAARCQRRLRLVDGTL 224
Cdd:cd03248 180 ALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
24-205 |
5.14e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 73.38 E-value: 5.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 24 SILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLL---GQPLSQLdeegraalrARDIGFVFQSFMLV 100
Cdd:PLN03211 82 TILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILannRKPTKQI---------LKRTGFVTQDDILY 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 101 PTLTALENVQLPALLRGER---EHDSRQRAAALLTQLGLGQRLRHLPAQ-----LSGGEQQRVALARAFSARPQILFADE 172
Cdd:PLN03211 153 PHLTVRETLVFCSLLRLPKsltKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDE 232
|
170 180 190
....*....|....*....|....*....|...
gi 502612564 173 PTGNLDRQTGDRIADLLFELNQRqATTLVMVTH 205
Cdd:PLN03211 233 PTSGLDATAAYRLVLTLGSLAQK-GKTIVTSMH 264
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-178 |
5.87e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 73.14 E-value: 5.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 2 PAQNVIEVHHVAKRvgeGENQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDeeg 81
Cdd:COG3845 253 PGEVVLEVENLSVR---DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLS--- 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 82 RAALRARDIGFV---FQSFMLVPTLTALENVQL-----PALLRG--EREHDSRQRAAALLTQLGLGQRLRHLPA-QLSGG 150
Cdd:COG3845 327 PRERRRLGVAYIpedRLGRGLVPDMSVAENLILgryrrPPFSRGgfLDRKAIRAFAEELIEEFDVRTPGPDTPArSLSGG 406
|
170 180
....*....|....*....|....*...
gi 502612564 151 EQQRVALARAFSARPQILFADEPTGNLD 178
Cdd:COG3845 407 NQQKVILARELSRDPKLLIAAQPTRGLD 434
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
6-188 |
6.50e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 73.24 E-value: 6.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 6 VIEVHHVAKRVGegenQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSqlDEEGRAAL 85
Cdd:NF033858 1 VARLEGVSHRYG----KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA--DARHRRAV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 86 RARdIgfvfqSFM-------LVPTLTALENVQLPALLRGEREHDSRQRAAALLTQLGLgQRLRHLPA-QLSGGEQQRVAL 157
Cdd:NF033858 75 CPR-I-----AYMpqglgknLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGL-APFADRPAgKLSGGMKQKLGL 147
|
170 180 190
....*....|....*....|....*....|....*
gi 502612564 158 ARAFSARPQILFADEPTGNLD----RQTGDRIADL 188
Cdd:NF033858 148 CCALIHDPDLLILDEPTTGVDplsrRQFWELIDRI 182
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
26-205 |
6.75e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 72.90 E-value: 6.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 26 LTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDAS--AGEVRLLGQPlsqldeegraaLRARDI------GFVF--Q 95
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDGEV-----------CRFKDIrdsealGIVIihQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 96 SFMLVPTLTALENVqlpaLLRGERE-------HDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQIL 168
Cdd:NF040905 86 ELALIPYLSIAENI----FLGNERAkrgvidwNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLL 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 502612564 169 FADEPTGNLDRQTGDRIADLLFELnQRQATTLVMVTH 205
Cdd:NF040905 162 ILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISH 197
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
7-205 |
2.20e-14 |
|
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: 69.09 E-value: 2.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGEGEnqisILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDD--ASAGEVRLLGQPLSQLDEEGRAA 84
Cdd:cd03217 1 LEIKDLHVSVGGKE----ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLPPEERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 85 LrarDIGFVFQSFMLVPTLTalenvqlpallrgerehdsrqraaalltqlgLGQRLRHLPAQLSGGEQQRVALARAFSAR 164
Cdd:cd03217 77 L---GIFLAFQYPPEIPGVK-------------------------------NADFLRYVNEGFSGGEKKRNEILQLLLLE 122
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 502612564 165 PQILFADEPTGNLDRQTGDRIADLLFELNqRQATTLVMVTH 205
Cdd:cd03217 123 PDLAILDEPDSGLDIDALRLVAEVINKLR-EEGKSVLIITH 162
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
11-224 |
4.73e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 69.47 E-value: 4.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 11 HVAKRVGegenqiSILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASA--------GEVRLLGQPLSQLDEEGR 82
Cdd:PRK13547 8 HVARRHR------AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtGDVTLNGEPLAAIDAPRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 83 AALRA-----RDIGFVFQSFMLVptltaLENVQLPALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVAL 157
Cdd:PRK13547 82 ARLRAvlpqaAQPAFAFSAREIV-----LLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQF 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502612564 158 ARAFS---------ARPQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAARCQRRL-RLVDGTL 224
Cdd:PRK13547 157 ARVLAqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIaMLADGAI 233
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
29-226 |
7.80e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 70.00 E-value: 7.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 29 VDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPlsqLDEEGRAALRARdIGFVFQSFMLvptltalen 108
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKP---VTAEQPEDYRKL-FSAVFTDFHL--------- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 109 vqLPALLRGEREHDSRQRAAALLTQLGLGQRLRH-----LPAQLSGGEQQRVALARAFSARPQILFADEPTGNLDRQTGD 183
Cdd:PRK10522 409 --FDQLLGPEGKPANPALVEKWLERLKMAHKLELedgriSNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRR 486
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 502612564 184 RIADLLFELNQRQATTLVMVTHDVQLAARCQRRLRLVDGTLRE 226
Cdd:PRK10522 487 EFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
14-216 |
1.06e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 67.98 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 14 KRVGEGENQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEegrAALRARDIGFV 93
Cdd:PRK11614 9 DKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQT---AKIMREAVAIV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 94 FQSFMLVPTLTALENVQLPALLRGEREHDSR-QRAAALLTQlgLGQRLRHLPAQLSGGEQQRVALARAFSARPQILFADE 172
Cdd:PRK11614 86 PEGRRVFSRMTVEENLAMGGFFAERDQFQERiKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 502612564 173 PTGNLDRQTGDRIADLLFELNQrQATTLVMVTHDVQLAARCQRR 216
Cdd:PRK11614 164 PSLGLAPIIIQQIFDTIEQLRE-QGMTIFLVEQNANQALKLADR 206
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
19-212 |
2.62e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 67.32 E-value: 2.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 19 GENQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEGRAalraRDIGFVFQSFM 98
Cdd:PRK10253 16 GYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA----RRIGLLAQNAT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 99 LVPTLTALENVQlpallRGEREHDS-----RQRAAALLTQLGLGQRLRHLPAQ----LSGGEQQRVALARAFSARPQILF 169
Cdd:PRK10253 92 TPGDITVQELVA-----RGRYPHQPlftrwRKEDEEAVTKAMQATGITHLADQsvdtLSGGQRQRAWIAMVLAQETAIML 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 502612564 170 ADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAAR 212
Cdd:PRK10253 167 LDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACR 209
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-206 |
3.28e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 67.84 E-value: 3.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 1 MPAQNVIEVHHVAKRVGEGENqisILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLlgqplsqldEE 80
Cdd:PRK11819 1 MMAQYIYTMNRVSKVVPPKKQ---ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARP---------AP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 81 GRAalrardIGFVFQSFMLVPTLTALENVQ-----LPALLR---------GEREHDSRQ---RAAALLTQL------GLG 137
Cdd:PRK11819 69 GIK------VGYLPQEPQLDPEKTVRENVEegvaeVKAALDrfneiyaayAEPDADFDAlaaEQGELQEIIdaadawDLD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 138 QRLR------HLP------AQLSGGEQQRVALARAFSARPQILFADEPTGNLDRQTgdrIADLLFELnQRQATTLVMVTH 205
Cdd:PRK11819 143 SQLEiamdalRCPpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES---VAWLEQFL-HDYPGTVVAVTH 218
|
.
gi 502612564 206 D 206
Cdd:PRK11819 219 D 219
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
29-178 |
5.77e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 66.07 E-value: 5.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 29 VDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEGRAAlraRDIGFVFQSFMLVPTLTALEN 108
Cdd:PRK10895 22 VSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARAR---RGIGYLPQEASIFRRLSVYDN 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502612564 109 VQLPALLRGEREHDSRQ-RAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEPTGNLD 178
Cdd:PRK10895 99 LMAVLQIRDDLSAEQREdRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
12-178 |
1.00e-12 |
|
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: 64.59 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 12 VAKRVGEGENQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASA---GEVRLLGQPLSQLDEEGRaalraR 88
Cdd:cd03233 9 ISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKEFAEKYP-----G 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 89 DIGFVFQSFMLVPTLTALENVQLPALLRGerehdsrqraaalltqlglGQRLRhlpaQLSGGEQQRVALARAFSARPQIL 168
Cdd:cd03233 84 EIIYVSEEDVHFPTLTVRETLDFALRCKG-------------------NEFVR----GISGGERKRVSIAEALVSRASVL 140
|
170
....*....|
gi 502612564 169 FADEPTGNLD 178
Cdd:cd03233 141 CWDNSTRGLD 150
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
23-223 |
1.15e-12 |
|
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: 64.66 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 23 ISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGqplSQLDEEGRAALRARDIGFVFQSfmlvpt 102
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSN---KNESEPSFEATRSRNRYSVAYA------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 103 ltalenVQLPALLRGEREHD-------SRQRAAALLTQLGLGQRLRHLP-----------AQLSGGEQQRVALARAFSAR 164
Cdd:cd03290 85 ------AQKPWLLNATVEENitfgspfNKQRYKAVTDACSLQPDIDLLPfgdqteigergINLSGGQRQRICVARALYQN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 165 PQILFADEPTGNLDRQTGDRI-ADLLFELNQRQATTLVMVTHDVQLAARCQRRLRLVDGT 223
Cdd:cd03290 159 TNIVFLDDPFSALDIHLSDHLmQEGILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-228 |
1.26e-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: 64.36 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 2 PAQNVIEVHHVAKRVGEgeNQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEg 81
Cdd:cd03369 2 PEHGEIEVENLSVRYAP--DLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 82 raALRardigfvfQSFMLVPtltalenvQLPALLRG--------EREHDSRQRAAAL-LTQLGLgqrlrhlpaQLSGGEQ 152
Cdd:cd03369 79 --DLR--------SSLTIIP--------QDPTLFSGtirsnldpFDEYSDEEIYGALrVSEGGL---------NLSQGQR 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502612564 153 QRVALARAFSARPQILFADEPTGNLDRQTGDRIADLLFELNQRqaTTLVMVTHDVQLAARCQRRLRLVDGTLREVA 228
Cdd:cd03369 132 QLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFTN--STILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
25-192 |
1.99e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 65.90 E-value: 1.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 25 ILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDAS--AGEVRLLGQPlsqldeeGRAALRARDIGFVFQSFMLVPT 102
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTGviTGGDRLVNGR-------PLDSSFQRSIGYVQQQDLHLPT 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 103 LTALENVQLPALLR-----GEREHDS-----------RQRAAALLTQLGLGqrlrhlpaqLSGGEQQRVALARAFSARPQ 166
Cdd:TIGR00956 851 STVRESLRFSAYLRqpksvSKSEKMEyveevikllemESYADAVVGVPGEG---------LNVEQRKRLTIGVELVAKPK 921
|
170 180
....*....|....*....|....*..
gi 502612564 167 -ILFADEPTGNLDRQTGDRIADLLFEL 192
Cdd:TIGR00956 922 lLLFLDEPTSGLDSQTAWSICKLMRKL 948
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
25-224 |
2.25e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 65.96 E-value: 2.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 25 ILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVrllgqplsqldeegraaLRARDIGFVFQSFMLVpTLT 104
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-----------------WAERSIAYVPQQAWIM-NAT 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 105 ALENVQLPALLRGER----------EHDSRQRAAALLTQLGlgqrlrHLPAQLSGGEQQRVALARAFSARPQILFADEPT 174
Cdd:PTZ00243 737 VRGNILFFDEEDAARladavrvsqlEADLAQLGGGLETEIG------EKGVNLSGGQKARVSLARAVYANRDVYLLDDPL 810
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 502612564 175 GNLDRQTGDRIADLLFeLNQRQATTLVMVTHDVQLAARCQRRLRLVDGTL 224
Cdd:PTZ00243 811 SALDAHVGERVVEECF-LGALAGKTRVLATHQVHVVPRADYVVALGDGRV 859
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
14-225 |
1.28e-11 |
|
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: 63.88 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 14 KRVGEGENQISILT--------------AVDLV---VKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQP-LS 75
Cdd:TIGR01257 1926 QRIISGGNKTDILRlneltkvysgtsspAVDRLcvgVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiLT 2005
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 76 QLDEEgraalrARDIGFVFQSFMLVPTLTALENVQLPALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRV 155
Cdd:TIGR01257 2006 NISDV------HQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKL 2079
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502612564 156 ALARAFSARPQILFADEPTGNLDRQTGDRIADLLFELnQRQATTLVMVTHDV-QLAARCQRRLRLVDGTLR 225
Cdd:TIGR01257 2080 STAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSI-IREGRAVVLTSHSMeECEALCTRLAIMVKGAFQ 2149
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
29-227 |
1.46e-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: 63.28 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 29 VDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPlsqLDEEGRAALRARdIGFVFQSFMLVPTLTALEN 108
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQP---VTADNREAYRQL-FSAVFSDFHLFDRLLGLDG 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 109 VQLPAllrgerehdsrqRAAALLTQLGLGQRLRH-----LPAQLSGGEQQRVALARAF-SARPQILFaDEPTgnldrqtg 182
Cdd:COG4615 427 EADPA------------RARELLERLELDHKVSVedgrfSTTDLSQGQRKRLALLVALlEDRPILVF-DEWA-------- 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502612564 183 driAD------------LLFELnQRQATTLVMVTHDVQLAARCQRRLRLVDGTLREV 227
Cdd:COG4615 486 ---ADqdpefrrvfyteLLPEL-KARGKTVIAISHDDRYFDLADRVLKMDYGKLVEL 538
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
25-209 |
2.08e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 61.95 E-value: 2.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 25 ILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSqLDEEGRAALRaRDIGFVFQSFMLVPTLT 104
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD-YSKRGLLALR-QQVATVFQDPEQQIFYT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 105 ALENvQLPALLR--GEREHDSRQRAAALLTqLGLGQRLRHLPAQ-LSGGEQQRVALARAFSARPQILFADEPTGNLDRQT 181
Cdd:PRK13638 94 DIDS-DIAFSLRnlGVPEAEITRRVDEALT-LVDAQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAG 171
|
170 180
....*....|....*....|....*...
gi 502612564 182 GDRIADLLFELNQrQATTLVMVTHDVQL 209
Cdd:PRK13638 172 RTQMIAIIRRIVA-QGNHVIISSHDIDL 198
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
41-206 |
2.66e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 62.22 E-value: 2.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 41 LIGESGSGKSTLLGILAGLDDASAGEVRL-----LGQpLSQlDEegraalrardigFVFQSFMLVPTL----TALENVQ- 110
Cdd:PRK15064 32 LIGANGCGKSTFMKILGGDLEPSAGNVSLdpnerLGK-LRQ-DQ------------FAFEEFTVLDTVimghTELWEVKq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 111 -------LP----------ALLRGE-REHD---SRQRAAALLTQLGLGQRLRHLP-AQLSGGEQQRVALARAFSARPQIL 168
Cdd:PRK15064 98 erdriyaLPemseedgmkvADLEVKfAEMDgytAEARAGELLLGVGIPEEQHYGLmSEVAPGWKLRVLLAQALFSNPDIL 177
|
170 180 190
....*....|....*....|....*....|....*...
gi 502612564 169 FADEPTGNLDRQTgdrIADLLFELNQRQAtTLVMVTHD 206
Cdd:PRK15064 178 LLDEPTNNLDINT---IRWLEDVLNERNS-TMIIISHD 211
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
6-227 |
9.80e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 60.57 E-value: 9.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 6 VIEVHHVAKRVGEGENQISiltavdLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQ---PLSQLD--EE 80
Cdd:PRK09700 265 VFEVRNVTSRDRKKVRDIS------FSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdisPRSPLDavKK 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 81 GRAALRA--RDIGFvFQSFML---VPTLTALENVQLPALL-----RGEREHDSRQRAAALLTQLGLGQRLrhlpAQLSGG 150
Cdd:PRK09700 339 GMAYITEsrRDNGF-FPNFSIaqnMAISRSLKDGGYKGAMglfheVDEQRTAENQRELLALKCHSVNQNI----TELSGG 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502612564 151 EQQRVALARAFSARPQILFADEPTGNLDRQTGDRIADLLFELNQrQATTLVMVTHDV-QLAARCQRRLRLVDGTLREV 227
Cdd:PRK09700 414 NQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAD-DGKVILMVSSELpEIITVCDRIAVFCEGRLTQI 490
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
14-178 |
1.24e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 60.63 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 14 KRVGEGENQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDAS--AGEVRLLGQPLSQldeegraALRARDIG 91
Cdd:PLN03140 884 KEQGVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFPKKQ-------ETFARISG 956
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 92 FVFQSFMLVPTLTALENVQLPALLRGEREHDSRQR------AAALLTQLGLGQRLRHLPA--QLSGGEQQRVALARAFSA 163
Cdd:PLN03140 957 YCEQNDIHSPQVTVRESLIYSAFLRLPKEVSKEEKmmfvdeVMELVELDNLKDAIVGLPGvtGLSTEQRKRLTIAVELVA 1036
|
170
....*....|....*
gi 502612564 164 RPQILFADEPTGNLD 178
Cdd:PLN03140 1037 NPSIIFMDEPTSGLD 1051
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
29-203 |
2.94e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 59.17 E-value: 2.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 29 VDLVVKRGQSLALIGESGSGK----STLLGILAGlddASAGEVRLLGQPLSQldeegRAALRARDIGFVF-----QSFML 99
Cdd:PRK13549 281 VSFSLRRGEILGIAGLVGAGRtelvQCLFGAYPG---RWEGEIFIDGKPVKI-----RNPQQAIAQGIAMvpedrKRDGI 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 100 VPTLTALENVQLPALLRgeREHDSRQRAAALLTQLGLG-QRLR------HLP-AQLSGGEQQRVALARAFSARPQILFAD 171
Cdd:PRK13549 353 VPVMGVGKNITLAALDR--FTGGSRIDDAAELKTILESiQRLKvktaspELAiARLSGGNQQKAVLAKCLLLNPKILILD 430
|
170 180 190
....*....|....*....|....*....|..
gi 502612564 172 EPTGNLDRQTGDRIADLLFELNQrQATTLVMV 203
Cdd:PRK13549 431 EPTRGIDVGAKYEIYKLINQLVQ-QGVAIIVI 461
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
26-177 |
3.14e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 59.36 E-value: 3.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 26 LTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQldEEGRAALRArDIGFVFQSFMLVPTLTA 105
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDF--KSSKEALEN-GISMVHQELNLVLQRSV 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502612564 106 LENVQL---PalLRGE-REHDSRQR-AAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEPTGNL 177
Cdd:PRK10982 91 MDNMWLgryP--TKGMfVDQDKMYRdTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
3-221 |
3.35e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 58.98 E-value: 3.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 3 AQNVIEVHHVAKRVGEgenqISILTAVDLVVKRGQSLALIGESGSG--KSTLLGILAGlDDASAGEVRLLGQPLSqldee 80
Cdd:NF000106 10 ARNAVEVRGLVKHFGE----VKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G-PDAGRRPWRF*TWCAN----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 81 gRAALRaRDIGF-------VFQSFmlvptlTALENVQLPALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQ 153
Cdd:NF000106 80 -RRALR-RTIG*hrpvr*gRRESF------SGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502612564 154 RVALARAFSARPQILFADEPTGNLDRQTGDRIADLLFELnQRQATTLVMVTHDVQLAARCQRRLRLVD 221
Cdd:NF000106 152 RLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSM-VRDGATVLLTTQYMEEAEQLAHELTVID 218
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
20-205 |
6.10e-10 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 58.57 E-value: 6.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 20 ENQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEgraALRARdIGFVFQSFML 99
Cdd:PRK10789 325 QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLD---SWRSR-LAVVSQTPFL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 100 VPTLTAlENVqlpALLRGEREHDSRQRAAALLT------------QLGLGQRlrhlPAQLSGGEQQRVALARAFSARPQI 167
Cdd:PRK10789 401 FSDTVA-NNI---ALGRPDATQQEIEHVARLASvhddilrlpqgyDTEVGER----GVMLSGGQKQRISIARALLLNAEI 472
|
170 180 190
....*....|....*....|....*....|....*....
gi 502612564 168 LFADEPTGNLDRQTGDRIadlLFELNQ-RQATTLVMVTH 205
Cdd:PRK10789 473 LILDDALSAVDGRTEHQI---LHNLRQwGEGRTVIISAH 508
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-222 |
7.95e-10 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 57.03 E-value: 7.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 33 VKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLS------QLDEEG--RAALRARDIGFVFQSFMLVPTLT 104
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpqyiKADYEGtvRDLLSSITKDFYTHPYFKTEIAK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 105 ALenvQLPALLrgEREhdsrqraaalltqlglgqrlrhLPaQLSGGEQQRVALARAFSARPQILFADEPTGNLDRQTGDR 184
Cdd:cd03237 102 PL---QIEQIL--DRE----------------------VP-ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLM 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 502612564 185 IADLL--FELNQrQATTLVmVTHDVQLAARCQRRLRLVDG 222
Cdd:cd03237 154 ASKVIrrFAENN-EKTAFV-VEHDIIMIDYLADRLIVFEG 191
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
26-201 |
8.05e-10 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 58.11 E-value: 8.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 26 LTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQplsQLDEEGRAALRaRDIGFVFQSFMLVPTLTA 105
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGH---DLRDYTLASLR-NQVALVSQNVHLFNDTIA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 106 lENVQLPALLRGEREhdSRQRAAALLTQLGLGQRLRHL--------PAQLSGGEQQRVALARAFSARPQILFADEPTGNL 177
Cdd:PRK11176 435 -NNIAYARTEQYSRE--QIEEAARMAYAMDFINKMDNGldtvigenGVLLSGGQRQRIAIARALLRDSPILILDEATSAL 511
|
170 180
....*....|....*....|....
gi 502612564 178 DRQTGDRIADLLFELnQRQATTLV 201
Cdd:PRK11176 512 DTESERAIQAALDEL-QKNRTSLV 534
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
29-206 |
8.14e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 58.00 E-value: 8.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 29 VDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQldEEGRAALRArdiGFVF-----QSFMLVPTL 103
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDI--RSPRDAIRA---GIMLcpedrKAEGIIPVH 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 104 TALENVQLPA---------LLRGEREhdsRQRAAALLTQLGLGQRLRHLP-AQLSGGEQQRVALARAFSARPQILFADEP 173
Cdd:PRK11288 347 SVADNINISArrhhlragcLINNRWE---AENADRFIRSLNIKTPSREQLiMNLSGGNQQKAILGRWLSEDMKVILLDEP 423
|
170 180 190
....*....|....*....|....*....|...
gi 502612564 174 TGNLDRQTGDRIADLLFELNQrQATTLVMVTHD 206
Cdd:PRK11288 424 TRGIDVGAKHEIYNVIYELAA-QGVAVLFVSSD 455
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-178 |
1.01e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 57.71 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 2 PAQNVIEVHHVAkrvGEGENQISiltavdLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLD-EE 80
Cdd:PRK10762 253 PGEVRLKVDNLS---GPGVNDVS------FTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSpQD 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 81 GRAAlrardiGFVFQSF-----MLVPTLTALENVQLPAL-----LRGEREHDSRQRAAALLTQL------GLGQRLRhlp 144
Cdd:PRK10762 324 GLAN------GIVYISEdrkrdGLVLGMSVKENMSLTALryfsrAGGSLKHADEQQAVSDFIRLfniktpSMEQAIG--- 394
|
170 180 190
....*....|....*....|....*....|....
gi 502612564 145 aQLSGGEQQRVALARAFSARPQILFADEPTGNLD 178
Cdd:PRK10762 395 -LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-206 |
1.58e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.13 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 32 VVKRGQSLALIGESGSGKSTLLGILAGL---------DDASAGEV------RLLGQPLSQL-DEEGRAALRARDIGfvfq 95
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGElipnlgdyeEEPSWDEVlkrfrgTELQNYFKKLyNGEIKVVHKPQYVD---- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 96 sfmlvptltalenvQLPALLRGE-----REHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQILFA 170
Cdd:PRK13409 171 --------------LIPKVFKGKvrellKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190
....*....|....*....|....*....|....*....
gi 502612564 171 DEPTGNLD-RQtgdRI--ADLLFELNQRQAttLVMVTHD 206
Cdd:PRK13409 237 DEPTSYLDiRQ---RLnvARLIRELAEGKY--VLVVEHD 270
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-206 |
1.65e-09 |
|
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: 56.22 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 32 VVKRGQSLALIGESGSGKSTLLGILAGlddasagEVrllgQP-LSQLDEEGR-----AALRARDIGFVFQSfMLVPTLTA 105
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAG-------KL----KPnLGKFDDPPDwdeilDEFRGSELQNYFTK-LLEGDVKV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 106 LENVQ----LPALLRGE-----REHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEPTGN 176
Cdd:cd03236 90 IVKPQyvdlIPKAVKGKvgellKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSY 169
|
170 180 190
....*....|....*....|....*....|
gi 502612564 177 LDRQTGDRIADLLFELNQRQATTLVmVTHD 206
Cdd:cd03236 170 LDIKQRLNAARLIRELAEDDNYVLV-VEHD 198
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
26-227 |
2.33e-09 |
|
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: 56.88 E-value: 2.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 26 LTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQplsqldeegraalrardIGFVFQSfMLVPTLTA 105
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-----------------VAYVPQQ-AWIQNDSL 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 106 LENVQLPALLRgEREHDSRQRAAALLTQLGL---GQR--LRHLPAQLSGGEQQRVALARAFSARPQILFADEPTGNLDRQ 180
Cdd:TIGR00957 716 RENILFGKALN-EKYYQQVLEACALLPDLEIlpsGDRteIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH 794
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502612564 181 TGDRIAD-LLFELNQRQATTLVMVTHDVQLAARCQRRLRLVDGTLREV 227
Cdd:TIGR00957 795 VGKHIFEhVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEM 842
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-206 |
3.15e-09 |
|
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: 56.10 E-value: 3.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 5 NVIEVHHVAKRVGEGenqiSILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLlGQPLsqldeegraa 84
Cdd:TIGR03719 321 KVIEAENLTKAFGDK----LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV---------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 85 lrarDIGFVFQSF-MLVPTLTALENVQ--LPALLRGEREHDSRqraaALLTQLGL-GQRLRHLPAQLSGGEQQRVALARA 160
Cdd:TIGR03719 386 ----KLAYVDQSRdALDPNKTVWEEISggLDIIKLGKREIPSR----AYVGRFNFkGSDQQKKVGQLSGGERNRVHLAKT 457
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 502612564 161 FSARPQILFADEPTGNLDRQTGDRIADLLFELnqrqATTLVMVTHD 206
Cdd:TIGR03719 458 LKSGGNVLLLDEPTNDLDVETLRALEEALLNF----AGCAVVISHD 499
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
9-212 |
4.46e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 55.83 E-value: 4.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 9 VHHVAKRVGEGENQISiltavdLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEGRAALrar 88
Cdd:PRK15439 268 VLTVEDLTGEGFRNIS------LEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLAR--- 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 89 diGFVF-----QS---FMLVP---TLTALENVQLPALLRGEREHD--SRQRAAalltqlgLGQRLRHL--PAQ-LSGGEQ 152
Cdd:PRK15439 339 --GLVYlpedrQSsglYLDAPlawNVCALTHNRRGFWIKPARENAvlERYRRA-------LNIKFNHAeqAARtLSGGNQ 409
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502612564 153 QRVALARAFSARPQILFADEPTGNLDRQTGDRIADLLFELNQrQATTLVMVTHD----VQLAAR 212
Cdd:PRK15439 410 QKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAA-QNVAVLFISSDleeiEQMADR 472
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
30-206 |
5.09e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 55.73 E-value: 5.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 30 DLVVKRGQSLALIGESGSGKSTLLGILAG---LDDasaGEV---------RLLGQPLSqlDEEGRA----ALRARDIGFV 93
Cdd:PRK11147 23 ELHIEDNERVCLVGRNGAGKSTLMKILNGevlLDD---GRIiyeqdlivaRLQQDPPR--NVEGTVydfvAEGIEEQAEY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 94 FQSFMLVPTLTALE----NVQLPALLRGEREH------DSRqrAAALLTQLGLG--QRLrhlpAQLSGGEQQRVALARAF 161
Cdd:PRK11147 98 LKRYHDISHLVETDpsekNLNELAKLQEQLDHhnlwqlENR--INEVLAQLGLDpdAAL----SSLSGGWLRKAALGRAL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 502612564 162 SARPQILFADEPTGNLDRQTGDRIADLLFELNqrqaTTLVMVTHD 206
Cdd:PRK11147 172 VSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQ----GSIIFISHD 212
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
15-226 |
5.28e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 55.67 E-value: 5.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 15 RVGEGENQISiLTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVrllgqplsqlDEEGRAALRARDIGFVF 94
Cdd:PRK13545 30 RSKDGEYHYA-LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV----------DIKGSAALIAISSGLNG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 95 QsfmlvptLTALENVQLPALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEPT 174
Cdd:PRK13545 99 Q-------LTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEAL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502612564 175 GNLDRQTGDRIADLLFELNQrQATTLVMVTHDV-QLAARCQRRLRLVDGTLRE 226
Cdd:PRK13545 172 SVGDQTFTKKCLDKMNEFKE-QGKTIFFISHSLsQVKSFCTKALWLHYGQVKE 223
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
30-203 |
5.33e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.41 E-value: 5.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 30 DLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGE--------VRLLGQPLSQLDEEgraalrardigfVFQ---SFM 98
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGErqsqfshiTRLSFEQLQKLVSD------------EWQrnnTDM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 99 LVPT-----LTALENVQLpallrgerEHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEP 173
Cdd:PRK10938 91 LSPGeddtgRTTAEIIQD--------EVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEP 162
|
170 180 190
....*....|....*....|....*....|
gi 502612564 174 TGNLDRQTGDRIADLLFELNQrQATTLVMV 203
Cdd:PRK10938 163 FDGLDVASRQQLAELLASLHQ-SGITLVLV 191
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
29-204 |
9.43e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 54.83 E-value: 9.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 29 VDLVVKRGQSLALIGESGSGKSTLLGILAGL-DDASAGEVRLLGQPLSQldeegRAALRARDIGFVF-----QSFMLVPT 102
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDI-----RNPAQAIRAGIAMvpedrKRHGIVPI 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 103 LTALENVQLPALLRGEREhdSRQRAAALLTQLGLG-QRLR------HLP-AQLSGGEQQRVALARAFSARPQILFADEPT 174
Cdd:TIGR02633 354 LGVGKNITLSVLKSFCFK--MRIDAAAELQIIGSAiQRLKvktaspFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPT 431
|
170 180 190
....*....|....*....|....*....|
gi 502612564 175 GNLDRQTGDRIADLLFELNQrQATTLVMVT 204
Cdd:TIGR02633 432 RGVDVGAKYEIYKLINQLAQ-EGVAIIVVS 460
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-206 |
1.17e-08 |
|
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: 54.41 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 32 VVKRGQSLALIGESGSGKSTLLGILAGL---------DDASAGEV------RLLGQPLSQL-DEEGRAALRARDIGFVFQ 95
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGElkpnlgdydEEPSWDEVlkrfrgTELQDYFKKLaNGEIKVAHKPQYVDLIPK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 96 SFML-VPTLtaLENVqlpallrgerehDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEPT 174
Cdd:COG1245 175 VFKGtVREL--LEKV------------DERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPS 240
|
170 180 190
....*....|....*....|....*....|....*
gi 502612564 175 GNLD-RQtgdRI--ADLLFELNQRQATTLVmVTHD 206
Cdd:COG1245 241 SYLDiYQ---RLnvARLIRELAEEGKYVLV-VEHD 271
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
25-181 |
1.73e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 54.34 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 25 ILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASA----GEVRLLGQPLSQLDEEGRAalrarDIGFVFQSFMLV 100
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHigveGVITYDGITPEEIKKHYRG-----DVVYNAETDVHF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 101 PTLTALENVQLPALLRG--------EREHDSRQRAAALLTQLGLgqrlRH---------LPAQLSGGEQQRVALARAFSA 163
Cdd:TIGR00956 151 PHLTVGETLDFAARCKTpqnrpdgvSREEYAKHIADVYMATYGL----SHtrntkvgndFVRGVSGGERKRVSIAEASLG 226
|
170
....*....|....*...
gi 502612564 164 RPQILFADEPTGNLDRQT 181
Cdd:TIGR00956 227 GAKIQCWDNATRGLDSAT 244
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
146-212 |
2.21e-08 |
|
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: 51.59 E-value: 2.21e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502612564 146 QLSGGEQQRVALARAFS----ARPQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVmVTHDVQLAAR 212
Cdd:cd03227 77 QLSGGEKELSALALILAlaslKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIV-ITHLPELAEL 146
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
33-208 |
2.45e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.80 E-value: 2.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 33 VKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLlGQPL--SQLDEEgRAALRardigfvfqsfmlvPTLTALENVq 110
Cdd:PRK11147 342 VQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLevAYFDQH-RAELD--------------PEKTVMDNL- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 111 lpALLRGEREHDSRQRAAalltqLGLGQ-------RLRHLPAQLSGGEQQRVALARAFSARPQILFADEPTGNLDRQTgd 183
Cdd:PRK11147 405 --AEGKQEVMVNGRPRHV-----LGYLQdflfhpkRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVET-- 475
|
170 180
....*....|....*....|....*
gi 502612564 184 riADLLFELNQRQATTLVMVTHDVQ 208
Cdd:PRK11147 476 --LELLEELLDSYQGTVLLVSHDRQ 498
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
25-178 |
4.75e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 52.10 E-value: 4.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 25 ILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDD--ASAGEVRLLGQPLSQLDEEGRAalrARDIGFVFQSFMLVPT 102
Cdd:PRK09580 16 ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGTVEFKGKDLLELSPEDRA---GEGIFMAFQYPVEIPG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 103 L-------TALENV----QLPALLRGEREHDSRQRAAALLTQLGLGQrlRHLPAQLSGGEQQRVALARAFSARPQILFAD 171
Cdd:PRK09580 93 VsnqfflqTALNAVrsyrGQEPLDRFDFQDLMEEKIALLKMPEDLLT--RSVNVGFSGGEKKRNDILQMAVLEPELCILD 170
|
....*..
gi 502612564 172 EPTGNLD 178
Cdd:PRK09580 171 ESDSGLD 177
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
36-206 |
6.97e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.48 E-value: 6.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 36 GQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQ-PLSQLDEEgRAALRARDIGFVFQSfmlvptltALENVQLPAL 114
Cdd:PRK10636 27 GQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwQLAWVNQE-TPALPQPALEYVIDG--------DREYRQLEAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 115 LRGEREHDS-------------------RQRAAALLTQLGLGQ-RLRHLPAQLSGGEQQRVALARAFSARPQILFADEPT 174
Cdd:PRK10636 98 LHDANERNDghaiatihgkldaidawtiRSRAASLLHGLGFSNeQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPT 177
|
170 180 190
....*....|....*....|....*....|..
gi 502612564 175 GNLDRqtgDRIADLLFELNQRQAtTLVMVTHD 206
Cdd:PRK10636 178 NHLDL---DAVIWLEKWLKSYQG-TLILISHD 205
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
25-205 |
8.62e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 50.72 E-value: 8.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 25 ILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLsqldEEGRAALRaRDIGFVFQSFMLVPTLT 104
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCTYQ-KQLCFVGHRSGINPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 105 ALENVqlpalLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEPTGNLDRQTGDR 184
Cdd:PRK13540 91 LRENC-----LYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLT 165
|
170 180
....*....|....*....|.
gi 502612564 185 IADLLfELNQRQATTLVMVTH 205
Cdd:PRK13540 166 IITKI-QEHRAKGGAVLLTSH 185
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
26-226 |
8.96e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 52.29 E-value: 8.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 26 LTAVDLVVKRGQSLALIGESGSGKSTLlgILAGLDDASAGEVrllgqplSQLDEEGRAALrARDIGFVFQSfmlvptlTA 105
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSL--ISAMLGELSHAET-------SSVVIRGSVAY-VPQVSWIFNA-------TV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 106 LENVQLPALLRGER----------EHDSRQRAAALLTQLGlgQRlrhlPAQLSGGEQQRVALARAFSARPQILFADEPTG 175
Cdd:PLN03232 696 RENILFGSDFESERywraidvtalQHDLDLLPGRDLTEIG--ER----GVNISGGQKQRVSMARAVYSNSDIYIFDDPLS 769
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502612564 176 NLDRQTGDRIADLLFElNQRQATTLVMVTHDVQLAARCQRRLRLVDGTLRE 226
Cdd:PLN03232 770 ALDAHVAHQVFDSCMK-DELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKE 819
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-226 |
9.20e-08 |
|
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: 52.22 E-value: 9.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 2 PAQNVIEVHHVAKRVGEGENqiSILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLdDASAGEVRLLGQPLSQLD-EE 80
Cdd:TIGR01271 1213 PSGGQMDVQGLTAKYTEAGR--AVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVSWNSVTlQT 1289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 81 GRAALrardiGFVFQSfMLVPTLTALENVQlpallrgEREHDSRQRAAALLTQLGLGQRLRHLPAQ-----------LSG 149
Cdd:TIGR01271 1290 WRKAF-----GVIPQK-VFIFSGTFRKNLD-------PYEQWSDEEIWKVAEEVGLKSVIEQFPDKldfvlvdggyvLSN 1356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 150 GEQQRVALARAFSARPQILFADEPTGNLDRQTGDRIADLLfelnqRQA---TTLVMVTHDVQLAARCQRRLRLVDGTLRE 226
Cdd:TIGR01271 1357 GHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTL-----KQSfsnCTVILSEHRVEALLECQQFLVIEGSSVKQ 1431
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
144-212 |
1.18e-07 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 50.30 E-value: 1.18e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502612564 144 PAQLSGGEQQ------RVALARAFSARPQILFADEPTGNLDRQTGD-RIADLLFELNQRQATTLVMVTHDVQLAAR 212
Cdd:cd03240 113 RGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEeSLAEIIEERKSQKNFQLIVITHDEELVDA 188
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
5-205 |
1.47e-07 |
|
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: 51.29 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 5 NVIEVHHVAKRVGEGENQISILTavdLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGevrLLGQP-------LSQL 77
Cdd:TIGR00954 450 NGIKFENIPLVTPNGDVLIESLS---FEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGG---RLTKPakgklfyVPQR 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 78 DEEGRAALRARDI--GFVFQSFM-------LVptlTALENVQLPALLRGEREHDSRQRAAALLtqlglgqrlrhlpaqlS 148
Cdd:TIGR00954 524 PYMTLGTLRDQIIypDSSEDMKRrglsdkdLE---QILDNVQLTHILEREGGWSAVQDWMDVL----------------S 584
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502612564 149 GGEQQRVALARAFSARPQILFADEPTGNLDRQTGDRIadllFELNQRQATTLVMVTH 205
Cdd:TIGR00954 585 GGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYM----YRLCREFGITLFSVSH 637
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
147-215 |
1.85e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.18 E-value: 1.85e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502612564 147 LSGGEQQRVALARAFSARPQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAARCQR 215
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDK 1427
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
25-187 |
2.07e-07 |
|
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: 50.24 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 25 ILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRllgqplsqldEEGRaalrardIGFVFQSFMLVPTlT 104
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK----------HSGR-------ISFSSQFSWIMPG-T 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 105 ALENVqlpalLRGEREHDSRQRAAALLTQlgLGQRLRHLPAQ-----------LSGGEQQRVALARAFSARPQILFADEP 173
Cdd:cd03291 114 IKENI-----IFGVSYDEYRYKSVVKACQ--LEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSP 186
|
170
....*....|....
gi 502612564 174 TGNLDRQTGDRIAD 187
Cdd:cd03291 187 FGYLDVFTEKEIFE 200
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
14-209 |
2.62e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.55 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 14 KRVGEGENQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLL-GQPLSQLDEEGRAALRARDigf 92
Cdd:PRK10636 316 EKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAkGIKLGYFAQHQLEFLRADE--- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 93 vfqsfmlvptlTALENVQLPAllrgerEHDSRQRAAALLTQLGL-GQRLRHLPAQLSGGEQQRVALARAFSARPQILFAD 171
Cdd:PRK10636 393 -----------SPLQHLARLA------PQELEQKLRDYLGGFGFqGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLD 455
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 502612564 172 EPTGNLDrqtgdriadllfeLNQRQATT---------LVMVTHDVQL 209
Cdd:PRK10636 456 EPTNHLD-------------LDMRQALTealidfegaLVVVSHDRHL 489
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
21-85 |
4.00e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 49.26 E-value: 4.00e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502612564 21 NQISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDAS--AGEVRLLGQPLSQLDEEGRAAL 85
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKGESILDLEPEERAHL 84
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-212 |
5.27e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.51 E-value: 5.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 5 NVIEVHHVAKRVGEGEnqisILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVrllgqplsQLDEEGRAA 84
Cdd:PRK15064 318 NALEVENLTKGFDNGP----LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV--------KWSENANIG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 85 LRARDIGFVFQSFMlvpTLTALenvqlpaLLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQ-LSGGEQQRVALARAFSA 163
Cdd:PRK15064 386 YYAQDHAYDFENDL---TLFDW-------MSQWRQEGDDEQAVRGTLGRLLFSQDDIKKSVKvLSGGEKGRMLFGKLMMQ 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502612564 164 RPQILFADEPTGNLDRQTgdrIADLLFELNQRQAtTLVMVTHDVQ----LAAR 212
Cdd:PRK15064 456 KPNVLVMDEPTNHMDMES---IESLNMALEKYEG-TLIFVSHDREfvssLATR 504
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-213 |
7.21e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.24 E-value: 7.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 2 PAQNVIEVHHVAKRVGEGenqiSILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGldDASAG---EVRLLGQPlsqld 78
Cdd:PRK10938 256 ANEPRIVLNNGVVSYNDR----PILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG--DHPQGysnDLTLFGRR----- 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 79 eegRAALRA-----RDIGFVFQSFMLVPTL-TALENVQLPALlrgereHDS-----------RQRAAALLTQLGLGQRLR 141
Cdd:PRK10938 325 ---RGSGETiwdikKHIGYVSSSLHLDYRVsTSVRNVILSGF------FDSigiyqavsdrqQKLAQQWLDILGIDKRTA 395
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502612564 142 HLPAQ-LSGGEQQRVALARAFSARPQILFADEPTGNLD---RQTGDRIADLLFELNQRQattLVMVTHDVQLAARC 213
Cdd:PRK10938 396 DAPFHsLSWGQQRLALIVRALVKHPTLLILDEPLQGLDplnRQLVRRFVDVLISEGETQ---LLFVSHHAEDAPAC 468
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
25-185 |
1.08e-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: 49.14 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 25 ILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRllgqplsqldEEGRaalrardIGFVFQSFMLVPTlT 104
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK----------HSGR-------ISFSPQTSWIMPG-T 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 105 ALENVqLPALLRGEREHDSRQRAAALLTQLGLGQRLRHLP-----AQLSGGEQQRVALARAFSARPQILFADEPTGNLDR 179
Cdd:TIGR01271 503 IKDNI-IFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
....*.
gi 502612564 180 QTGDRI 185
Cdd:TIGR01271 582 VTEKEI 587
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
26-226 |
1.65e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 47.50 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 26 LTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVrllgqplsqlDEEGRAALRARDIGFVFQsfmlvptLTA 105
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV----------DRNGEVSVIAISAGLSGQ-------LTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 106 LENVQLPALLRGEREHDSRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEPTGNLDRQTGDRI 185
Cdd:PRK13546 103 IENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKC 182
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 502612564 186 ADLLFELNQrQATTLVMVTHDV-QLAARCQRRLRLVDGTLRE 226
Cdd:PRK13546 183 LDKIYEFKE-QNKTIFFVSHNLgQVRQFCTKIAWIEGGKLKD 223
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
26-209 |
1.68e-06 |
|
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: 46.55 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 26 LTAVDLVVKRGQSLALIGESGSGKSTLLgiLAGLddASAGEVRLlgqplsqldEEGRAALRARDIGFVFQsfmlvptLTA 105
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLV--NEGL--YASGKARL---------ISFLPKFSRNKLIFIDQ-------LQF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 106 LENVQLpallrgerehdsrqraaallTQLGLGQRLrhlpAQLSGGEQQRVALAR-AFSARPQILFA-DEPTGNLDRQTGD 183
Cdd:cd03238 71 LIDVGL--------------------GYLTLGQKL----STLSGGELQRVKLASeLFSEPPGTLFIlDEPSTGLHQQDIN 126
|
170 180
....*....|....*....|....*.
gi 502612564 184 RIADLLFELNQrQATTLVMVTHDVQL 209
Cdd:cd03238 127 QLLEVIKGLID-LGNTVILIEHNLDV 151
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
25-226 |
2.93e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 47.66 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 25 ILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLdeeGRAALRaRDIGFVFQSFML----- 99
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKF---GLTDLR-RVLSIIPQSPVLfsgtv 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 100 ---VPTLTALENVQLPALLrgEREH--DSRQRAAalltqLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEPT 174
Cdd:PLN03232 1327 rfnIDPFSEHNDADLWEAL--ERAHikDVIDRNP-----FGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEAT 1399
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 502612564 175 GNLDRQTGDRIADLLFElnQRQATTLVMVTHDVQLAARCQRRLRLVDGTLRE 226
Cdd:PLN03232 1400 ASVDVRTDSLIQRTIRE--EFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLE 1449
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
25-226 |
3.54e-06 |
|
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: 47.25 E-value: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 25 ILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGqplsqldeegraaLRARDIGFVFQSFMLvpTLT 104
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG-------------LNIAKIGLHDLRFKI--TII 1365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 105 ALENVQLPALLRGEREHDSRQRAAALLTQLGLGQ----------RLRHLPAQ----LSGGEQQRVALARAFSARPQILFA 170
Cdd:TIGR00957 1366 PQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHlktfvsalpdKLDHECAEggenLSVGQRQLVCLARALLRKTKILVL 1445
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502612564 171 DEPTGNLDRQTGDRIADLLfeLNQRQATTLVMVTHDVQLAARCQRRLRLVDGTLRE 226
Cdd:TIGR00957 1446 DEATAAVDLETDNLIQSTI--RTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAE 1499
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
7-226 |
5.91e-06 |
|
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: 46.00 E-value: 5.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVGEGENqiSILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDaSAGEVRLLGQPLSQLD-EEGRAAL 85
Cdd:cd03289 3 MTVKDLTAKYTEGGN--AVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPlQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 86 rardiGFVFQSfMLVPTLTALENVQlpallrgEREHDSRQRAAALLTQLGLGQRLRHLPAQL-----------SGGEQQR 154
Cdd:cd03289 80 -----GVIPQK-VFIFSGTFRKNLD-------PYGKWSDEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502612564 155 VALARAFSARPQILFADEPTGNLDRQTGDRIADLLfelnqRQA---TTLVMVTHDVQLAARCQRRLRLVDGTLRE 226
Cdd:cd03289 147 MCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTL-----KQAfadCTVILSEHRIEAMLECQRFLVIEENKVRQ 216
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
129-215 |
1.84e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.20 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 129 ALLTQLGLGQRL--RHLpAQLSGGEQQRVALARAFSAR----PQILfaDEPTGNLDRQTGDRIADLLFELnQRQATTLVM 202
Cdd:PRK00635 458 SILIDLGLPYLTpeRAL-ATLSGGEQERTALAKHLGAEligiTYIL--DEPSIGLHPQDTHKLINVIKKL-RDQGNTVLL 533
|
90
....*....|...
gi 502612564 203 VTHDVQLAARCQR 215
Cdd:PRK00635 534 VEHDEQMISLADR 546
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
147-222 |
2.10e-05 |
|
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: 43.71 E-value: 2.10e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502612564 147 LSGGEQQRVALARAFSARPQILFADEPTGNLDRQTGDRIADLLFELNQRQATTLVMVTHDVQLAARCQRRLRLVDG 222
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEG 147
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
40-206 |
2.43e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 43.85 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 40 ALIGESGSGKSTLL-GILAGLDDASAGEVRLLGQPLSQLDEEGRAALRARDIGFV---------FQSFMLVPT---LTAL 106
Cdd:COG0419 27 LIVGPNGAGKSTILeAIRYALYGKARSRSKLRSDLINVGSEEASVELEFEHGGKRyrierrqgeFAEFLEAKPserKEAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 107 ENV-------QLPALLRGEREHDSRQRAAALLTQLGLGQRLRHL-----PAQLSGGEQQRVALARAFSarpqiLFADepT 174
Cdd:COG0419 107 KRLlgleiyeELKERLKELEEALESALEELAELQKLKQEILAQLsgldpIETLSGGERLRLALADLLS-----LILD--F 179
|
170 180 190
....*....|....*....|....*....|..
gi 502612564 175 GNLDRQTGDRIADLLFElnqrqattLVMVTHD 206
Cdd:COG0419 180 GSLDEERLERLLDALEE--------LAIITHV 203
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
23-181 |
2.46e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.02 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 23 ISILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLlgQPLSQLDEEGRAALRARdIGFVFQSFML--- 99
Cdd:PTZ00265 398 VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIII--NDSHNLKDINLKWWRSK-IGVVSQDPLLfsn 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 100 ------------VPTLTALENVQLPALLRGEREHDSRQRAAA-------LLTQLGLGQRLRH------------------ 142
Cdd:PTZ00265 475 siknnikyslysLKDLEALSNYYNEDGNDSQENKNKRNSCRAkcagdlnDMSNTTDSNELIEmrknyqtikdsevvdvsk 554
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 143 ----------LP-----------AQLSGGEQQRVALARAFSARPQILFADEPTGNLDRQT 181
Cdd:PTZ00265 555 kvlihdfvsaLPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
39-209 |
2.92e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.47 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 39 LALIGESGSGKSTLLGILAGLDDASAGEV----RLLGQPLSQLDEEGrAALRARDIGFVFQSFMLVPtltalenvqlpal 114
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTVfrsaKVRMAVFSQHHVDG-LDLSSNPLLYMMRCFPGVP------------- 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 115 lrgerehdsRQRAAALLTQLGLGQRLRHLPA-QLSGGEQQRVALARAFSARPQILFADEPTGNLDRqtgDRIADLLFELN 193
Cdd:PLN03073 604 ---------EQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDL---DAVEALIQGLV 671
|
170
....*....|....*.
gi 502612564 194 QRQATTLvMVTHDVQL 209
Cdd:PLN03073 672 LFQGGVL-MVSHDEHL 686
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-181 |
3.23e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 44.34 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 4 QNVIEVHHVAKRVGEG---ENqisiltaVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRlLGQPLsqldee 80
Cdd:PRK11819 322 DKVIEAENLSKSFGDRlliDD-------LSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIK-IGETV------ 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 81 graalrarDIGFVFQSF-MLVPTLTALENVQ--LPALLRGEREHDSRqraaALLTQLGL-GQRLRHLPAQLSGGEQQRVA 156
Cdd:PRK11819 388 --------KLAYVDQSRdALDPNKTVWEEISggLDIIKVGNREIPSR----AYVGRFNFkGGDQQKKVGVLSGGERNRLH 455
|
170 180
....*....|....*....|....*
gi 502612564 157 LARAFSARPQILFADEPTGNLDRQT 181
Cdd:PRK11819 456 LAKTLKQGGNVLLLDEPTNDLDVET 480
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
7-68 |
4.10e-05 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 43.77 E-value: 4.10e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502612564 7 IEVHHVAKRVGEGenqISILTAVdlvVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVR 68
Cdd:PRK01889 172 VPVLAVSALDGEG---LDVLAAW---LSGGKTVALLGSSGVGKSTLVNALLGEEVQKTGAVR 227
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
35-207 |
6.00e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 41.98 E-value: 6.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 35 RGQSLALIGESGSGKSTLLGILAGLddasagevrllgqplsqldeegraaLRARDIGFVFqsfmlvptltalenvqlpal 114
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARE-------------------------LGPPGGGVIY-------------------- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 115 LRGEREHDSrqraaalLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEPTGNLDRQTGDRI-----ADLL 189
Cdd:smart00382 36 IDGEDILEE-------VLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLllleeLRLL 108
|
170
....*....|....*...
gi 502612564 190 FELNQRQATTLVMVTHDV 207
Cdd:smart00382 109 LLLKSEKNLTVILTTNDE 126
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
43-189 |
6.47e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 42.55 E-value: 6.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 43 GESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEGraalrardIGFVFQSFMLVPTLTALENVQLPALLrgereHD 122
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPY--------CTYIGHNLGLKLEMTVFENLKFWSEI-----YN 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502612564 123 SRQRAAALLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEPTGNLDRQTGDRIADLL 189
Cdd:PRK13541 100 SAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLI 166
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
18-226 |
7.09e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 43.57 E-value: 7.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 18 EGENQISILTAVDLVVKRGQSLALIGESGSGKSTL----LGILAGLDDASA---GEVRLLGQplsqldeegraalrardI 90
Cdd:PLN03130 625 DSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLisamLGELPPRSDASVvirGTVAYVPQ-----------------V 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 91 GFVFQSfmlvptlTALENVQLPALLRGER----------EHDSRQRAAALLTQLGlgQRlrhlPAQLSGGEQQRVALARA 160
Cdd:PLN03130 688 SWIFNA-------TVRDNILFGSPFDPERyeraidvtalQHDLDLLPGGDLTEIG--ER----GVNISGGQKQRVSMARA 754
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502612564 161 FSARPQILFADEPTGNLDRQTGDRIAD--LLFELNQRqatTLVMVTHDVQLAARCQRRLRLVDGTLRE 226
Cdd:PLN03130 755 VYSNSDVYIFDDPLSALDAHVGRQVFDkcIKDELRGK---TRVLVTNQLHFLSQVDRIILVHEGMIKE 819
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
126-178 |
7.49e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.31 E-value: 7.49e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 502612564 126 RAAALLTQLGLGQRLRHLPA-QLSGGEQQRVALARAFSARPQILFADEPTGNLD 178
Cdd:PLN03073 323 RAASILAGLSFTPEMQVKATkTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
33-209 |
2.45e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 41.72 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 33 VKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVrllgqpLSQL-----------DEEGRAALRARDIGFVFQSFMLVP 101
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV------DPELkisykpqyikpDYDGTVEDLLRSITDDLGSSYYKS 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 102 TLtaLENVQLPALLrgEREHDsrqraaalltqlglgqrlrhlpaQLSGGEQQRVALARAFSARPQILFADEPTGNLD--- 178
Cdd:PRK13409 436 EI--IKPLQLERLL--DKNVK-----------------------DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveq 488
|
170 180 190
....*....|....*....|....*....|....*....
gi 502612564 179 --------RqtgdRIADllfelnQRQATTLVmVTHDVQL 209
Cdd:PRK13409 489 rlavakaiR----RIAE------EREATALV-VDHDIYM 516
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
33-209 |
3.37e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 41.31 E-value: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 33 VKRGQSLALIGESGSGKSTLLGILAGLDDASAGEV----RLLGQP---LSQLDEEGRAALRARDIGFVFQSFmlvptlta 105
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVdedlKISYKPqyiSPDYDGTVEEFLRSANTDDFGSSY-------- 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 106 lenvqlpalLRGErehdsrqraaaLLTQLGLGQRLRHLPAQLSGGEQQRVALARAFSARPQILFADEPTGNLD------- 178
Cdd:COG1245 435 ---------YKTE-----------IIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrlav 494
|
170 180 190
....*....|....*....|....*....|....*
gi 502612564 179 ----RqtgdRIADllfelnQRQATTLVmVTHDVQL 209
Cdd:COG1245 495 akaiR----RFAE------NRGKTAMV-VDHDIYL 518
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
154-218 |
3.92e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.19 E-value: 3.92e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502612564 154 RVALARAFSARPQILFADEPTGNLDRQTGDRIADLLFEL----NQRQATTLVMVTHDVQLAARCQRRLR 218
Cdd:TIGR00606 1213 RLALAETFCLNCGIIALDEPTTNLDRENIESLAHALVEIiksrSQQRNFQLLVITHDEDFVELLGRSEY 1281
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
131-207 |
4.47e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.77 E-value: 4.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 131 LTQLGLGQrlrhlPA-QLSGGEQQRVALARAFSAR---PQILFADEPTgnldrqTGDRIADL--LFELNQR---QATTLV 201
Cdd:TIGR00630 818 LGYIRLGQ-----PAtTLSGGEAQRIKLAKELSKRstgRTLYILDEPT------TGLHFDDIkkLLEVLQRlvdKGNTVV 886
|
....*...
gi 502612564 202 MVTH--DV 207
Cdd:TIGR00630 887 VIEHnlDV 894
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
147-195 |
5.04e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.48 E-value: 5.04e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 502612564 147 LSGGEQQRVALARAFSARPQILFADEPTGNLDRQTGDRIADLLFELNQR 195
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK 440
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
7-181 |
7.78e-04 |
|
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: 39.51 E-value: 7.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 7 IEVHHVAKRVgegENQIS-ILTAVDLVVKRGQSLALIGESGSGKSTLLGILAGLDDASAGEVRLLGQPLSQLDEEgraAL 85
Cdd:cd03288 20 IKIHDLCVRY---ENNLKpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLH---TL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 86 RARdIGFVFQSFMLVPTLTALEnvqlpalLRGERE-HDSRQRAAALLTQLGLgqRLRHLPAQL-----------SGGEQQ 153
Cdd:cd03288 94 RSR-LSIILQDPILFSGSIRFN-------LDPECKcTDDRLWEALEIAQLKN--MVKSLPGGLdavvteggenfSVGQRQ 163
|
170 180
....*....|....*....|....*...
gi 502612564 154 RVALARAFSARPQILFADEPTGNLDRQT 181
Cdd:cd03288 164 LFCLARAFVRKSSILIMDEATASIDMAT 191
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
129-206 |
9.62e-04 |
|
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: 39.16 E-value: 9.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 129 ALLTQLGLGQ-RLRHLPAQLSGGEQQRVALARAFSAR-PQILFA-DEPTGNLDRQTGDRIADLLFELnQRQATTLVMVTH 205
Cdd:cd03270 119 GFLVDVGLGYlTLSRSAPTLSGGEAQRIRLATQIGSGlTGVLYVlDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEH 197
|
.
gi 502612564 206 D 206
Cdd:cd03270 198 D 198
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
136-174 |
1.11e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 39.62 E-value: 1.11e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 502612564 136 LGQrlrhlPA-QLSGGEQQRVALARAFSARPQ-----ILfaDEPT 174
Cdd:COG0178 820 LGQ-----PAtTLSGGEAQRVKLASELSKRSTgktlyIL--DEPT 857
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
147-174 |
1.74e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 39.00 E-value: 1.74e-03
10 20
....*....|....*....|....*...
gi 502612564 147 LSGGEQQRVALARAFSARPQILFADEPT 174
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPT 432
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
139-219 |
1.88e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.04 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612564 139 RLRHLP-----AQLSGGEQQRVALARAFSA---RPQILFADEPTGNLDRQTGDRIADLLFELNQrQATTLVMVTHDVQLA 210
Cdd:PRK00635 797 GLDYLPlgrplSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTH-QGHTVVIIEHNMHVV 875
|
....*....
gi 502612564 211 ARCQRRLRL 219
Cdd:PRK00635 876 KVADYVLEL 884
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
136-174 |
1.97e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 38.90 E-value: 1.97e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 502612564 136 LGQrlrhlPA-QLSGGEQQRVALARAFSARPQ-----ILfaDEPT 174
Cdd:PRK00349 824 LGQ-----PAtTLSGGEAQRVKLAKELSKRSTgktlyIL--DEPT 861
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
35-68 |
7.04e-03 |
|
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: 36.61 E-value: 7.04e-03
10 20 30
....*....|....*....|....*....|....
gi 502612564 35 RGQSLALIGESGSGKSTLLGILAGLDDASAGEVR 68
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLNALLPELVLATGEIS 117
|
|
| |
