|
Name |
Accession |
Description |
Interval |
E-value |
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
11-240 |
2.20e-120 |
|
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: 342.49 E-value: 2.20e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 11 MPQTIISAQNLTQKIQLAQKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQ 90
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 91 RAEVRLKHIGFVFQSFQLLPHLTALENVMLPLRLQEKfkyAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARA 170
Cdd:COG4181 84 RARLRARHVGFVFQSFQLLPTLTALENVMLPLELAGR---RDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 171 LIREPKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDPKLAAQCQRHYALIDGQLVEQFAA 240
Cdd:COG4181 161 FATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTAA 230
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
13-237 |
2.82e-115 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 329.31 E-value: 2.82e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 13 QTIISAQNLTQKIQLAQKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRA 92
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 93 EVRLKHIGFVFQSFQLLPHLTALENVMLPLRLQeKFKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALI 172
Cdd:COG1136 82 RLRRRHIGFVFQFFNLLPELTALENVALPLLLA-GVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491113568 173 REPKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDPKLAAQCQRHYALIDGQLVEQ 237
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
16-234 |
3.92e-102 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 295.55 E-value: 3.92e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 16 ISAQNLTQKIQLAQKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAEVR 95
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 96 LKHIGFVFQSFQLLPHLTALENVMLPLRLQEKFKyAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREP 175
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPK-KERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491113568 176 KIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDPKLAAQCQRHYALIDGQL 234
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
15-236 |
9.68e-84 |
|
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: 249.19 E-value: 9.68e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 15 IISAQNLTQKIQLAQKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAEV 94
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 95 RLKHIGFVFQSFQLLPHLTALENVMLPLrLQEKFKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIRE 174
Cdd:TIGR02211 81 RNKKLGFIYQFHHLLPDFTALENVAMPL-LIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491113568 175 PKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDPKLAAQCQRHYALIDGQLVE 236
Cdd:TIGR02211 160 PSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVLEMKDGQLFN 221
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
15-236 |
6.06e-82 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 244.58 E-value: 6.06e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 15 IISAQNLTqKIQlaQKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAEV 94
Cdd:COG2884 1 MIRFENVS-KRY--PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 95 RlKHIGFVFQSFQLLPHLTALENVMLPLRLQEKfKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIRE 174
Cdd:COG2884 78 R-RRIGVVFQDFRLLPDRTVYENVALPLRVTGK-SRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491113568 175 PKIIFADEPTGNLDGETATEIEQLLFELNReLGTTLVLVTHDPKLAAQCQ-RHYALIDGQLVE 236
Cdd:COG2884 156 PELLLADEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPkRVLELEDGRLVR 217
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
11-237 |
4.20e-79 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 237.75 E-value: 4.20e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 11 MP-QTIISAQNLTQKIQLAQKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEE 89
Cdd:PRK10584 1 MPaENIVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 90 QRAEVRLKHIGFVFQSFQLLPHLTALENVMLPLRLQEKfKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIAR 169
Cdd:PRK10584 81 ARAKLRAKHVGFVFQSFMLIPTLNALENVELPALLRGE-SSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALAR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491113568 170 ALIREPKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDPKLAAQCQRHYALIDGQLVEQ 237
Cdd:PRK10584 160 AFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
11-216 |
3.30e-72 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 221.12 E-value: 3.30e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 11 MPQTIISAQNLTQKIQLAQKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEq 90
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 91 raevrlkhIGFVFQSFQLLPHLTALENVMLPLRLQEKFKyAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARA 170
Cdd:COG1116 82 --------RGVVFQEPALLPWLTVLDNVALGLELRGVPK-AERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491113568 171 LIREPKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHD 216
Cdd:COG1116 153 LANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHD 198
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
11-239 |
1.59e-68 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 210.83 E-value: 1.59e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 11 MPQTIISAQNLTQKIQLAQKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQ 90
Cdd:PRK11629 1 MNKILLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 91 RAEVRLKHIGFVFQSFQLLPHLTALENVMLPLrLQEKFKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARA 170
Cdd:PRK11629 81 KAELRNQKLGFIYQFHHLLPDFTALENVAMPL-LIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491113568 171 LIREPKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDPKLAAQCQRHYALIDGQLVEQFA 239
Cdd:PRK11629 160 LVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELS 228
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
15-216 |
1.74e-68 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 211.01 E-value: 1.74e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 15 IISAQNLTQKIqlaqKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAeLNEEQRAEV 94
Cdd:COG1126 1 MIEIENLHKSF----GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 95 RlKHIGFVFQSFQLLPHLTALENVMLPLRLQEKFKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIRE 174
Cdd:COG1126 76 R-RKVGMVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAME 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 491113568 175 PKIIFADEPTGNLDGETATEIEQLLFELNRElGTTLVLVTHD 216
Cdd:COG1126 155 PKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHE 195
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
16-216 |
2.06e-68 |
|
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: 210.02 E-value: 2.06e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 16 ISAQNLTQKIQLAQKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNeeqraevr 95
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 96 lKHIGFVFQSFQLLPHLTALENVMLPLRLQeKFKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREP 175
Cdd:cd03293 73 -PDRGYVFQQDALLPWLTVLDNVALGLELQ-GVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDP 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 491113568 176 KIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHD 216
Cdd:cd03293 151 DVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHD 191
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
11-237 |
2.07e-66 |
|
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: 205.60 E-value: 2.07e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 11 MPQTIISAQNLTqkiqLAQKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQ 90
Cdd:COG1127 1 MSEPMIEVRNLT----KSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 91 RAEVRlKHIGFVFQSFQLLPHLTALENVMLPLRLQEKFKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARA 170
Cdd:COG1127 77 LYELR-RRIGMLFQGGALFDSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491113568 171 LIREPKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHD-PKLAAQCQRHYALIDGQLVEQ 237
Cdd:COG1127 156 LALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDlDSAFAIADRVAVLADGKIIAE 223
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
19-225 |
5.46e-65 |
|
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: 200.92 E-value: 5.46e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 19 QNLTQKIqlaqKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAEVRLKH 98
Cdd:TIGR03608 2 KNISKKF----GDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRREK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 99 IGFVFQSFQLLPHLTALENVMLPLRLQEKFKyAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKII 178
Cdd:TIGR03608 78 LGYLFQNFALIENETVEENLDLGLKYKKLSK-KEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491113568 179 FADEPTGNLDGETATEIEQLLFELNRElGTTLVLVTHDPKLAAQCQR 225
Cdd:TIGR03608 157 LADEPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDPEVAKQADR 202
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
33-235 |
1.17e-64 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 201.44 E-value: 1.17e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 33 TIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAEVRlKHIGFVFQSFQLLPHL 112
Cdd:COG3638 17 PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLR-RRIGMIFQQFNLVPRL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 113 TALENVM---LP--------LRLqekfkYAEAE-QKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFA 180
Cdd:COG3638 96 SVLTNVLagrLGrtstwrslLGL-----FPPEDrERALEALERVGLADKAYQRADQLSGGQQQRVAIARALVQEPKLILA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491113568 181 DEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDPKLAAQ-CQRHYALIDGQLV 235
Cdd:COG3638 171 DEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRyADRIIGLRDGRVV 226
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
16-216 |
1.72e-63 |
|
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: 197.37 E-value: 1.72e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 16 ISAQNLTQKIqlaqKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIaELNEEQRAEVR 95
Cdd:cd03262 1 IEIKNLHKSF----GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL-TDDKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 96 lKHIGFVFQSFQLLPHLTALENVMLPLRLQEKFKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREP 175
Cdd:cd03262 76 -QKVGMVFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 491113568 176 KIIFADEPTGNLDGETATEIEQLLFELNRElGTTLVLVTHD 216
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHE 194
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
15-238 |
8.41e-63 |
|
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: 196.26 E-value: 8.41e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 15 IISAQNLTQKIQLAQKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAEV 94
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 95 RlKHIGFVFQSFQLLPHLTALENVMLPLRLqEKFKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIRE 174
Cdd:cd03258 81 R-RRIGMIFQHFNLLSSRTVFENVALPLEI-AGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491113568 175 PKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDPKLAAQCQRHYALID-GQLVEQF 238
Cdd:cd03258 159 PKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEkGEVVEEG 223
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
33-217 |
1.70e-62 |
|
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: 194.66 E-value: 1.70e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 33 TIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRaevrlkHIGFVFQSFQLLPHL 112
Cdd:cd03259 14 RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERR------NIGMVFQDYALFPHL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 113 TALENVMLPLRLQeKFKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETA 192
Cdd:cd03259 88 TVAENIAFGLKLR-GVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLR 166
|
170 180
....*....|....*....|....*
gi 491113568 193 TEIEQLLFELNRELGTTLVLVTHDP 217
Cdd:cd03259 167 EELREELKELQRELGITTIYVTHDQ 191
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
11-217 |
4.00e-62 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 198.40 E-value: 4.00e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 11 MPQTIISAQNLTQKIqlaqKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQ 90
Cdd:COG3842 1 MAMPALELENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 91 RaevrlkHIGFVFQSFQLLPHLTALENVMLPLRLQeKFKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARA 170
Cdd:COG3842 77 R------NVGMVFQDYALFPHLTVAENVAFGLRMR-GVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARA 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491113568 171 LIREPKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDP 217
Cdd:COG3842 150 LAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQ 196
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
15-247 |
6.16e-62 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 197.61 E-value: 6.16e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 15 IISAQNLTQKIQLAQKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAEV 94
Cdd:COG1135 1 MIELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 95 RlKHIGFVFQSFQLLPHLTALENVMLPLRLQeKFKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIRE 174
Cdd:COG1135 81 R-RKIGMIFQHFNLLSSRTVAENVALPLEIA-GVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 175 PKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDPKLAAQ-CQRhYALID-GQLVEQ-----FAAKPTAAIT 247
Cdd:COG1135 159 PKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRiCDR-VAVLEnGRIVEQgpvldVFANPQSELT 237
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
15-235 |
2.43e-61 |
|
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: 192.16 E-value: 2.43e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 15 IISAQNLTQKIQLAQKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAEV 94
Cdd:TIGR02982 1 VISIRNLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 95 RlKHIGFVFQSFQLLPHLTALENVMLPLRLQEKFKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIRE 174
Cdd:TIGR02982 81 R-RRIGYIFQAHNLLGFLTARQNVQMALELQPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHH 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491113568 175 PKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDPKLAAQCQRHYALIDGQLV 235
Cdd:TIGR02982 160 PKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDNRILDVADRILQMEDGKLL 220
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
15-237 |
1.57e-60 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 190.41 E-value: 1.57e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 15 IISAQNLTQKIQLAQKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRaEV 94
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLR-KI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 95 RLKHIGFVFQ-SFQLL-PHLTALENVMLPLRLQEKFKYAEAEQKA-LNLLKRVGL-ERQAQQTPKVLSGGEQQRVAIARA 170
Cdd:cd03257 80 RRKEIQMVFQdPMSSLnPRMTIGEQIAEPLRIHGKLSKKEARKEAvLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491113568 171 LIREPKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDPKLAAQ-CQRHYALIDGQLVEQ 237
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKiADRVAVMYAGKIVEE 227
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
33-237 |
1.36e-59 |
|
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: 188.09 E-value: 1.36e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 33 TIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAEVRlKHIGFVFQSFQLLPHL 112
Cdd:cd03261 14 TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR-RRMGMLFQSGALFDSL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 113 TALENVMLPLRLQEKFKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETA 192
Cdd:cd03261 93 TVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIAS 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491113568 193 TEIEQLLFELNRELGTTLVLVTHD-PKLAAQCQRHYALIDGQLVEQ 237
Cdd:cd03261 173 GVIDDLIRSLKKELGLTSIMVTHDlDTAFAIADRIAVLYDGKIVAE 218
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
19-248 |
5.98e-59 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 197.25 E-value: 5.98e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 19 QNLTQKIQLAQKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAEVRLKH 98
Cdd:PRK10535 8 KDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRREH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 99 IGFVFQSFQLLPHLTALENVMLPLRLQEKFKyAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKII 178
Cdd:PRK10535 88 FGFIFQRYHLLSHLTAAQNVEVPAVYAGLER-KQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVI 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 179 FADEPTGNLDGETATEIEQLLFELnRELGTTLVLVTHDPKLAAQCQRHYALIDGQLVEQFAAKPTAAITG 248
Cdd:PRK10535 167 LADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVRNPPAQEKVNVAG 235
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
34-233 |
1.64e-58 |
|
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: 184.76 E-value: 1.64e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 34 IFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAEVRlKHIGFVFQSFQLLPHLT 113
Cdd:TIGR02673 17 ALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLR-RRIGVVFQDFRLLPDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 114 ALENVMLPLRLQEKfKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETAT 193
Cdd:TIGR02673 96 VYENVALPLEVRGK-KEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGNLDPDLSE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 491113568 194 EIEQLLFELNReLGTTLVLVTHDPKLAAQC-QRHYALIDGQ 233
Cdd:TIGR02673 175 RILDLLKRLNK-RGTTVIVATHDLSLVDRVaHRVIILDDGR 214
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
11-237 |
1.91e-56 |
|
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: 187.80 E-value: 1.91e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 11 MPQTIISAQNLTQK-IQLAQKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEE 89
Cdd:COG1123 256 AAEPLLEVRNLSKRyPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 90 QRAEVRlKHIGFVFQ--SFQLLPHLTALENVMLPLRLQEKFKYAEAEQKALNLLKRVGLERQ-AQQTPKVLSGGEQQRVA 166
Cdd:COG1123 336 SLRELR-RRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDlADRYPHELSGGQRQRVA 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491113568 167 IARALIREPKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDPKLAAQ-CQRHYALIDGQLVEQ 237
Cdd:COG1123 415 IARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVED 486
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
33-235 |
5.55e-56 |
|
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: 179.30 E-value: 5.55e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 33 TIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAEVRlKHIGFVFQSFQLLPHL 112
Cdd:cd03256 15 KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR-RQIGMIFQQFNLIERL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 113 TALENVMLPlRLQEK--------FKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPT 184
Cdd:cd03256 94 SVLENVLSG-RLGRRstwrslfgLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491113568 185 GNLDGETATEIEQLLFELNRELGTTLVLVTHDPKLAAQ-CQRHYALIDGQLV 235
Cdd:cd03256 173 ASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREyADRIVGLKDGRIV 224
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
16-237 |
1.89e-54 |
|
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: 174.83 E-value: 1.89e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 16 ISAQNLTQKIQlaqKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIaelNEEQRAEVR 95
Cdd:COG1122 1 IELENLSFSYP---GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDI---TKKNLRELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 96 lKHIGFVFQS--FQLLpHLTALENVMLPLRlQEKFKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIR 173
Cdd:COG1122 75 -RKVGLVFQNpdDQLF-APTVEEDVAFGPE-NLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491113568 174 EPKIIFADEPTGNLDGETATEIEQLLFELNRElGTTLVLVTHDPKLAAQ-CQRHYALIDGQLVEQ 237
Cdd:COG1122 152 EPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAElADRVIVLDDGRIVAD 215
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
37-234 |
2.09e-54 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 174.13 E-value: 2.09e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 37 NLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAEVRlKHIGFVFQSFQLLPHLTALE 116
Cdd:cd03292 19 GINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR-RKIGVVFQDFRLLPDRNVYE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 117 NVMLPLRLQEKfKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETATEIE 196
Cdd:cd03292 98 NVAFALEVTGV-PPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIM 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 491113568 197 QLLFELNRElGTTLVLVTHDPKLAAQCQ-RHYALIDGQL 234
Cdd:cd03292 177 NLLKKINKA-GTTVVVATHAKELVDTTRhRVIALERGKL 214
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
30-233 |
2.45e-54 |
|
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: 172.76 E-value: 2.45e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 30 KQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAEVRlkHIGFVFQSFQLL 109
Cdd:cd03229 11 GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRR--RIGMVFQDFALF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 110 PHLTALENVMLPlrlqekfkyaeaeqkalnllkrvglerqaqqtpkvLSGGEQQRVAIARALIREPKIIFADEPTGNLDG 189
Cdd:cd03229 89 PHLTVLENIALG-----------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDP 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 491113568 190 ETATEIEQLLFELNRELGTTLVLVTHDPKLAAQ-CQRHYALIDGQ 233
Cdd:cd03229 134 ITRREVRALLKSLQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
36-217 |
2.61e-54 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 178.34 E-value: 2.61e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 36 ENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRaevrlkHIGFVFQSFQLLPHLTAL 115
Cdd:COG3839 20 KDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDR------NIAMVFQSYALYPHMTVY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 116 ENVMLPLRLQeKFKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETATEI 195
Cdd:COG3839 94 ENIAFPLKLR-KVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEM 172
|
170 180
....*....|....*....|..
gi 491113568 196 EQLLFELNRELGTTLVLVTHDP 217
Cdd:COG3839 173 RAEIKRLHRRLGTTTIYVTHDQ 194
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
16-234 |
4.05e-54 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 173.46 E-value: 4.05e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 16 ISAQNLTQKIQlaqkQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEqraEVR 95
Cdd:COG4619 1 LELEGLSFRVG----GKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPP---EWR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 96 lKHIGFVFQSFQLLPHlTALENVMLPLRLQEKfkyAEAEQKALNLLKRVG-----LERQAQQtpkvLSGGEQQRVAIARA 170
Cdd:COG4619 74 -RQVAYVPQEPALWGG-TVRDNLPFPFQLRER---KFDRERALELLERLGlppdiLDKPVER----LSGGERQRLALIRA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491113568 171 LIREPKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDPKLAAQ-CQRHYALIDGQL 234
Cdd:COG4619 145 LLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
31-216 |
4.02e-53 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 171.81 E-value: 4.02e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 31 QLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRaEVRLKhIGFVFQSFQLLP 110
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDER-LIRQE-AGMVFQQFYLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 111 HLTALENVML-PLRLQEKFKyAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDG 189
Cdd:PRK09493 91 HLTALENVMFgPLRVRGASK-EEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDP 169
|
170 180
....*....|....*....|....*..
gi 491113568 190 ETATEIEQLLFELNRElGTTLVLVTHD 216
Cdd:PRK09493 170 ELRHEVLKVMQDLAEE-GMTMVIVTHE 195
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
37-236 |
6.16e-53 |
|
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: 172.06 E-value: 6.16e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 37 NLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAEVRLKHIGFVFQSFQLLPHLTALE 116
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 117 NVMLPLRLQEKFKyAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETATEIE 196
Cdd:cd03294 122 NVAFGLEVQGVPR-AEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQ 200
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 491113568 197 QLLFELNRELGTTLVLVTHDPKLAAQCQRHYALI-DGQLVE 236
Cdd:cd03294 201 DELLRLQAELQKTIVFITHDLDEALRLGDRIAIMkDGRLVQ 241
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
37-241 |
9.79e-53 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 174.18 E-value: 9.79e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 37 NLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVvcgesiaeLNEEQ---RAEVRLKHIGFVFQSFQLLPHLT 113
Cdd:COG1118 20 DVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIV--------LNGRDlftNLPPRERRVGFVFQHYALFPHMT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 114 ALENVMLPLRLQEKFKyAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETAT 193
Cdd:COG1118 92 VAENIAFGLRVRPPSK-AEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRK 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491113568 194 EIEQLLFELNRELGTTLVLVTHDPKLAAQCQRHYALIDGQLVEQFAAK 241
Cdd:COG1118 171 ELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTP 218
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
15-237 |
1.38e-52 |
|
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: 172.93 E-value: 1.38e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 15 IISAQNLTQKIQLAQKQLTIFENLNFDIQEGEQVAITGRSGSGKSTL----LGILATLDQaSSGKLVVCGESIAELNEEQ 90
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLaraiLGLLPPPGI-TSGEILFDGEDLLKLSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 91 RAEVRLKHIGFVFQ----SfqLLPHLTALENVMLPLRLQEKFKYAEAEQKALNLLKRVGL---ERQAQQTPKVLSGGEQQ 163
Cdd:COG0444 80 LRKIRGREIQMIFQdpmtS--LNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491113568 164 RVAIARALIREPKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDPKLAAQ-CQR---HYAlidGQLVEQ 237
Cdd:COG0444 158 RVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEiADRvavMYA---GRIVEE 232
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
16-237 |
1.70e-52 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 173.45 E-value: 1.70e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 16 ISAQNLTQKIQLAQKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAEVR 95
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 96 lKHIGFVFQSFQLLPHLTALENVMLPLRLQEKFKyAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREP 175
Cdd:PRK11153 82 -RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPK-AEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491113568 176 KIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDPKLAAQ-CQRHYALIDGQLVEQ 237
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQ 222
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
33-244 |
1.86e-52 |
|
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: 170.17 E-value: 1.86e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 33 TIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAEVRlKHIGFVFQSFQLLPHL 112
Cdd:TIGR02315 16 QALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLR-RRIGMIFQHYNLIERL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 113 TALENVMLPlRLQEK-------FKYAEAE-QKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPT 184
Cdd:TIGR02315 95 TVLENVLHG-RLGYKptwrsllGRFSEEDkERALSALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILADEPI 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491113568 185 GNLDGETATEIEQLLFELNRELGTTLVLVTHDPKLAAQ-CQRHYALIDGQLVeqFAAKPTA 244
Cdd:TIGR02315 174 ASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKyADRIVGLKAGEIV--FDGAPSE 232
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
34-233 |
2.39e-52 |
|
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: 168.80 E-value: 2.39e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 34 IFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAevrlKHIGFVFQSF--QLLpH 111
Cdd:cd03225 16 ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELR----RKVGLVFQNPddQFF-G 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 112 LTALENVMLPLRlQEKFKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGET 191
Cdd:cd03225 91 PTVEEEVAFGLE-NLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAG 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 491113568 192 ATEIEQLLFELNRElGTTLVLVTHDPKLAAQ-CQRHYALIDGQ 233
Cdd:cd03225 170 RRELLELLKKLKAE-GKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
16-241 |
4.95e-52 |
|
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: 169.21 E-value: 4.95e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 16 ISAQNLTQKIQLAQKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAElneeQRAEVR 95
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTR----RRRKAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 96 LKHIGFVFQ----SFQllPHLTALENVMLPLRLQEKfkyAEAEQKALNLLKRVGL-ERQAQQTPKVLSGGEQQRVAIARA 170
Cdd:COG1124 78 RRRVQMVFQdpyaSLH--PRHTVDRILAEPLRIHGL---PDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491113568 171 LIREPKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDPKLAAQ-CQRHYALIDGQLVEQFAAK 241
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVA 224
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
16-237 |
5.32e-52 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 168.70 E-value: 5.32e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 16 ISAQNLTQKIqlaqKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAElneeQRAEVR 95
Cdd:COG1131 1 IEVRGLTKRY----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR----DPAEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 96 lKHIGFVFQSFQLLPHLTALENVMLPLRLQeKFKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREP 175
Cdd:COG1131 73 -RRIGYVPQEPALYPDLTVRENLRFFARLY-GLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491113568 176 KIIFADEPTGNLDGETATEIEQLLFELNRElGTTLVLVTHDPKLAAQCQRHYALID-GQLVEQ 237
Cdd:COG1131 151 ELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDkGRIVAD 212
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
36-241 |
1.49e-50 |
|
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: 165.17 E-value: 1.49e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 36 ENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEeqraeVRLK-HIGFVFQSFQLLPHLTA 114
Cdd:cd03295 18 NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDP-----VELRrKIGYVIQQIGLFPHMTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 115 LENVMLPLRLqEKFKYAEAEQKALNLLKRVGLERQ--AQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETA 192
Cdd:cd03295 93 EENIALVPKL-LKWPKEKIRERADELLALVGLDPAefADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITR 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491113568 193 TEIEQLLFELNRELGTTLVLVTHDPKLAAQCQRHYALIDGQLVEQFAAK 241
Cdd:cd03295 172 DQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTP 220
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
13-237 |
2.88e-50 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 171.62 E-value: 2.88e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 13 QTIISAQNLTqkIQLAQKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQAS---SGKLVVCGESIAELNEE 89
Cdd:COG1123 2 TPLLEVRDLS--VRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 90 QRAevrlKHIGFVFQSF--QLLPhLTALENVMLPLRLQEKFKyAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAI 167
Cdd:COG1123 80 LRG----RRIGMVFQDPmtQLNP-VTVGDQIAEALENLGLSR-AEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491113568 168 ARALIREPKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDPKLAAQ-CQRHYALIDGQLVEQ 237
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEiADRVVVMDDGRIVED 224
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
33-216 |
8.95e-49 |
|
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: 160.48 E-value: 8.95e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 33 TIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRaevrlkHIGFVFQSFQLLPHL 112
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKR------PVNTVFQNYALFPHL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 113 TALENVMLPLRLQeKFKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETA 192
Cdd:cd03300 88 TVFENIAFGLRLK-KLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLR 166
|
170 180
....*....|....*....|....
gi 491113568 193 TEIEQLLFELNRELGTTLVLVTHD 216
Cdd:cd03300 167 KDMQLELKRLQKELGITFVFVTHD 190
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
15-235 |
1.27e-48 |
|
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: 160.59 E-value: 1.27e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 15 IISAQNLTqkiqLAQKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAev 94
Cdd:COG1120 1 MLEAENLS----VGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELA-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 95 rlKHIGFVFQSFQLLPHLTALENVML---P-LRLQEKFKyAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARA 170
Cdd:COG1120 75 --RRIAYVPQEPPAPFGLTVRELVALgryPhLGLFGRPS-AEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491113568 171 LIREPKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDPKLAAQ-CQRHYALIDGQLV 235
Cdd:COG1120 152 LAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARyADRLVLLKDGRIV 217
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
36-238 |
2.97e-48 |
|
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: 159.43 E-value: 2.97e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 36 ENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRaevrlkHIGFVFQSFQLLPHLTAL 115
Cdd:cd03296 19 DDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQER------NVGFVFQHYALFRHMTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 116 ENVMLPLRLQEKFKY---AEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETA 192
Cdd:cd03296 93 DNVAFGLRVKPRSERppeAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVR 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491113568 193 TEIEQLLFELNRELGTTLVLVTHDPKLAAQCQRHYALIDGQLVEQF 238
Cdd:cd03296 173 KELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQV 218
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
33-239 |
7.83e-47 |
|
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: 154.72 E-value: 7.83e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 33 TIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRaevrlkHIGFVFQSFQLLPHL 112
Cdd:cd03301 14 TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDR------DIAMVFQNYALYPHM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 113 TALENVMLPLRLQeKFKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETA 192
Cdd:cd03301 88 TVYDNIAFGLKLR-KVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491113568 193 TEIEQLLFELNRELGTTLVLVTHDPKLA-AQCQRHYALIDGQlVEQFA 239
Cdd:cd03301 167 VQMRAELKRLQQRLGTTTIYVTHDQVEAmTMADRIAVMNDGQ-IQQIG 213
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
34-216 |
2.22e-46 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 157.94 E-value: 2.22e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 34 IFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRaevrlkHIGFVFQSFQLLPHLT 113
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDR------KVGFVFQHYALFRHMT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 114 ALENV-----MLPLRlqEKFKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLD 188
Cdd:PRK10851 91 VFDNIafgltVLPRR--ERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
|
170 180
....*....|....*....|....*...
gi 491113568 189 GETATEIEQLLFELNRELGTTLVLVTHD 216
Cdd:PRK10851 169 AQVRKELRRWLRQLHEELKFTSVFVTHD 196
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
16-236 |
2.28e-46 |
|
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: 153.88 E-value: 2.28e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 16 ISAQNLTqkiqLAQKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATL-----DQASSGKLVVCGESIAELNEEq 90
Cdd:cd03260 1 IELRDLN----VYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVD- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 91 RAEVRLKhIGFVFQSFQLLPhLTALENVMLPLRLQEKFKYAEAEQKALNLLKRVGLERQA--QQTPKVLSGGEQQRVAIA 168
Cdd:cd03260 76 VLELRRR-VGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVkdRLHALGLSGGQQQRLCLA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491113568 169 RALIREPKIIFADEPTGNLDGETATEIEQLLFELNRElgTTLVLVTHDPKLAAQCQRHYALI-DGQLVE 236
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLlNGRLVE 220
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
14-241 |
1.11e-45 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 152.98 E-value: 1.11e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 14 TIISAQNLTQKIqlaqKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESI---AELNEEQ 90
Cdd:PRK11264 2 SAIEVKNLVKKF----HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtaRSLSQQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 91 RAEVRLK-HIGFVFQSFQLLPHLTALENVMLPLRLQEKFKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIAR 169
Cdd:PRK11264 78 GLIRQLRqHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491113568 170 ALIREPKIIFADEPTGNLD----GETATEIEQLLFElNRelgtTLVLVTHDPKLAAQCQRHYALID-GQLVEQFAAK 241
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDpelvGEVLNTIRQLAQE-KR----TMVIVTHEMSFARDVADRAIFMDqGRIVEQGPAK 229
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
3-216 |
2.95e-45 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 155.49 E-value: 2.95e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 3 QNTKESNIMPQTIISAQNLTqkiqlaqKQL---TIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVC 79
Cdd:PRK09452 2 KKLNKQPSSLSPLVELRGIS-------KSFdgkEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 80 GESIAELNEEQRaevrlkHIGFVFQSFQLLPHLTALENVMLPLRLQeKFKYAEAEQKALNLLKRVGLERQAQQTPKVLSG 159
Cdd:PRK09452 75 GQDITHVPAENR------HVNTVFQSYALFPHMTVFENVAFGLRMQ-KTPAAEITPRVMEALRMVQLEEFAQRKPHQLSG 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491113568 160 GEQQRVAIARALIREPKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHD 216
Cdd:PRK09452 148 GQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHD 204
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
11-235 |
2.96e-45 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 151.78 E-value: 2.96e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 11 MPQTIISAQNLTqkiqLAQKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAElneeq 90
Cdd:COG1121 2 MMMPAIELENLT----VSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 91 raevRLKHIGFVFQSFQLLPH--LTALENVMLPLRLQEKFKY---AEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRV 165
Cdd:COG1121 73 ----ARRRIGYVPQRAEVDWDfpITVRDVVLMGRYGRRGLFRrpsRADREAVDEALERVGLEDLADRPIGELSGGQQQRV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 166 AIARALIREPKIIFADEPTGNLDGETATEIEQLLFELNRElGTTLVLVTHDPKLAAQCQRHYALIDGQLV 235
Cdd:COG1121 149 LLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
43-220 |
8.53e-45 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 151.11 E-value: 8.53e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 43 QEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIA-------ELNEEQRAEV-RLK-HIGFVFQSFQLLPHLT 113
Cdd:COG4598 32 RKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkpdrdgELVPADRRQLqRIRtRLGMVFQSFNLWSHMT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 114 ALENVML-PLRLQEKFKyAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETA 192
Cdd:COG4598 112 VLENVIEaPVHVLGRPK-AEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELV 190
|
170 180
....*....|....*....|....*...
gi 491113568 193 TEIEQLLFELNRElGTTLVLVTHDPKLA 220
Cdd:COG4598 191 GEVLKVMRDLAEE-GRTMLVVTHEMGFA 217
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
34-233 |
1.24e-44 |
|
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: 147.53 E-value: 1.24e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 34 IFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNeeqRAEVRlKHIGFVFQSFQLLpHLT 113
Cdd:cd03228 17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLD---LESLR-KNIAYVPQDPFLF-SGT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 114 ALENVmlplrlqekfkyaeaeqkalnllkrvglerqaqqtpkvLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETAT 193
Cdd:cd03228 92 IRENI--------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEA 133
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 491113568 194 EIEQLLFELNRelGTTLVLVTHDPKLAAQCQRHYALIDGQ 233
Cdd:cd03228 134 LILEALRALAK--GKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
35-184 |
1.24e-44 |
|
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: 147.02 E-value: 1.24e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 35 FENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRaevrLKHIGFVFQSFQLLPHLTA 114
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSL----RKEIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491113568 115 LENVMLPLRLQEkFKYAEAEQKALNLLKRVGLE----RQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPT 184
Cdd:pfam00005 77 RENLRLGLLLKG-LSKREKDARAEEALEKLGLGdladRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
33-225 |
1.74e-44 |
|
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: 148.40 E-value: 1.74e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 33 TIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAevrlkHIGFVFQSFQLLPHL 112
Cdd:COG4133 16 LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRR-----RLAYLGHADGLKPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 113 TALENvmlpLRLQEKFKYAEAEQKALN-LLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGET 191
Cdd:COG4133 91 TVREN----LRFWAALYGLRADREAIDeALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAG 166
|
170 180 190
....*....|....*....|....*....|....
gi 491113568 192 ATEIEQLLFELnRELGTTLVLVTHDPKLAAQCQR 225
Cdd:COG4133 167 VALLAELIAAH-LARGGAVLLTTHQPLELAAARV 199
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
38-249 |
1.85e-44 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 149.13 E-value: 1.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 38 LNFD--IQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAevrlkhIGFVFQSFQLLPHLTAL 115
Cdd:COG3840 16 LRFDltIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERP------VSMLFQENNLFPHLTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 116 ENVMLPLRlqEKFKYAEAEQKALN-LLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETATE 194
Cdd:COG3840 90 QNIGLGLR--PGLKLTAEQRAQVEqALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491113568 195 IEQLLFELNRELGTTLVLVTHDPKLAAQCQRHYALI-DGQLVEQFaakPTAAITGG 249
Cdd:COG3840 168 MLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVaDGRIAADG---PTAALLDG 220
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
16-234 |
9.21e-44 |
|
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: 145.62 E-value: 9.21e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 16 ISAQNLTQKIqlaqKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRaevr 95
Cdd:cd03230 1 IEVRNLSKRY----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVK---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 96 lKHIGFVFQSFQLLPHLTALENVMlplrlqekfkyaeaeqkalnllkrvglerqaqqtpkvLSGGEQQRVAIARALIREP 175
Cdd:cd03230 73 -RRIGYLPEEPSLYENLTVRENLK-------------------------------------LSGGMKQRLALAQALLHDP 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 176 KIIFADEPTGNLDGETATEIEQLLFELNRElGTTLVLVTHDPKLAAQ-CQRHYALIDGQL 234
Cdd:cd03230 115 ELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
37-237 |
2.16e-43 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 146.70 E-value: 2.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 37 NLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESI---AELNEEQRAEVRlKHIGFVFQSFQLLPHLT 113
Cdd:COG4161 20 DINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIRLLR-QKVGMVFQQYNLWPHLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 114 ALENVM-LPLRLQEKFKyAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETA 192
Cdd:COG4161 99 VMENLIeAPCKVLGLSK-EQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEIT 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491113568 193 TEIEQLLFELNrELGTTLVLVTHDPKLAAQCQRHYA-LIDGQLVEQ 237
Cdd:COG4161 178 AQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVyMEKGRIIEQ 222
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
36-216 |
2.89e-43 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 148.32 E-value: 2.89e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 36 ENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEqraEVRlKHIGFVFQSFQLLPHLTAL 115
Cdd:COG1125 19 DDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPV---ELR-RRIGYVIQQIGLFPHMTVA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 116 ENVMLPLRLQeKFKYAEAEQKALNLLKRVGL--ERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETAT 193
Cdd:COG1125 95 ENIATVPRLL-GWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILLMDEPFGALDPITRE 173
|
170 180
....*....|....*....|...
gi 491113568 194 EIEQLLFELNRELGTTLVLVTHD 216
Cdd:COG1125 174 QLQDELLRLQRELGKTIVFVTHD 196
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
33-240 |
6.06e-43 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 145.71 E-value: 6.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 33 TIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAelneeqRAEVRLKHIGFVFQSFQLLPHL 112
Cdd:TIGR00968 14 QALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDAT------RVHARDRKIGFVFQHYALFKHL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 113 TALENVMLPLRLQeKFKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETA 192
Cdd:TIGR00968 88 TVRDNIAFGLEIR-KHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGALDAKVR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491113568 193 TEIEQLLFELNRELGTTLVLVTHDPKLAAQCQRHYALIDGQLVEQFAA 240
Cdd:TIGR00968 167 KELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGS 214
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
37-215 |
7.65e-43 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 148.30 E-value: 7.65e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 37 NLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAevrlkhIGFVFQSFQLLPHLTALE 116
Cdd:NF040840 18 DISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRG------IAYVYQNYMLFPHKTVFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 117 NVMLPLRLQeKFKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETATEIE 196
Cdd:NF040840 92 NIAFGLKLR-KVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELI 170
|
170
....*....|....*....
gi 491113568 197 QLLFELNRELGTTLVLVTH 215
Cdd:NF040840 171 REMKRWHREFGFTAIHVTH 189
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
11-246 |
1.01e-42 |
|
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: 151.76 E-value: 1.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 11 MPQTIISAQNLTQKIQLAQKQLTIFENLNFDIQEGEQVAITGRSGSGKS----TLLGILATLDQASSGKLVVCGESIAEL 86
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 87 NEEQRAEVRLKHIGFVFQ----SfqLLPHLTALENVMLPLRLQEKFKYAEAEQKALNLLKRVGL---ERQAQQTPKVLSG 159
Cdd:COG4172 82 SERELRRIRGNRIAMIFQepmtS--LNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIpdpERRLDAYPHQLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 160 GEQQRVAIARALIREPKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDPKLAAQ-CQRHYALIDGQLVEQf 238
Cdd:COG4172 160 GQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRfADRVAVMRQGEIVEQ- 238
|
....*...
gi 491113568 239 aaKPTAAI 246
Cdd:COG4172 239 --GPTAEL 244
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
16-237 |
1.48e-42 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 144.62 E-value: 1.48e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 16 ISAQNLTQKIqlaqKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRaevr 95
Cdd:COG4555 2 IEVENLSKKY----GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREAR---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 96 lKHIGFVFQSFQLLPHLTALENVMLPLRLQEKFKyAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREP 175
Cdd:COG4555 74 -RQIGVLPDERGLYDRLTVRENIRYFAELYGLFD-EELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491113568 176 KIIFADEPTGNLDGETATEIEQLLFELnRELGTTLVLVTHDPK-LAAQCQRHYALIDGQLVEQ 237
Cdd:COG4555 152 KVLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQeVEALCDRVVILHKGKVVAQ 213
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
37-237 |
1.51e-42 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 144.77 E-value: 1.51e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 37 NLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESI---AELNEEQRAEVRlKHIGFVFQSFQLLPHLT 113
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAIRELR-RNVGMVFQQYNLWPHLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 114 ALENVM-LPLRLQEKFKyAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETA 192
Cdd:PRK11124 99 VQQNLIeAPCRVLGLSK-DQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEIT 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491113568 193 TEIEQLLFELnRELGTTLVLVTHDPKLAAQCQRHYALID-GQLVEQ 237
Cdd:PRK11124 178 AQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMEnGHIVEQ 222
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
33-237 |
1.87e-42 |
|
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: 151.46 E-value: 1.87e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 33 TIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAEvrlkHIGFVFQSfqllPHL 112
Cdd:COG4987 349 PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRR----RIAVVPQR----PHL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 113 ---TALENvmlpLRLqekfkyA--EA-EQKALNLLKRVGLERQAQQTPK-----V------LSGGEQQRVAIARALIREP 175
Cdd:COG4987 421 fdtTLREN----LRL------ArpDAtDEELWAALERVGLGDWLAALPDgldtwLgeggrrLSGGERRRLALARALLRDA 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491113568 176 KIIFADEPTGNLDGETATEIEQLLFELNRelGTTLVLVTHDPKLAAQCQRHYALIDGQLVEQ 237
Cdd:COG4987 491 PILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLERMDRILVLEDGRIVEQ 550
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
24-216 |
2.11e-42 |
|
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: 144.02 E-value: 2.11e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 24 KIQLAQKQLTIFE--NLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRaevrlkHIGF 101
Cdd:cd03299 2 KVENLSKDWKEFKlkNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKR------DISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 102 VFQSFQLLPHLTALENVMLPLRLQEKFKyAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFAD 181
Cdd:cd03299 76 VPQNYALFPHMTVYKNIAYGLKKRKVDK-KEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLD 154
|
170 180 190
....*....|....*....|....*....|....*
gi 491113568 182 EPTGNLDGETATEIEQLLFELNRELGTTLVLVTHD 216
Cdd:cd03299 155 EPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHD 189
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
33-216 |
4.37e-42 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 144.05 E-value: 4.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 33 TIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRaevrlkhigFVFQSFQLLPHL 112
Cdd:PRK11247 26 TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTR---------LMFQDARLLPWK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 113 TALENVMLPLRLQEKfkyaeaeQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETA 192
Cdd:PRK11247 97 KVIDNVGLGLKGQWR-------DAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTR 169
|
170 180
....*....|....*....|....
gi 491113568 193 TEIEQLLFELNRELGTTLVLVTHD 216
Cdd:PRK11247 170 IEMQDLIESLWQQHGFTVLLVTHD 193
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
34-237 |
5.39e-42 |
|
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: 151.53 E-value: 5.39e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 34 IFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNeeqRAEVRlKHIGFVFQSFQLLpHLT 113
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQID---PASLR-RQIGVVLQDVFLF-SGT 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 114 ALENVMLplrlqekFKYAEAEQKALNLLKRVGLERQAQQTPK-----------VLSGGEQQRVAIARALIREPKIIFADE 182
Cdd:COG2274 565 IRENITL-------GDPDATDEEIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIARALLRNPRILILDE 637
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491113568 183 PTGNLDGETATEIEQLLFELNRelGTTLVLVTHDPKLAAQCQRHYALIDGQLVEQ 237
Cdd:COG2274 638 ATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRLADRIIVLDKGRIVED 690
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
50-216 |
5.95e-42 |
|
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: 145.71 E-value: 5.95e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 50 ITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRaevrlkHIGFVFQSFQLLPHLTALENVMLPLRLQeKFK 129
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLR------HINMVFQSYALFPHMTVEENVAFGLKMR-KVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 130 YAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETATEIEQLLFELNRELGTT 209
Cdd:TIGR01187 74 RAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGIT 153
|
....*..
gi 491113568 210 LVLVTHD 216
Cdd:TIGR01187 154 FVFVTHD 160
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
36-216 |
1.74e-41 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 142.69 E-value: 1.74e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 36 ENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQraevrlkhiGFVFQSFQLLPHLTAL 115
Cdd:COG4525 24 QDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR---------GVVFQKDALLPWLNVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 116 ENVMLPLRLQeKFKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETATEI 195
Cdd:COG4525 95 DNVAFGLRLR-GVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQM 173
|
170 180
....*....|....*....|.
gi 491113568 196 EQLLFELNRELGTTLVLVTHD 216
Cdd:COG4525 174 QELLLDVWQRTGKGVFLITHS 194
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
33-237 |
2.53e-41 |
|
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: 139.49 E-value: 2.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 33 TIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAevrlKHIGFVFQSfqllphl 112
Cdd:cd03214 13 TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELA----RKIAYVPQA------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 113 talenvmlplrlqekfkyaeaeqkalnlLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETA 192
Cdd:cd03214 82 ----------------------------LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQ 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491113568 193 TEIEQLLFELNRELGTTLVLVTHDPKLAAQ-CQRHYALIDGQLVEQ 237
Cdd:cd03214 134 IELLELLRRLARERGKTVVMVLHDLNLAARyADRVILLKDGRIVAQ 179
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
16-237 |
4.36e-41 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 141.80 E-value: 4.36e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 16 ISAQNLTQKIQLAQKQltIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGesIAELNEEQRAEVR 95
Cdd:TIGR04520 1 IEVENVSFSYPESEKP--ALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENLWEIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 96 lKHIGFVFQ---------------SFqllphltALENVMLPlrlqekfkYAEAEQKALNLLKRVGLERQAQQTPKVLSGG 160
Cdd:TIGR04520 77 -KKVGMVFQnpdnqfvgatveddvAF-------GLENLGVP--------REEMRKRVDEALKLVGMEDFRDREPHLLSGG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491113568 161 EQQRVAIARALIREPKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDPKLAAQCQRHYALIDGQLVEQ 237
Cdd:TIGR04520 141 QKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAE 217
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
24-237 |
7.21e-41 |
|
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: 143.25 E-value: 7.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 24 KIQLAQKQL---TIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRaevrlkHIG 100
Cdd:TIGR03265 6 SIDNIRKRFgafTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKR------DYG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 101 FVFQSFQLLPHLTALENVMLPLRLQeKFKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFA 180
Cdd:TIGR03265 80 IVFQSYALFPNLTVADNIAYGLKNR-GMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491113568 181 DEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDPKLAAQCQRHYALIDGQLVEQ 237
Cdd:TIGR03265 159 DEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQ 215
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
13-217 |
2.81e-40 |
|
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: 138.34 E-value: 2.81e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 13 QTIISAQNLTQKIQLAQ---KQLTIFENLNFDIQEGEQVAITGRSGSGKSTLL-GILATLdQASSGKLVVCGES----IA 84
Cdd:COG4778 2 TTLLEVENLSKTFTLHLqggKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLkCIYGNY-LPDSGSILVRHDGgwvdLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 85 ELNEEQRAEVRLKHIGFVFQSFQLLPHLTALENVMLPLRLQEkFKYAEAEQKALNLLKRVGL-ERQAQQTPKVLSGGEQQ 163
Cdd:COG4778 81 QASPREILALRRRTIGYVSQFLRVIPRVSALDVVAEPLLERG-VDREEARARARELLARLNLpERLWDLPPATFSGGEQQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491113568 164 RVAIARALIREPKIIFADEPTGNLDGETATEIEQLLFELNRElGTTLVLVTHDP 217
Cdd:COG4778 160 RVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDE 212
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
33-237 |
3.91e-40 |
|
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: 145.29 E-value: 3.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 33 TIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAevrlKHIGFVFQSfQLLPHL 112
Cdd:COG4988 351 PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWR----RQIAWVPQN-PYLFAG 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 113 TALENvmlpLRLQEkfkyAEAEQKALN-LLKRVGLERQAQQTPKV-----------LSGGEQQRVAIARALIREPKIIFA 180
Cdd:COG4988 426 TIREN----LRLGR----PDASDEELEaALEAAGLDEFVAALPDGldtplgeggrgLSGGQAQRLALARALLRDAPLLLL 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491113568 181 DEPTGNLDGETATEIEQLLFELNRelGTTLVLVTHDPKLAAQCQRHYALIDGQLVEQ 237
Cdd:COG4988 498 DEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQADRILVLDDGRIVEQ 552
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
36-237 |
5.08e-40 |
|
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: 139.12 E-value: 5.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 36 ENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAEVRlKHIGFVFQsF---QLLpHL 112
Cdd:TIGR04521 22 DDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLR-KKVGLVFQ-FpehQLF-EE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 113 TALENVML-PLRLqeKFKYAEAEQKALNLLKRVGLERQ-AQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGE 190
Cdd:TIGR04521 99 TVYKDIAFgPKNL--GLSEEEAEERVKEALELVGLDEEyLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPK 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491113568 191 TATEIEQLLFELNRELGTTLVLVTHDPKLAAQ-CQRHYALIDGQLVEQ 237
Cdd:TIGR04521 177 GRKEILDLFKRLHKEKGLTVILVTHSMEDVAEyADRVIVMHKGKIVLD 224
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
33-235 |
7.22e-40 |
|
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: 136.89 E-value: 7.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 33 TIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNeeqraevrlKHIGFVFQSFQLLPH- 111
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER---------KRIGYVPQRRSIDRDf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 112 -LTALENVMLPL----RLQEKFKyAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGN 186
Cdd:cd03235 84 pISVRDVVLMGLyghkGLFRRLS-KADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491113568 187 LDGETATEIEQLLFELNRElGTTLVLVTHDPKLAAQCQRHYALIDGQLV 235
Cdd:cd03235 163 VDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
12-216 |
1.64e-39 |
|
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: 137.09 E-value: 1.64e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 12 PQTIISAQNLTqkiqlaqKQ---LTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNE 88
Cdd:COG0411 1 SDPLLEVRGLT-------KRfggLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 89 EQRAevrlkHIGFV--FQSFQLLPHLTALENVMLPLRLQEKFKY--------------AEAEQKALNLLKRVGLERQAQQ 152
Cdd:COG0411 74 HRIA-----RLGIArtFQNPRLFPELTVLENVLVAAHARLGRGLlaallrlprarreeREARERAEELLERVGLADRADE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491113568 153 TPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHD 216
Cdd:COG0411 149 PAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHD 212
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
32-216 |
3.70e-39 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 135.64 E-value: 3.70e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 32 LTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAevRLKhIGFVFQSFQLLPH 111
Cdd:cd03219 13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIA--RLG-IGRTFQIPRLFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 112 LTALENVMLPLRLQEK---------FKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADE 182
Cdd:cd03219 90 LTVLENVMVAAQARTGsglllararREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDE 169
|
170 180 190
....*....|....*....|....*....|....
gi 491113568 183 PTGNLDGETATEIEQLLFELNRElGTTLVLVTHD 216
Cdd:cd03219 170 PAAGLNPEETEELAELIRELRER-GITVLLVEHD 202
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
14-237 |
1.76e-38 |
|
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: 134.93 E-value: 1.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 14 TIISAQNLTQKIQL-----AQKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNE 88
Cdd:TIGR02769 1 SLLEVRDVTHTYRTgglfgAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 89 EQRAEVRlKHIGFVFQSF--QLLPHLTALENVMLPLRLQEKFKYAEAEQKALNLLKRVGLERQ-AQQTPKVLSGGEQQRV 165
Cdd:TIGR02769 81 KQRRAFR-RDVQLVFQDSpsAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEdADKLPRQLSGGQLQRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491113568 166 AIARALIREPKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDPKLAAQ-CQRHYALIDGQLVEQ 237
Cdd:TIGR02769 160 NIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEE 232
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
33-233 |
1.86e-38 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 131.60 E-value: 1.86e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 33 TIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRaevrLKHIGFVFQsfqllphl 112
Cdd:cd00267 13 TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL----RRRIGYVPQ-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 113 talenvmlplrlqekfkyaeaeqkalnllkrvglerqaqqtpkvLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETA 192
Cdd:cd00267 81 --------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASR 116
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 491113568 193 TEIEQLLFELNRElGTTLVLVTHDPKLAAQ-CQRHYALIDGQ 233
Cdd:cd00267 117 ERLLELLRELAEE-GRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
34-216 |
3.28e-38 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 136.70 E-value: 3.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 34 IFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAevrlkhIGFVFQSFQLLPHLT 113
Cdd:PRK11000 18 ISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERG------VGMVFQSYALYPHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 114 ALENVMLPLRLQeKFKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETAT 193
Cdd:PRK11000 92 VAENMSFGLKLA-GAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRV 170
|
170 180
....*....|....*....|...
gi 491113568 194 EIEQLLFELNRELGTTLVLVTHD 216
Cdd:PRK11000 171 QMRIEISRLHKRLGRTMIYVTHD 193
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
23-217 |
4.02e-38 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 132.22 E-value: 4.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 23 QKIQLAQKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLG-ILATLDQA--SSGKLVVCGESIAELNEEQRaevrlkHI 99
Cdd:COG4136 5 ENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAaIAGTLSPAfsASGEVLLNGRRLTALPAEQR------RI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 100 GFVFQSFQLLPHLTALENvmLPLRLQEKFKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIF 179
Cdd:COG4136 79 GILFQDDLLFPHLSVGEN--LAFALPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALL 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 491113568 180 ADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDP 217
Cdd:COG4136 157 LDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDE 194
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
29-237 |
8.45e-38 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 133.04 E-value: 8.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 29 QKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAevrlKHIGFVFQ--SF 106
Cdd:COG4167 23 RQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRC----KHIRMIFQdpNT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 107 QLLPHLTALENVMLPLRLQEKFKYAEAEQKALNLLKRVGLER-QAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTG 185
Cdd:COG4167 99 SLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLLPeHANFYPHMLSSGQKQRVALARALILQPKIIIADEALA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491113568 186 NLDGETATEIEQLLFELNRELGTTLVLVTHDPKLAaqcqRHYA-----LIDGQLVEQ 237
Cdd:COG4167 179 ALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIV----KHISdkvlvMHQGEVVEY 231
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
35-235 |
1.66e-37 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 131.15 E-value: 1.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 35 FENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAEVRlKHIGFVFQSFQLLPHLTA 114
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLR-RQIGMIFQDHHLLMDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 115 LENVMLPLRLQEKfKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETATE 194
Cdd:PRK10908 97 YDNVAIPLIIAGA-SGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491113568 195 IEQLLFELNReLGTTLVLVTHDPKLAAqcQRHY---ALIDGQLV 235
Cdd:PRK10908 176 ILRLFEEFNR-VGVTVLMATHDIGLIS--RRSYrmlTLSDGHLH 216
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
40-216 |
2.47e-37 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 133.32 E-value: 2.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 40 FDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAEVRlKHIGFVFQ----SfqLLPHLTAL 115
Cdd:COG4608 39 FDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLR-RRMQMVFQdpyaS--LNPRMTVG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 116 ENVMLPLRLQEKFKYAEAEQKALNLLKRVGLER-QAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETATE 194
Cdd:COG4608 116 DIIAEPLRIHGLASKAERRERVAELLELVGLRPeHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQ 195
|
170 180
....*....|....*....|..
gi 491113568 195 IEQLLFELNRELGTTLVLVTHD 216
Cdd:COG4608 196 VLNLLEDLQDELGLTYLFISHD 217
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
29-235 |
2.59e-37 |
|
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: 130.49 E-value: 2.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 29 QKQLTIFE-NLNFDIqEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAEVRLKHIGFVFQSFQ 107
Cdd:cd03297 7 EKRLPDFTlKIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 108 LLPHLTALENVMLPLRLQEKfkyAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNL 187
Cdd:cd03297 86 LFPHLNVRENLAFGLKRKRN---REDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSAL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491113568 188 DGETATEIEQLLFELNRELGTTLVLVTHDP-KLAAQCQRHYALIDGQLV 235
Cdd:cd03297 163 DRALRLQLLPELKQIKKNLNIPVIFVTHDLsEAEYLADRIVVMEDGRLQ 211
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
16-235 |
6.89e-37 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 129.41 E-value: 6.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 16 ISAQNLTQKIQlaqkQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAElneeQRAEVR 95
Cdd:cd03265 1 IEVENLVKKYG----DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR----EPREVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 96 lKHIGFVFQSFQLLPHLTALENVMLPLRLQeKFKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREP 175
Cdd:cd03265 73 -RRIGIVFQDLSVDDELTGWENLYIHARLY-GVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491113568 176 KIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDPKLAAQCQRHYALID-GQLV 235
Cdd:cd03265 151 EVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDhGRII 211
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
31-241 |
1.16e-36 |
|
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: 128.71 E-value: 1.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 31 QLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAEvrlKHIGFVFQSFQLLP 110
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERAR---AGIGYVPEGRRIFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 111 HLTALENVMLPLRLQEKFKYAEAEQKALNLLKRVGlERQAQQTpKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGE 190
Cdd:cd03224 89 ELTVEENLLLGAYARRRAKRKARLERVYELFPRLK-ERRKQLA-GTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPK 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491113568 191 TATEIEQLLFELNRElGTTLVLVTHDPKLAAQ-CQRHYALIDGQLVEQFAAK 241
Cdd:cd03224 167 IVEEIFEAIRELRDE-GVTILLVEQNARFALEiADRAYVLERGRVVLEGTAA 217
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
30-223 |
1.71e-36 |
|
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: 127.76 E-value: 1.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 30 KQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAelneeqrAEVRLKHIGFVFQS--FQ 107
Cdd:cd03226 11 KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK-------AKERRKSIGYVMQDvdYQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 108 LLphltaLENVMLPLRLQEKFKYAEAEQKAlNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNL 187
Cdd:cd03226 84 LF-----TDSVREELLLGLKELDAGNEQAE-TVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGL 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 491113568 188 DGETATEIEQLLFELNRElGTTLVLVTHDPKLAAQC 223
Cdd:cd03226 158 DYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKV 192
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
36-216 |
5.51e-36 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 127.58 E-value: 5.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 36 ENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAevrlkhigfVFQSFQLLPHLTAL 115
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV---------VFQNYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 116 ENVMLPL-RLQEKFKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETATE 194
Cdd:TIGR01184 73 ENIALAVdRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180
....*....|....*....|..
gi 491113568 195 IEQLLFELNRELGTTLVLVTHD 216
Cdd:TIGR01184 153 LQEELMQIWEEHRVTVLMVTHD 174
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
13-234 |
7.71e-36 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 127.82 E-value: 7.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 13 QTIISAQNLTQKIQlaqkQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATL---DQASSGKLVVCGESIAELNEE 89
Cdd:PRK09984 2 QTIIRVEKLAKTFN----QHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 90 QRaEVRLK--HIGFVFQSFQLLPHLTALENVML------PL-RLQEKFKYAEAEQKALNLLKRVGLERQAQQTPKVLSGG 160
Cdd:PRK09984 78 AR-DIRKSraNTGYIFQQFNLVNRLSVLENVLIgalgstPFwRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491113568 161 EQQRVAIARALIREPKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDPKLAAQ-CQRHYALIDGQL 234
Cdd:PRK09984 157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRyCERIVALRQGHV 231
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
14-236 |
1.44e-35 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 127.50 E-value: 1.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 14 TIISAQNL-----TQKIQLAQKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNE 88
Cdd:PRK10419 2 TLLNVSGLshhyaHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 89 EQRAEVRlKHIGFVFQ-SFQLL-PHLTALENVMLPLRLQEKFKYAEAEQKALNLLKRVGL-ERQAQQTPKVLSGGEQQRV 165
Cdd:PRK10419 82 AQRKAFR-RDIQMVFQdSISAVnPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491113568 166 AIARALIREPKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDPKLAAQ-CQRHYALIDGQLVE 236
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
16-237 |
1.72e-35 |
|
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: 132.23 E-value: 1.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 16 ISAQNLTQKIqlaqKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQ--ASSGKLV---------------- 77
Cdd:TIGR03269 1 IEVKNLTKKF----DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIyhvalcekcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 78 -------VCGESIAE-------LNEEQRAEVRlKHIGFVFQ-SFQLLPHLTALENVMLPLRlQEKFKYAEAEQKALNLLK 142
Cdd:TIGR03269 77 kvgepcpVCGGTLEPeevdfwnLSDKLRRRIR-KRIAIMLQrTFALYGDDTVLDNVLEALE-EIGYEGKEAVGRAVDLIE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 143 RVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDPKLAAQ 222
Cdd:TIGR03269 155 MVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIED 234
|
250
....*....|....*.
gi 491113568 223 CQRHYALID-GQLVEQ 237
Cdd:TIGR03269 235 LSDKAIWLEnGEIKEE 250
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
37-237 |
3.49e-35 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 124.91 E-value: 3.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 37 NLNFDIQ--EGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAevrlkhIGFVFQSFQLLPHLTA 114
Cdd:cd03298 14 PMHFDLTfaQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP------VSMLFQENNLFAHLTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 115 LENVMLPLRLQEKFKyAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETATE 194
Cdd:cd03298 88 EQNVGLGLSPGLKLT-AEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491113568 195 IEQLLFELNRELGTTLVLVTHDPKLAAQC-QRHYALIDGQLVEQ 237
Cdd:cd03298 167 MLDLVLDLHAETKMTVLMVTHQPEDAKRLaQRVVFLDNGRIAAQ 210
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
33-216 |
6.62e-35 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 127.53 E-value: 6.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 33 TIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRaevrlkHIGFVFQSFQLLPHL 112
Cdd:PRK11432 20 TVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQR------DICMVFQSYALFPHM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 113 TALENVMLPLRLQEKFKyAEAEQK---ALNLLKRVGLE-RQAQQtpkvLSGGEQQRVAIARALIREPKIIFADEPTGNLD 188
Cdd:PRK11432 94 SLGENVGYGLKMLGVPK-EERKQRvkeALELVDLAGFEdRYVDQ----ISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
170 180
....*....|....*....|....*...
gi 491113568 189 GETATEIEQLLFELNRELGTTLVLVTHD 216
Cdd:PRK11432 169 ANLRRSMREKIRELQQQFNITSLYVTHD 196
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
33-215 |
7.53e-35 |
|
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: 124.81 E-value: 7.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 33 TIFENLNFDIQEGEQVAITGRSGSGKSTLLGILAT-LDQASSGKLVVCGEsiaELNEEQRAEVRlKHIGFVFQSFQ--LL 109
Cdd:COG1119 17 TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVRLFGE---RRGGEDVWELR-KRIGLVSPALQlrFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 110 PHLTALENVM--------LPLRLQEkfkyaEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFAD 181
Cdd:COG1119 93 RDETVLDVVLsgffdsigLYREPTD-----EQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILD 167
|
170 180 190
....*....|....*....|....*....|....
gi 491113568 182 EPTGNLDGETATEIEQLLFELNRELGTTLVLVTH 215
Cdd:COG1119 168 EPTAGLDLGARELLLALLDKLAAEGAPTLVLVTH 201
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
37-246 |
1.10e-34 |
|
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: 129.80 E-value: 1.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 37 NLNFDIQEGEQVAITGRSGSGKSTL-LGILATLDqaSSGKLVVCGESIAELNEEQRAEVRlKHIGFVFQ----SfqLLPH 111
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTLgLALLRLIP--SEGEIRFDGQDLDGLSRRALRPLR-RRMQVVFQdpfgS--LSPR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 112 LTALENVMLPLRLQE-KFKYAEAEQKALNLLKRVGLERQAQQT-PKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDG 189
Cdd:COG4172 379 MTVGQIIAEGLRVHGpGLSAAERRARVAEALEEVGLDPAARHRyPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDV 458
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 190 ETATEIEQLLFELNRELGTTLVLVTHDpkLA---AQCQRHYALIDGQLVEQfaaKPTAAI 246
Cdd:COG4172 459 SVQAQILDLLRDLQREHGLAYLFISHD--LAvvrALAHRVMVMKDGKVVEQ---GPTEQV 513
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
16-235 |
1.20e-34 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 123.38 E-value: 1.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 16 ISAQNLTQKiqLAQKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAelneEQRAEVR 95
Cdd:cd03263 1 LQIRNLTKT--YKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR----TDRKAAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 96 lKHIGFVFQSFQLLPHLTALENVMLPLRLQEKFKyAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREP 175
Cdd:cd03263 75 -QSLGYCPQFDALFDELTVREHLRFYARLKGLPK-SEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491113568 176 KIIFADEPTGNLDGETATEIEQLLFELNRelGTTLVLVTHDPKLAAQ-CQRHYALIDGQLV 235
Cdd:cd03263 153 SVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEAlCDRIAIMSDGKLR 211
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
16-234 |
1.42e-34 |
|
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: 121.94 E-value: 1.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 16 ISAQNLTqkIQLAQKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAevr 95
Cdd:cd03246 1 LEVENVS--FRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELG--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 96 lKHIGFVFQSFQLLPHlTALENvmlplrlqekfkyaeaeqkalnllkrvglerqaqqtpkVLSGGEQQRVAIARALIREP 175
Cdd:cd03246 76 -DHVGYLPQDDELFSG-SIAEN--------------------------------------ILSGGQRQRLGLARALYGNP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491113568 176 KIIFADEPTGNLDGETATEIEQLLFELnRELGTTLVLVTHDPKLAAQCQRHYALIDGQL 234
Cdd:cd03246 116 RILVLDEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
36-220 |
2.98e-34 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 126.49 E-value: 2.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 36 ENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAevrlkhIGFVFQSFQLLPHLTAL 115
Cdd:PRK11607 36 DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRP------INMMFQSYALFPHMTVE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 116 ENVMLPLRlQEKFKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETATEI 195
Cdd:PRK11607 110 QNIAFGLK-QDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRM 188
|
170 180
....*....|....*....|....*
gi 491113568 196 EQLLFELNRELGTTLVLVTHDPKLA 220
Cdd:PRK11607 189 QLEVVDILERVGVTCVMVTHDQEEA 213
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
34-237 |
1.11e-33 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 122.38 E-value: 1.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 34 IFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESI-------AELNEEQRAEVRL--KHIGFVFQ 104
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdGQLKVADKNQLRLlrTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 105 SFQLLPHLTALENVM-LPLRLQEKFKyAEAEQKALNLLKRVGL-ERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADE 182
Cdd:PRK10619 100 HFNLWSHMTVLENVMeAPIQVLGLSK-QEARERAVKYLAKVGIdERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491113568 183 PTGNLDGETATEIEQLLFELNRElGTTLVLVTHDPKLAAQCQRHYALIDGQLVEQ 237
Cdd:PRK10619 179 PTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEE 232
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
20-217 |
1.58e-33 |
|
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: 120.84 E-value: 1.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 20 NLTQKIQLAQKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQ---ASSGKLVVCGEsiaelnEEQRAEVRl 96
Cdd:cd03234 8 DVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQ------PRKPDQFQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 97 KHIGFVFQSFQLLPHLTALENV--MLPLRLQEKFKYAEAEQK-ALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIR 173
Cdd:cd03234 81 KCVAYVRQDDILLPGLTVRETLtyTAILRLPRKSSDAIRKKRvEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLW 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 491113568 174 EPKIIFADEPTGNLDGETATEIEQLLFELNRelGTTLVLVT-HDP 217
Cdd:cd03234 161 DPKVLILDEPTSGLDSFTALNLVSTLSQLAR--RNRIVILTiHQP 203
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
37-237 |
2.73e-33 |
|
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: 120.86 E-value: 2.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 37 NLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQA-----SSGKLVVCGESIaelNEEQRAEVRL-KHIGFVFQSFQLLP 110
Cdd:TIGR00972 19 NINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDLvpgvrIEGKVLFDGQDI---YDKKIDVVELrRRVGMVFQKPNPFP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 111 hLTALENVMLPLRLQEKFKYAEAEQKALNLLKRVGL----ERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGN 186
Cdd:TIGR00972 96 -MSIYDNIAYGPRLHGIKDKKELDEIVEESLKKAALwdevKDRLHDSALGLSGGQQQRLCIARALAVEPEVLLLDEPTSA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491113568 187 LDGETATEIEQLLFELNRELgtTLVLVTHDPKLAAQCQRHYALI-DGQLVEQ 237
Cdd:TIGR00972 175 LDPIATGKIEELIQELKKKY--TIVIVTHNMQQAARISDRTAFFyDGELVEY 224
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
37-235 |
4.42e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 120.95 E-value: 4.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 37 NLNFDIQEGEQVAITGRSGSGKSTLL----GILatldQASSGKLVVCGESIaELNEEQRAEVRlKHIGFVFQS--FQLLP 110
Cdd:PRK13639 20 GINFKAEKGEMVALLGPNGAGKSTLFlhfnGIL----KPTSGEVLIKGEPI-KYDKKSLLEVR-KTVGIVFQNpdDQLFA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 111 HlTALENVML-PLRLqeKFKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDG 189
Cdd:PRK13639 94 P-TVEEDVAFgPLNL--GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491113568 190 ETATEIEQLLFELNRElGTTLVLVTHDPKLAA-QCQRHYALIDGQLV 235
Cdd:PRK13639 171 MGASQIMKLLYDLNKE-GITIIISTHDVDLVPvYADKVYVMSDGKII 216
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
37-243 |
7.85e-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: 7.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 37 NLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNeeqRAEVRLKHIGFVFQSFQLLPHLTALE 116
Cdd:COG1129 22 GVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRS---PRDAQAAGIAIIHQELNLVPNLSVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 117 NVMLPlRLQEKF---KYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLdgeTAT 193
Cdd:COG1129 99 NIFLG-REPRRGgliDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASL---TER 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491113568 194 EIEQlLFELNREL---GTTLVLVTHdpKLA---AQCQRHYALIDGQLVEQFAAKPT 243
Cdd:COG1129 175 EVER-LFRIIRRLkaqGVAIIYISH--RLDevfEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
30-216 |
8.18e-33 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 121.74 E-value: 8.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 30 KQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAEVRlKHIGFVFQS--FQ 107
Cdd:PRK15079 32 KTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVR-SDIQMIFQDplAS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 108 LLPHLTALENVMLPLRL-QEKFKYAEAEQKALNLLKRVGL-ERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTG 185
Cdd:PRK15079 111 LNPRMTIGEIIAEPLRTyHPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 190
|
170 180 190
....*....|....*....|....*....|.
gi 491113568 186 NLDGETATEIEQLLFELNRELGTTLVLVTHD 216
Cdd:PRK15079 191 ALDVSIQAQVVNLLQQLQREMGLSLIFIAHD 221
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
24-217 |
1.22e-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: 121.75 E-value: 1.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 24 KIQLAQKQLTIfeNLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGE----SIAELNE--EQRaevrlk 97
Cdd:COG4148 6 DFRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdSARGIFLppHRR------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 98 HIGFVFQSFQLLPHLTALENvmlpLRLQEKFKYAEAEQKALN-LLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPK 176
Cdd:COG4148 78 RIGYVFQEARLFPHLSVRGN----LLYGRKRAPRAERRISFDeVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPR 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 491113568 177 IIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDP 217
Cdd:COG4148 154 LLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSL 194
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
28-235 |
1.24e-32 |
|
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: 118.46 E-value: 1.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 28 AQKQLTIfENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNeeqRAEVRlKHIGFVFQSfq 107
Cdd:cd03245 14 NQEIPAL-DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLD---PADLR-RNIGYVPQD-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 108 llPHL---TALENVML--PL----RLQEKFKYAEAEQKALNLLKrvGLERQAQQTPKVLSGGEQQRVAIARALIREPKII 178
Cdd:cd03245 87 --VTLfygTLRDNITLgaPLaddeRILRAAELAGVTDFVNKHPN--GLDLQIGERGRGLSGGQRQAVALARALLNDPPIL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491113568 179 FADEPTGNLDGETATEIEQLLFELNRelGTTLVLVTHDPKLAAQCQRHYALIDGQLV 235
Cdd:cd03245 163 LLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
19-236 |
1.40e-32 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 122.45 E-value: 1.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 19 QNLTQKIQLAQKQLTI-FENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAEVRLK 97
Cdd:PRK10070 27 QGLSKEQILEKTGLSLgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 98 HIGFVFQSFQLLPHLTALENVMLPLRLQeKFKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKI 177
Cdd:PRK10070 107 KIAMVFQSFALMPHMTVLDNTAFGMELA-GINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDI 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 178 IFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDPKLAAQCQRHYALI-DGQLVE 236
Cdd:PRK10070 186 LLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMqNGEVVQ 245
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
34-237 |
1.81e-32 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 124.12 E-value: 1.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 34 IFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNeeqRAEVRlKHIGFVFQSFQLLpHLT 113
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLT---LESLR-RQIGVVPQDTFLF-SGT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 114 ALENVMLPL------RLQEKFKYAEAEQKALNLLK----RVGlERQAQqtpkvLSGGEQQRVAIARALIREPKIIFADEP 183
Cdd:COG1132 430 IRENIRYGRpdatdeEVEEAAKAAQAHEFIEALPDgydtVVG-ERGVN-----LSGGQRQRIAIARALLKDPPILILDEA 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491113568 184 TGNLDGETATEIEQLLFELNRelGTTLVLVTHDPKLAAQCQRHYALIDGQLVEQ 237
Cdd:COG1132 504 TSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRNADRILVLDDGRIVEQ 555
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
36-236 |
5.93e-32 |
|
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: 122.22 E-value: 5.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 36 ENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKL-VVCGES---IAELNEEQRAEVRlKHIGFVFQSFQLLPH 111
Cdd:TIGR03269 301 DNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnVRVGDEwvdMTKPGPDGRGRAK-RYIGILHQEYDLYPH 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 112 LTALENVMLPLRLQEKFKYAEaeQKALNLLKRVGL-ERQAQQT----PKVLSGGEQQRVAIARALIREPKIIFADEPTGN 186
Cdd:TIGR03269 380 RTVLDNLTEAIGLELPDELAR--MKAVITLKMVGFdEEKAEEIldkyPDELSEGERHRVALAQVLIKEPRIVILDEPTGT 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491113568 187 LDGETATEIEQLLFELNRELGTTLVLVTHDPKLAAQ-CQRHYALIDGQLVE 236
Cdd:TIGR03269 458 MDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDvCDRAALMRDGKIVK 508
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
37-237 |
6.85e-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: 116.70 E-value: 6.85e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 37 NLNFDIQEGEQVAITGRSGSGKST----LLGILATLDQASSGKLVVCGESIAELneeqraEVRLKHIGFVFQSFQ--LLP 110
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSLtclaILGLLPPGLTQTSGEILLDGRPLLPL------SIRGRHIATIMQNPRtaFNP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 111 HLTALENVMLPLRLQEKFkYAEAEQKALNLLKRVGLERQAQ---QTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNL 187
Cdd:TIGR02770 78 LFTMGNHAIETLRSLGKL-SKQARALILEALEAVGLPDPEEvlkKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491113568 188 DGETATEIEQLLFELNRELGTTLVLVTHDPKLAAQCQRHYALID-GQLVEQ 237
Cdd:TIGR02770 157 DVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDdGRIVER 207
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
5-242 |
2.05e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 116.63 E-value: 2.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 5 TKESNIMpqtiISAQNLTQKIQLAQKQLtiFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGEsia 84
Cdd:PRK13632 1 IKNKSVM----IKVENVSFSYPNSENNA--LKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGI--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 85 ELNEEQRAEVRlKHIGFVFQSfqllPH-----LTA-------LENVMLPlrlQEKFKyaeaeQKALNLLKRVGLERQAQQ 152
Cdd:PRK13632 72 TISKENLKEIR-KKIGIIFQN----PDnqfigATVeddiafgLENKKVP---PKKMK-----DIIDDLAKKVGMEDYLDK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 153 TPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDPKLAAQCQRHYALIDG 232
Cdd:PRK13632 139 EPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEG 218
|
250
....*....|
gi 491113568 233 QLVEQfaAKP 242
Cdd:PRK13632 219 KLIAQ--GKP 226
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
37-225 |
3.77e-31 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 120.08 E-value: 3.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 37 NLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRaevrLKHIGFVFQSFQLLPHlTALE 116
Cdd:TIGR02857 340 PVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW----RDQIAWVPQHPFLFAG-TIAE 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 117 NVMLPLRLQEKFKYAEAEQKA--LNLLK--RVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETA 192
Cdd:TIGR02857 415 NIRLARPDASDAEIREALERAglDEFVAalPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETE 494
|
170 180 190
....*....|....*....|....*....|...
gi 491113568 193 TEIEQLLFELNRelGTTLVLVTHDPKLAAQCQR 225
Cdd:TIGR02857 495 AEVLEALRALAQ--GRTVLLVTHRLALAALADR 525
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
36-216 |
4.62e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 116.08 E-value: 4.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 36 ENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESI-AELNEEQRAEVRlKHIGFVFQ--SFQLLPHl 112
Cdd:PRK13641 24 DNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItPETGNKNLKKLR-KKVSLVFQfpEAQLFEN- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 113 TALENVML-PLRLqeKFKYAEAEQKALNLLKRVGL-ERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGE 190
Cdd:PRK13641 102 TVLKDVEFgPKNF--GFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPE 179
|
170 180
....*....|....*....|....*.
gi 491113568 191 TATEIEQLLFELNRElGTTLVLVTHD 216
Cdd:PRK13641 180 GRKEMMQLFKDYQKA-GHTVILVTHN 204
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-241 |
5.98e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 115.01 E-value: 5.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 13 QTIISAQNLtqKIQLAQKQltIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATL-----DQASSGKLVVCGESIAELN 87
Cdd:PRK14247 1 MNKIEIRDL--KVSFGQVE--VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 88 eeqRAEVRlKHIGFVFQSFQLLPHLTALENVMLPLRLQEKFKY-AEAEQKALNLLKRVGLERQAQQTPKV----LSGGEQ 162
Cdd:PRK14247 77 ---VIELR-RRVQMVFQIPNPIPNLSIFENVALGLKLNRLVKSkKELQERVRWALEKAQLWDEVKDRLDApagkLSGGQQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 163 QRVAIARALIREPKIIFADEPTGNLDGETATEIEQLLFELNRELgtTLVLVTHDPKLAAQCQRHYA-LIDGQLVEQFAAK 241
Cdd:PRK14247 153 QRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAfLYKGQIVEWGPTR 230
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
15-215 |
6.53e-31 |
|
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: 114.00 E-value: 6.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 15 IISAQNLTQKIQLAQKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAElneeQRAEV 94
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK----EPAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 95 RLKhIGFVFQSFQLLPHLTALENVMLPLRLQeKFKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIRE 174
Cdd:cd03266 77 RRR-LGFVSDSTGLYDRLTARENLEYFAGLY-GLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 491113568 175 PKIIFADEPTGNLDGETATEIEQLLFELnRELGTTLVLVTH 215
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTH 194
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
39-249 |
7.69e-31 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 113.91 E-value: 7.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 39 NFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAevrlkhIGFVFQSFQLLPHLTALENV 118
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRP------VSMLFQENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 119 ML---P-LRLqekfkyaEAEQKAL--NLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETA 192
Cdd:PRK10771 93 GLglnPgLKL-------NAAQREKlhAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491113568 193 TEIEQLLFELNRELGTTLVLVTHDPKLAAQ-CQRHYALIDGQLVEQfaaKPTAAITGG 249
Cdd:PRK10771 166 QEMLTLVSQVCQERQLTLLMVSHSLEDAARiAPRSLVVADGRIAWD---GPTDELLSG 220
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-236 |
9.19e-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: 9.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 1 MTQNTKESNimpqTIISAQNLTqkIQLAQKQltIFENLNFDIQEGEQVAITGRSGSGKSTLL----GILATLDQAS-SGK 75
Cdd:COG1117 1 MTAPASTLE----PKIEVRNLN--VYYGDKQ--ALKDINLDIPENKVTALIGPSGCGKSTLLrclnRMNDLIPGARvEGE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 76 LVVCGESIAELNEEQrAEVRlKHIGFVFQSFQLLPHlTALENVMLPLRLQEKFKYAEAEQKALNLLKRVG--------LE 147
Cdd:COG1117 73 ILLDGEDIYDPDVDV-VELR-RRVGMVFQKPNPFPK-SIYDNVAYGLRLHGIKSKSELDEIVEESLRKAAlwdevkdrLK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 148 RQAQQtpkvLSGGEQQRVAIARALIREPKIIFADEPTGNLD-GETATeIEQLLFELNRELgtTLVLVTHDPKLAAQCQRH 226
Cdd:COG1117 150 KSALG----LSGGQQQRLCIARALAVEPEVLLMDEPTSALDpISTAK-IEELILELKKDY--TIVIVTHNMQQAARVSDY 222
|
250
....*....|.
gi 491113568 227 YALI-DGQLVE 236
Cdd:COG1117 223 TAFFyLGELVE 233
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
33-216 |
1.29e-30 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 118.63 E-value: 1.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 33 TIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVC-GESIAELNEEQRAEVRLKHIGFVFQSF----Q 107
Cdd:COG0488 12 PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPkGLRIGYLPQEPPLDDDLTVLDTVLDGDaelrA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 108 LLPHLTALENVMLPL--------RLQEKFKYA---EAEQKALNLLKRVGLERQAQQTP-KVLSGGEQQRVAIARALIREP 175
Cdd:COG0488 92 LEAELEELEAKLAEPdedlerlaELQEEFEALggwEAEARAEEILSGLGFPEEDLDRPvSELSGGWRRRVALARALLSEP 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 491113568 176 KIIFADEPTGNLDGETATEIEQLLfelnRELGTTLVLVTHD 216
Cdd:COG0488 172 DLLLLDEPTNHLDLESIEWLEEFL----KNYPGTVLVVSHD 208
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
34-241 |
2.10e-30 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 113.71 E-value: 2.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 34 IFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAEVRlKHIGFVFQSFQLLPHLT 113
Cdd:PRK11831 22 IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVR-KRMSMLFQSGALFTDMN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 114 ALENVMLPLRLQEKFKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETAT 193
Cdd:PRK11831 101 VFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491113568 194 EIEQLLFELNRELGTTLVLVTHD-PKLAAQCQRHYALIDGQLVEQFAAK 241
Cdd:PRK11831 181 VLVKLISELNSALGVTCVVVSHDvPEVLSIADHAYIVADKKIVAHGSAQ 229
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
38-216 |
2.49e-30 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 115.71 E-value: 2.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 38 LNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELneeqraEVRLKHIGFVFQSFQLLPHLTALEN 117
Cdd:PRK11650 23 IDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNEL------EPADRDIAMVFQNYALYPHMSVREN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 118 VMLPLRLQeKFKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDG----ETAT 193
Cdd:PRK11650 97 MAYGLKIR-GMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAklrvQMRL 175
|
170 180
....*....|....*....|...
gi 491113568 194 EIEQllfeLNRELGTTLVLVTHD 216
Cdd:PRK11650 176 EIQR----LHRRLKTTSLYVTHD 194
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
33-216 |
2.55e-30 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 115.21 E-value: 2.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 33 TIFENLNFDIQEGEQVAITGRSGSGKS----TLLGILATlDQASSGKLVVCGESIAELNEEQRAEVRLKHIGFVFQS--F 106
Cdd:PRK09473 30 TAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAA-NGRIGGSATFNGREILNLPEKELNKLRAEQISMIFQDpmT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 107 QLLPHLTALENVMLPLRLQEKFKYAEAEQKALNLLKRVGL---ERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEP 183
Cdd:PRK09473 109 SLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMpeaRKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEP 188
|
170 180 190
....*....|....*....|....*....|...
gi 491113568 184 TGNLDGETATEIEQLLFELNRELGTTLVLVTHD 216
Cdd:PRK09473 189 TTALDVTVQAQIMTLLNELKREFNTAIIMITHD 221
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
16-217 |
2.68e-30 |
|
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: 111.49 E-value: 2.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 16 ISAQNLTQKIQ--LAQKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILAtldqassGKLV---VCGEsiAELNEEQ 90
Cdd:cd03213 4 LSFRNLTVTVKssPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALA-------GRRTglgVSGE--VLINGRP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 91 RAEVRLK-HIGFVFQSFQLLPHLTALENVMLPLRLqekfkyaeaeqkalnllkrvglerqaqqtpKVLSGGEQQRVAIAR 169
Cdd:cd03213 75 LDKRSFRkIIGYVPQDDILHPTLTVRETLMFAAKL------------------------------RGLSGGERKRVSIAL 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491113568 170 ALIREPKIIFADEPTGNLDGETATEIEQLLFELnRELGTTLVLVTHDP 217
Cdd:cd03213 125 ELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRL-ADTGRTIICSIHQP 171
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
11-216 |
3.06e-30 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 114.68 E-value: 3.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 11 MPQTIISAQNLTQKIQL------AQKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIA 84
Cdd:PRK11308 1 SQQPLLQAIDLKKHYPVkrglfkPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 85 ELNEEQRAEVRLKhIGFVFQS--FQLLPHLTALENVMLPLRLQEKFKYAEAEQKALNLLKRVGLE-RQAQQTPKVLSGGE 161
Cdd:PRK11308 81 KADPEAQKLLRQK-IQIVFQNpyGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLRpEHYDRYPHMFSGGQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491113568 162 QQRVAIARALIREPKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHD 216
Cdd:PRK11308 160 RQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHD 214
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
34-217 |
3.73e-30 |
|
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: 117.46 E-value: 3.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 34 IFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEqraEVRlKHIGFVFQSfqllPHL- 112
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQD---EVR-RRVSVCAQD----AHLf 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 113 --TALENVMLPlrlqekfKYAEAEQKALNLLKRVGLERQAQQTP-----------KVLSGGEQQRVAIARALIREPKIIF 179
Cdd:TIGR02868 422 dtTVRENLRLA-------RPDATDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILL 494
|
170 180 190
....*....|....*....|....*....|....*...
gi 491113568 180 ADEPTGNLDGETATEIEQLLFELNRelGTTLVLVTHDP 217
Cdd:TIGR02868 495 LDEPTEHLDAETADELLEDLLAALS--GRTVVLITHHL 530
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
11-237 |
4.04e-30 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 113.19 E-value: 4.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 11 MPQTIISAQNLTQKIQLAQKQltIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGesiAELNEEQ 90
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDAATY--ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG---MVLSEET 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 91 RAEVRlKHIGFVFQ---------------SFqllphltALENVMLP-LRLQEKFKYAeaeqkalnlLKRVGLERQAQQTP 154
Cdd:PRK13635 76 VWDVR-RQVGMVFQnpdnqfvgatvqddvAF-------GLENIGVPrEEMVERVDQA---------LRQVGMEDFLNREP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 155 KVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDPKLAAQCQRHYALIDGQL 234
Cdd:PRK13635 139 HRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEI 218
|
...
gi 491113568 235 VEQ 237
Cdd:PRK13635 219 LEE 221
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
16-244 |
5.00e-30 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 117.22 E-value: 5.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 16 ISAQNLTqkIQLAQKQlTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVV-CGESIAELneEQRAev 94
Cdd:COG4178 363 LALEDLT--LRTPDGR-PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLFL--PQRP-- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 95 rlkhigfvfqsfqLLPHLTaLENVMLPLRLQEKFKYAEAEQkalnLLKRVGLER------QAQQTPKVLSGGEQQRVAIA 168
Cdd:COG4178 436 -------------YLPLGT-LREALLYPATAEAFSDAELRE----ALEAVGLGHlaerldEEADWDQVLSLGEQQRLAFA 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491113568 169 RALIREPKIIFADEPTGNLDGETATEIEQLLfeLNRELGTTLVLVTHDPKLAAQCQRHYALIDGQLVEQFAAKPTA 244
Cdd:COG4178 498 RLLLHKPDWLFLDEATSALDEENEAALYQLL--REELPGTTVISVGHRSTLAAFHDRVLELTGDGSWQLLPAEAPA 571
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
36-216 |
5.26e-30 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 112.49 E-value: 5.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 36 ENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQraevrlkhiGFVFQSFQLLPHLTAL 115
Cdd:PRK11248 18 EDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER---------GVVFQNEGLLPWRNVQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 116 ENVMLPLRLQEKFKyAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETATEI 195
Cdd:PRK11248 89 DNVAFGLQLAGVEK-MQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQM 167
|
170 180
....*....|....*....|.
gi 491113568 196 EQLLFELNRELGTTLVLVTHD 216
Cdd:PRK11248 168 QTLLLKLWQETGKQVLLITHD 188
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
34-236 |
5.34e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 112.24 E-value: 5.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 34 IFENLNFDIQEGEQVAITGRSGSGKSTLLGILATL-----DQASSGKLVVCGESIAElNEEQRAEVRlKHIGFVFQSFQL 108
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYS-PDVDPIEVR-REVGMVFQYPNP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 109 LPHLTALENVMLPLRLQEKFK-YAEAEQKALNLLKRVGL----ERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEP 183
Cdd:PRK14267 97 FPHLTIYDNVAIGVKLNGLVKsKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEP 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491113568 184 TGNLDGETATEIEQLLFELNRELgtTLVLVTHDPKLAAQCQRHYALID-GQLVE 236
Cdd:PRK14267 177 TANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYlGKLIE 228
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
28-217 |
6.25e-30 |
|
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: 114.44 E-value: 6.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 28 AQKQLTIFE-NLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAE------LNEEQRAevrlkhIG 100
Cdd:TIGR02142 5 FSKRLGDFSlDADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgifLPPEKRR------IG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 101 FVFQSFQLLPHLTALENvmlplrLQEKFKYAEAEQKALN---LLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKI 177
Cdd:TIGR02142 79 YVFQEARLFPHLSVRGN------LRYGMKRARPSERRISferVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 491113568 178 IFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDP 217
Cdd:TIGR02142 153 LLMDEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSL 192
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
10-237 |
9.78e-30 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 111.94 E-value: 9.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 10 IMPQTIISAQNLTQKIQlaqkQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGES-----IA 84
Cdd:PRK11701 1 MMDQPLLSVRGLTKLYG----PRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlrdLY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 85 ELNEEQRAEVRLKHIGFVFQSFQ--LLPHLTALENVMLPLRLQEKFKYAEAEQKALNLLKRVGLER-QAQQTPKVLSGGE 161
Cdd:PRK11701 77 ALSEAERRRLLRTEWGFVHQHPRdgLRMQVSAGGNIGERLMAVGARHYGDIRATAGDWLERVEIDAaRIDDLPTTFSGGM 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491113568 162 QQRVAIARALIREPKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDpkLA-AQCQRHYALI--DGQLVEQ 237
Cdd:PRK11701 157 QQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHD--LAvARLLAHRLLVmkQGRVVES 233
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
34-237 |
2.25e-29 |
|
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: 109.59 E-value: 2.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 34 IFENLNFDIQEGeQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAElneeQRAEVRlKHIGFVFQSFQLLPHLT 113
Cdd:cd03264 15 ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK----QPQKLR-RRIGYLPQEFGVYPNFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 114 ALENVMLPLRLQEKFKyAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGEtat 193
Cdd:cd03264 89 VREFLDYIAWLKGIPS-KEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPE--- 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491113568 194 eiEQLLF-ELNRELGT--TLVLVTHD-PKLAAQCQRHYALIDGQLVEQ 237
Cdd:cd03264 165 --ERIRFrNLLSELGEdrIVILSTHIvEDVESLCNQVAVLNKGKLVFE 210
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
37-219 |
2.48e-29 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 114.74 E-value: 2.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 37 NLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGEsiaelneeqraEVRLKH--------IGFVFQSFQL 108
Cdd:COG3845 23 DVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGK-----------PVRIRSprdaialgIGMVHQHFML 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 109 LPHLTALENVML--PLRLQEKFKYAEAEQKALNLLKRVGLE----RQAQQtpkvLSGGEQQRVAIARALIREPKIIFADE 182
Cdd:COG3845 92 VPNLTVAENIVLglEPTKGGRLDRKAARARIRELSERYGLDvdpdAKVED----LSVGEQQRVEILKALYRGARILILDE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 491113568 183 PTGNLdgeTATEIEQlLFELNREL---GTTLVLVTHdpKL 219
Cdd:COG3845 168 PTAVL---TPQEADE-LFEILRRLaaeGKSIIFITH--KL 201
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
16-237 |
3.39e-29 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 110.21 E-value: 3.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 16 ISAQNLTqkIQLAQKqlTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAEVR 95
Cdd:COG4559 2 LEAENLS--VRLGGR--TLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 96 lkhiGFVFQSFQLLPHLTALENVML---PLRLQEKFKYAEAEQKalnlLKRVGLERQAQQTPKVLSGGEQQRVAIARALI 172
Cdd:COG4559 78 ----AVLPQHSSLAFPFTVEEVVALgraPHGSSAAQDRQIVREA----LALVGLAHLAGRSYQTLSGGEQQRVQLARVLA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491113568 173 -------REPKIIFADEPTGNLDgetateI--EQLLFELNREL---GTTLVLVTHDPKLAAQ-CQRHYALIDGQLVEQ 237
Cdd:COG4559 150 qlwepvdGGPRWLFLDEPTSALD------LahQHAVLRLARQLarrGGGVVAVLHDLNLAAQyADRILLLHQGRLVAQ 221
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
37-241 |
7.23e-29 |
|
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: 108.92 E-value: 7.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 37 NLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAEvrlKHIGFVFQSFQLLPHLTALE 116
Cdd:COG0410 21 GVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIAR---LGIGYVPEGRRIFPSLTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 117 NVMLPLRLQ-EKFKYAEAEQKALNLLKRVGlERQAQQTpKVLSGGEQQRVAIARALIREPKIIFADEPTGNLdgetA--- 192
Cdd:COG0410 98 NLLLGAYARrDRAEVRADLERVYELFPRLK-ERRRQRA-GTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGL----Apli 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491113568 193 -TEIEQLLFELNRElGTTLVLVTHDPKLAAQ-CQRHYALIDGQLVEQFAAK 241
Cdd:COG0410 172 vEEIFEIIRRLNRE-GVTILLVEQNARFALEiADRAYVLERGRIVLEGTAA 221
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
23-237 |
1.30e-28 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 108.00 E-value: 1.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 23 QKIQLAQKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAEvrlKHIGFV 102
Cdd:TIGR03410 4 SNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERAR---AGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 103 FQSFQLLPHLTALENVMLPL-RLQEKFKYAEAEQKAL-----NLLKRVGlerqaqqtpKVLSGGEQQRVAIARALIREPK 176
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTGLaALPRRSRKIPDEIYELfpvlkEMLGRRG---------GDLSGGQQQQLAIARALVTRPK 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491113568 177 IIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDPKLAAQCQRHYALID-GQLVEQ 237
Cdd:TIGR03410 152 LLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMErGRVVAS 213
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
29-237 |
1.40e-28 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 113.38 E-value: 1.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 29 QKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQ-RAevrlkHIGFVFQSFQ 107
Cdd:PRK11160 350 DQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAlRQ-----AISVVSQRVH 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 108 LLPHlTALENVMLPlrlqekfKYAEAEQKALNLLKRVGLERQAQQTPKV----------LSGGEQQRVAIARALIREPKI 177
Cdd:PRK11160 425 LFSA-TLRDNLLLA-------APNASDEALIEVLQQVGLEKLLEDDKGLnawlgeggrqLSGGEQRRLGIARALLHDAPL 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 178 IFADEPTGNLDGETATEIEQLLFELNRelGTTLVLVTHDPKLAAQCQRHYALIDGQLVEQ 237
Cdd:PRK11160 497 LLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQFDRICVMDNGQIIEQ 554
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
33-237 |
1.41e-28 |
|
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: 106.63 E-value: 1.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 33 TIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRaevrlKHIGFVFQSfqllPHL 112
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALS-----SLISVLNQR----PYL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 113 --TALENvmlplrlqekfkyaeaeqkalNLLKRvglerqaqqtpkvLSGGEQQRVAIARALIREPKIIFADEPTGNLDGE 190
Cdd:cd03247 87 fdTTLRN---------------------NLGRR-------------FSGGERQRLALARILLQDAPIVLLDEPTVGLDPI 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491113568 191 TATEIEQLLFELNRElgTTLVLVTHDPKLAAQCQRHYALIDGQLVEQ 237
Cdd:cd03247 133 TERQLLSLIFEVLKD--KTLIWITHHLTGIEHMDKILFLENGKIIMQ 177
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
37-222 |
2.17e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 108.95 E-value: 2.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 37 NLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESI-AELNEEQRAEVRlKHIGFVFQ--SFQLLPHLT 113
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItAGKKNKKLKPLR-KKVGIVFQfpEHQLFEETV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 114 ALENVMLPLRLqeKFKYAEAEQKALNLLKRVGL-ERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETA 192
Cdd:PRK13634 104 EKDICFGPMNF--GVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGR 181
|
170 180 190
....*....|....*....|....*....|
gi 491113568 193 TEIEQLLFELNRELGTTLVLVTHDPKLAAQ 222
Cdd:PRK13634 182 KEMMEMFYKLHKEKGLTTVLVTHSMEDAAR 211
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
39-237 |
3.69e-28 |
|
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: 106.48 E-value: 3.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 39 NFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAevrlkhIGFVFQSFQLLPHLTALENV 118
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRP------VSMLFQENNLFAHLTVRQNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 119 MLPLRLQEKFKyAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETATEIEQL 198
Cdd:TIGR01277 92 GLGLHPGLKLN-AEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLAL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 491113568 199 LFELNRELGTTLVLVTHDPK-LAAQCQRHYALIDGQLVEQ 237
Cdd:TIGR01277 171 VKQLCSERQRTLLMVTHHLSdARAIASQIAVVSQGKIKVV 210
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
34-236 |
4.22e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 107.44 E-value: 4.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 34 IFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAE-VRL-KHIGFVFQSFQLLPH 111
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDaIKLrKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 112 LTALENVMLPLRLQEKFKYAEAEQKALNLLKRVGLERQA----QQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNL 187
Cdd:PRK14246 105 LSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVydrlNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491113568 188 DGETATEIEQLLFELNRELgtTLVLVTHDPKLAAQCQRHYA-LIDGQLVE 236
Cdd:PRK14246 185 DIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAfLYNGELVE 232
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
36-236 |
9.56e-28 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 111.10 E-value: 9.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 36 ENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAEVRlKHIGFVFQS--FQLLPHLT 113
Cdd:PRK10261 341 EKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALR-RDIQFIFQDpyASLDPRQT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 114 ALENVMLPLRLQEKFKYAEAEQKALNLLKRVGLE-RQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETA 192
Cdd:PRK10261 420 VGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIR 499
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 491113568 193 TEIEQLLFELNRELGTTLVLVTHDPKLAAQCQRHYALID-GQLVE 236
Cdd:PRK10261 500 GQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYlGQIVE 544
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
15-237 |
1.61e-27 |
|
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: 105.43 E-value: 1.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 15 IISAQNLTQKIqlaqKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAev 94
Cdd:TIGR04406 1 TLVAENLIKSY----KKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERA-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 95 RLKhIGFVFQSFQLLPHLTALENVMLPLRLQEKFKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIRE 174
Cdd:TIGR04406 75 RLG-IGYLPQEASIFRKLTVEENIMAVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491113568 175 PKIIFADEPTGNLDGETATEIEQLLFEL-NRELGttlVLVT-HDPK-LAAQCQRHYALIDGQLVEQ 237
Cdd:TIGR04406 154 PKFILLDEPFAGVDPIAVGDIKKIIKHLkERGIG---VLITdHNVReTLDICDRAYIISDGKVLAE 216
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
11-236 |
2.73e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 109.38 E-value: 2.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 11 MPQTIISAQNLTQKIQlaqkQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKlVVCGESIaelneeq 90
Cdd:COG0488 311 LGKKVLELEGLSKSYG----DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGT-VKLGETV------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 91 raevrlkHIGFVFQSFQLL-PHLTALENVMlplRLQEKFKyaeaEQKALNLLKRVGLERQAQQTP-KVLSGGEQQRVAIA 168
Cdd:COG0488 379 -------KIGYFDQHQEELdPDKTVLDELR---DGAPGGT----EQEVRGYLGRFLFSGDDAFKPvGVLSGGEKARLALA 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491113568 169 RALIREPKIIFADEPTGNLDGETATEIEQLL--FElnrelGtTLVLVTHDPK-LAAQCQRHYALIDGQLVE 236
Cdd:COG0488 445 KLLLSPPNVLLLDEPTNHLDIETLEALEEALddFP-----G-TVLLVSHDRYfLDRVATRILEFEDGGVRE 509
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
16-238 |
3.43e-27 |
|
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: 103.84 E-value: 3.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 16 ISAQNLTQKIqlaqKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEqraevr 95
Cdd:cd03268 1 LKTNDLTKTY----GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 96 LKHIGFVFQSFQLLPHLTALENVMLpLRLQEKFKYAEAEQkalnLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREP 175
Cdd:cd03268 71 LRRIGALIEAPGFYPNLTARENLRL-LARLLGIRKKRIDE----VLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNP 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491113568 176 KIIFADEPTGNLDGETATEIEQLLFELNRElGTTLVLVTHDPKLAAQCQRHYALI-DGQLVEQF 238
Cdd:cd03268 146 DLLILDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIInKGKLIEEG 208
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
15-241 |
4.96e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 105.94 E-value: 4.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 15 IISAQNLTQKIQLAQKQLTIF-----------------ENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLV 77
Cdd:COG4586 1 IIEVENLSKTYRVYEKEPGLKgalkglfrreyreveavDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 78 VCGESIAElneeQRAEVrLKHIGFVF-QSFQLLPHLTALENVMLplrLQEKFKYAEAE-QKALNLL-KRVGLERQAQQTP 154
Cdd:COG4586 81 VLGYVPFK----RRKEF-ARRIGVVFgQRSQLWWDLPAIDSFRL---LKAIYRIPDAEyKKRLDELvELLDLGELLDTPV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 155 KVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDPK-LAAQCQR-----HYA 228
Cdd:COG4586 153 RQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDdIEALCDRvividHGR 232
|
250
....*....|....*..
gi 491113568 229 LI-DG---QLVEQFAAK 241
Cdd:COG4586 233 IIyDGsleELKERFGPY 249
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
35-237 |
5.96e-27 |
|
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: 104.53 E-value: 5.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 35 FENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGES-----IAELNEEQRAEVRLKHIGFVFQSFQ-- 107
Cdd:TIGR02323 19 CRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgaeleLYQLSEAERRRLMRTEWGFVHQNPRdg 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 108 LLPHLTALENVMLPLRLQEKFKYAEAEQKALNLLKRVGLER-QAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGN 186
Cdd:TIGR02323 99 LRMRVSAGANIGERLMAIGARHYGNIRATAQDWLEEVEIDPtRIDDLPRAFSGGMQQRLQIARNLVTRPRLVFMDEPTGG 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491113568 187 LDGETATEIEQLLFELNRELGTTLVLVTHDPKLAA-QCQRHYALIDGQLVEQ 237
Cdd:TIGR02323 179 LDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARlLAQRLLVMQQGRVVES 230
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
13-235 |
7.94e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 104.78 E-value: 7.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 13 QTIISAQNLTQKIQLA--QKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVcgESIAELNEEQ 90
Cdd:PRK13633 2 NEMIKCKNVSYKYESNeeSTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYV--DGLDTSDEEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 91 RAEVRLKhIGFVFQS--FQLLPHLT------ALENV-MLPLRLQEKFKYAeaeqkalnlLKRVGLERQAQQTPKVLSGGE 161
Cdd:PRK13633 80 LWDIRNK-AGMVFQNpdNQIVATIVeedvafGPENLgIPPEEIRERVDES---------LKKVGMYEYRRHAPHLLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491113568 162 QQRVAIARALIREPKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDPKLAAQCQRHYALIDGQLV 235
Cdd:PRK13633 150 KQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVV 223
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
34-237 |
1.40e-26 |
|
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: 103.08 E-value: 1.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 34 IFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQraeVRlKHIGFVFQSFQLLpHLT 113
Cdd:cd03253 16 VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDS---LR-RAIGVVPQDTVLF-NDT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 114 ALENVML------PLRLQEKFKYAEAEQKALNLLK----RVGlERQAQqtpkvLSGGEQQRVAIARALIREPKIIFADEP 183
Cdd:cd03253 91 IGYNIRYgrpdatDEEVIEAAKAAQIHDKIMRFPDgydtIVG-ERGLK-----LSGGEKQRVAIARAILKNPPILLLDEA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491113568 184 TGNLDGETATEIEQLLFELNRelGTTLVLVTHDPKLAAQCQRHYALIDGQLVEQ 237
Cdd:cd03253 165 TSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVNADKIIVLKDGRIVER 216
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
31-217 |
1.72e-26 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 107.44 E-value: 1.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 31 QLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQAS---SGKLVVCGESIAElnEEQRAEVrlkhiGFVFQSFQ 107
Cdd:TIGR00955 37 RKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDA--KEMRAIS-----AYVQQDDL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 108 LLPHLTALE--NVMLPLRLQEKFKYAEAEQKALNLLKRVGLeRQAQQT-------PKVLSGGEQQRVAIARALIREPKII 178
Cdd:TIGR00955 110 FIPTLTVREhlMFQAHLRMPRRVTKKEKRERVDEVLQALGL-RKCANTrigvpgrVKGLSGGERKRLAFASELLTDPPLL 188
|
170 180 190
....*....|....*....|....*....|....*....
gi 491113568 179 FADEPTGNLDGETATEIEQLLFELNRElGTTLVLVTHDP 217
Cdd:TIGR00955 189 FCDEPTSGLDSFMAYSVVQVLKGLAQK-GKTIICTIHQP 226
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
11-242 |
2.22e-26 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 106.71 E-value: 2.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 11 MPQTIISAQNLTQKIQLAQKQLTIFENLNFDIQEGEQVAITGRSGSGKS-TLLGILATLDQAS----SGKLVVCGESIAE 85
Cdd:PRK15134 1 MTQPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 86 LNEEQRAEVRLKHIGFVFQS--FQLLPHLTALENVMLPLRLQEKFKYAEAEQKALNLLKRVGLeRQAQQT----PKVLSG 159
Cdd:PRK15134 81 ASEQTLRGVRGNKIAMIFQEpmVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGI-RQAAKRltdyPHQLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 160 GEQQRVAIARALIREPKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDPKLAAQCQRHYALI-DGQLVEQF 238
Cdd:PRK15134 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMqNGRCVEQN 239
|
....
gi 491113568 239 AAKP 242
Cdd:PRK15134 240 RAAT 243
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
30-225 |
2.64e-26 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 102.41 E-value: 2.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 30 KQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGEsiaeLNEEQRAEVrLKHIGFVF-QSFQL 108
Cdd:cd03267 32 REVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL----VPWKRRKKF-LRRIGVVFgQKTQL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 109 LPHLTALENVMLpLRLQEKFKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLD 188
Cdd:cd03267 107 WWDLPVIDSFYL-LAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD 185
|
170 180 190
....*....|....*....|....*....|....*...
gi 491113568 189 GETATEIEQLLFELNRELGTTLVLVTHDPK-LAAQCQR 225
Cdd:cd03267 186 VVAQENIRNFLKEYNRERGTTVLLTSHYMKdIEALARR 223
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
33-221 |
3.16e-26 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 100.77 E-value: 3.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 33 TIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVV-CGESIAELneEQRAEVRlkhigfvfqsfQLLPh 111
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRaGGARVAYV--PQRSEVP-----------DSLP- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 112 LTALENVML---PLRLQEKFKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLD 188
Cdd:NF040873 72 LTVRDLVAMgrwARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190
....*....|....*....|....*....|...
gi 491113568 189 GETATEIEQLLFELNRElGTTLVLVTHDPKLAA 221
Cdd:NF040873 152 AESRERIIALLAEEHAR-GATVVVVTHDLELVR 183
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
31-216 |
3.23e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 103.63 E-value: 3.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 31 QLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLV------------VCGESIAELNEEQRAEVR--- 95
Cdd:PRK13651 19 ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwifkdeknkkktKEKEKVLEKLVIQKTRFKkik 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 96 -----LKHIGFVFQ--SFQLLPHlTALENVML-PLRLqeKFKYAEAEQKALNLLKRVGL-ERQAQQTPKVLSGGEQQRVA 166
Cdd:PRK13651 99 kikeiRRRVGVVFQfaEYQLFEQ-TIEKDIIFgPVSM--GVSKEEAKKRAAKYIELVGLdESYLQRSPFELSGGQKRRVA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491113568 167 IARALIREPKIIFADEPTGNLDGETATEIEQLLFELNRElGTTLVLVTHD 216
Cdd:PRK13651 176 LAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHD 224
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
12-241 |
3.48e-26 |
|
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: 106.37 E-value: 3.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 12 PQTIISAQNLTQKIQLAQKqlTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQR 91
Cdd:COG4618 327 PKGRLSVENLTVVPPGSKR--PILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREEL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 92 AevrlKHIGFVFQSFQLLPHlTALENVMlplRLQEkfkyAEAEqKALNLLKRVGL----ERQAQ--QTP-----KVLSGG 160
Cdd:COG4618 405 G----RHIGYLPQDVELFDG-TIAENIA---RFGD----ADPE-KVVAAAKLAGVhemiLRLPDgyDTRigeggARLSGG 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 161 EQQRVAIARALIREPKIIFADEPTGNLD--GETA--TEIEQLlfelnRELGTTLVLVTHDPKLAAQCQRHYALIDGQlVE 236
Cdd:COG4618 472 QRQRIGLARALYGDPRLVVLDEPNSNLDdeGEAAlaAAIRAL-----KARGATVVVITHRPSLLAAVDKLLVLRDGR-VQ 545
|
....*
gi 491113568 237 QFAAK 241
Cdd:COG4618 546 AFGPR 550
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
37-215 |
3.79e-26 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 101.53 E-value: 3.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 37 NLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNeeqRAEVRlKHIGFVFQSFQLLPHlTALE 116
Cdd:cd03254 21 DINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIS---RKSLR-SMIGVVLQDTFLFSG-TIME 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 117 NVML--PLRLQEKFKYAEAEQKALNLLKRV--GLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETA 192
Cdd:cd03254 96 NIRLgrPNATDEEVIEAAKEAGAHDFIMKLpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETE 175
|
170 180
....*....|....*....|...
gi 491113568 193 TEIEQLLFELNRelGTTLVLVTH 215
Cdd:cd03254 176 KLIQEALEKLMK--GRTSIIIAH 196
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
36-241 |
5.97e-26 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 103.28 E-value: 5.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 36 ENLNFDIQEGEQVAITGRSGSGKS-TLLGILATLD---QASSGKLVVCGESIAELNEEQRAEVRLKHIGFVFQS--FQLL 109
Cdd:PRK11022 24 DRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDypgRVMAEKLEFNGQDLQRISEKERRNLVGAEVAMIFQDpmTSLN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 110 PHLTALENVMLPLRLQEKFKYAEAEQKALNLLKRVGLERQAQQT---PKVLSGGEQQRVAIARALIREPKIIFADEPTGN 186
Cdd:PRK11022 104 PCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLdvyPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTA 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491113568 187 LDGETATEIEQLLFELNRELGTTLVLVTHDPKLAAQCQRH----YAlidGQLVEQFAAK 241
Cdd:PRK11022 184 LDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKiivmYA---GQVVETGKAH 239
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
16-215 |
8.11e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 102.05 E-value: 8.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 16 ISAQNLT----QKIQLAQKQLtifENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQR 91
Cdd:PRK13637 3 IKIENLThiymEGTPFEKKAL---DNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 92 aEVRlKHIGFVFQ--SFQLLPHLTALENVMLP--LRLQEKfkyaEAEQKALNLLKRVGLERQ--AQQTPKVLSGGEQQRV 165
Cdd:PRK13637 80 -DIR-KKVGLVFQypEYQLFEETIEKDIAFGPinLGLSEE----EIENRVKRAMNIVGLDYEdyKDKSPFELSGGQKRRV 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491113568 166 AIARALIREPKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTH 215
Cdd:PRK13637 154 AIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSH 203
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
37-219 |
1.08e-25 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 101.22 E-value: 1.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 37 NLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAE---VRlkhigfVFQSFQLLPHLT 113
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARmgvVR------TFQHVRLFREMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 114 ALENVMLPLRLQEK------------FKYAEAE--QKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIF 179
Cdd:PRK11300 97 VIENLLVAQHQQLKtglfsgllktpaFRRAESEalDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILM 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 491113568 180 ADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDPKL 219
Cdd:PRK11300 177 LDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKL 216
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
16-244 |
1.29e-25 |
|
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: 100.31 E-value: 1.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 16 ISAQNLTQKIqlaqKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAevR 95
Cdd:cd03218 1 LRAENLSKRY----GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRA--R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 96 LKhIGFVFQSFQLLPHLTALENVMLPLRLQEKFKyAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREP 175
Cdd:cd03218 75 LG-IGYLPQEASIFRKLTVEENILAVLEIRGLSK-KEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491113568 176 KIIFADEPTGNLDGETATEIEQLLFEL-NRELGttlVLVT-HDPK-LAAQCQRHYALIDGQL-----VEQFAAKPTA 244
Cdd:cd03218 153 KFLLLDEPFAGVDPIAVQDIQKIIKILkDRGIG---VLITdHNVReTLSITDRAYIIYEGKVlaegtPEEIAANELV 226
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
14-247 |
1.65e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 100.62 E-value: 1.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 14 TIISAQNLTqkIQLAQKqlTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAe 93
Cdd:PRK13548 1 AMLEARNLS--VRLGGR--TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELA- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 94 vrlKHIGFVFQSFQLLPHLTALENVML---PLRLQEKfkyaEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARA 170
Cdd:PRK13548 76 ---RRRAVLPQHSSLSFPFTVEEVVAMgraPHGLSRA----EDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 171 LIR------EPKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDPKLAAQ-CQRHYALIDGQLVEQfaAKPT 243
Cdd:PRK13548 149 LAQlwepdgPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARyADRIVLLHQGRLVAD--GTPA 226
|
....
gi 491113568 244 AAIT 247
Cdd:PRK13548 227 EVLT 230
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
23-241 |
3.00e-25 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 100.06 E-value: 3.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 23 QKIQLAQKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAevrlKHIGFV 102
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA----RRIGLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 103 FQSFQLLPHLTALENVM------LPLRLQEKFKYAEAEQKALnllKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPK 176
Cdd:PRK10253 87 AQNATTPGDITVQELVArgryphQPLFTRWRKEDEEAVTKAM---QATGITHLADQSVDTLSGGQRQRAWIAMVLAQETA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491113568 177 IIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDPKLAAQCQRHY-ALIDGQLVEQFAAK 241
Cdd:PRK10253 164 IMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLiALREGKIVAQGAPK 229
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
11-235 |
5.10e-25 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 102.94 E-value: 5.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 11 MPQTIISAQNLTQKIQLAQKqltiFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQ 90
Cdd:PRK09700 1 MATPYISMAGIGKSFGPVHA----LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 91 RAEVrlkHIGFVFQSFQLLPHLTALENVMLPLRLQEKF------KYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQR 164
Cdd:PRK09700 77 AAQL---GIGIIYQELSVIDELTVLENLYIGRHLTKKVcgvniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491113568 165 VAIARALIREPKIIFADEPTGNLdgeTATEIEQLLFELN--RELGTTLVLVTHDPK-LAAQCQRHYALIDGQLV 235
Cdd:PRK09700 154 LEIAKTLMLDAKVIIMDEPTSSL---TNKEVDYLFLIMNqlRKEGTAIVYISHKLAeIRRICDRYTVMKDGSSV 224
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
11-236 |
5.99e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 99.08 E-value: 5.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 11 MPQTIISAQNLTqkIQLAQKQltIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQ-----ASSGKLVVCGESIAE 85
Cdd:PRK14239 1 MTEPILQVSDLS--VYYNKKK--ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIYS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 86 LNEEQrAEVRlKHIGFVFQSFQLLPhLTALENVMLPLRL---QEKFKYAEAEQKALnllkrvgleRQAQQTPKV------ 156
Cdd:PRK14239 77 PRTDT-VDLR-KEIGMVFQQPNPFP-MSIYENVVYGLRLkgiKDKQVLDEAVEKSL---------KGASIWDEVkdrlhd 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 157 ----LSGGEQQRVAIARALIREPKIIFADEPTGNLDGETATEIEQLLFELNRELgtTLVLVTHDPKLAAQ-CQRHYALID 231
Cdd:PRK14239 145 salgLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRiSDRTGFFLD 222
|
....*
gi 491113568 232 GQLVE 236
Cdd:PRK14239 223 GDLIE 227
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
37-238 |
6.51e-25 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 102.30 E-value: 6.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 37 NLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEeqrAEVRLKHIGFVFQSFQLLPHLTALE 116
Cdd:PRK11288 22 DISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFAST---TAALAAGVAIIYQELHLVPEMTVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 117 NVMLPlRLQEKF---KYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLdgeTAT 193
Cdd:PRK11288 99 NLYLG-QLPHKGgivNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSL---SAR 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491113568 194 EIEQlLFELNREL---GTTLVLVTHD-PKLAAQCQRHYALIDGQLVEQF 238
Cdd:PRK11288 175 EIEQ-LFRVIRELraeGRVILYVSHRmEEIFALCDAITVFKDGRYVATF 222
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
11-237 |
7.84e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 99.54 E-value: 7.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 11 MPQTIISAQNLTQKIQLAQKQLtifENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIaELNEEQ 90
Cdd:PRK13636 1 MEDYILKVEELNYNYSDGTHAL---KGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 91 RAEVRlKHIGFVFQS--FQLLPhLTALENV---MLPLRLQEKfkyaEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRV 165
Cdd:PRK13636 77 LMKLR-ESVGMVFQDpdNQLFS-ASVYQDVsfgAVNLKLPED----EVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491113568 166 AIARALIREPKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDPKLAA-QCQRHYALIDGQLVEQ 237
Cdd:PRK13636 151 AIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQ 223
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
15-222 |
1.21e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 98.65 E-value: 1.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 15 IISAQNLTQKIQLAQKQLtifENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGEsiaELNEEQRAEV 94
Cdd:PRK13647 4 IIEVEDLHFRYKDGTKAL---KGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGR---EVNAENEKWV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 95 RLKhIGFVFQS--FQLLPhLTALENVML-PLRLqeKFKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARAL 171
Cdd:PRK13647 78 RSK-VGLVFQDpdDQVFS-STVWDDVAFgPVNM--GLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491113568 172 IREPKIIFADEPTGNLDGETATEIEQLLFELNRElGTTLVLVTHDPKLAAQ 222
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAE 203
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
15-234 |
1.46e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 98.65 E-value: 1.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 15 IISAQNLTQKIQLAQKQLTIfENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGEsiaELNEEQRAEV 94
Cdd:PRK13650 4 IIEVKNLTFKYKEDQEKYTL-NDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD---LLTEENVWDI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 95 RlKHIGFVFQS--FQLLPHLT------ALENVMLPLRLQEkfkyaEAEQKALNLlkrVGLERQAQQTPKVLSGGEQQRVA 166
Cdd:PRK13650 80 R-HKIGMVFQNpdNQFVGATVeddvafGLENKGIPHEEMK-----ERVNEALEL---VGMQDFKEREPARLSGGQKQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491113568 167 IARALIREPKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDPKLAAQCQRHYALIDGQL 234
Cdd:PRK13650 151 IAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
33-221 |
2.20e-24 |
|
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: 95.30 E-value: 2.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 33 TIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESiaelneeqraevrlkHIGFVFQsfqlLPHL 112
Cdd:cd03223 15 VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE---------------DLLFLPQ----RPYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 113 TAlenvmlplrlqekfkyaeaeqkalnllkrvGLERQAQQTP--KVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGE 190
Cdd:cd03223 76 PL------------------------------GTLREQLIYPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEE 125
|
170 180 190
....*....|....*....|....*....|.
gi 491113568 191 TateiEQLLFELNRELGTTLVLVTHDPKLAA 221
Cdd:cd03223 126 S----EDRLYQLLKELGITVISVGHRPSLWK 152
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
37-235 |
5.12e-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: 94.03 E-value: 5.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 37 NLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNeeqRAEVRLKHIGFVFQsfqllphltale 116
Cdd:cd03216 18 GVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFAS---PRDARRAGIAMVYQ------------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 117 nvmlplrlqekfkyaeaeqkalnllkrvglerqaqqtpkvLSGGEQQRVAIARALIREPKIIFADEPTGNLdgeTATEIE 196
Cdd:cd03216 83 ----------------------------------------LSVGERQMVEIARALARNARLLILDEPTAAL---TPAEVE 119
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 491113568 197 QlLFELNREL---GTTLVLVTHDPKLAAQ-CQRHYALIDGQLV 235
Cdd:cd03216 120 R-LFKVIRRLraqGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
20-236 |
5.62e-24 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 98.05 E-value: 5.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 20 NLTQKIQLAQKQLTIFENLNFDIQEGEQVAITGRSGSGKS----TLLGILATLDQASSGKLVVCGESIAELNEEQRAEVR 95
Cdd:COG4170 8 NLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSliakAICGITKDNWHVTADRFRWNGIDLLKLSPRERRKII 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 96 LKHIGFVFQSFQ--LLPHLTA---LENVMLPLRLQEKF--KYAEAEQKALNLLKRVGL---ERQAQQTPKVLSGGEQQRV 165
Cdd:COG4170 88 GREIAMIFQEPSscLDPSAKIgdqLIEAIPSWTFKGKWwqRFKWRKKRAIELLHRVGIkdhKDIMNSYPHELTEGECQKV 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491113568 166 AIARALIREPKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHD-PKLAAQCQRHYALIDGQLVE 236
Cdd:COG4170 168 MIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDlESISQWADTITVLYCGQTVE 239
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
33-216 |
7.39e-24 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 95.55 E-value: 7.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 33 TIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQ-RAEVrlkhiGFVFQSfqllPH 111
Cdd:PRK10247 21 KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyRQQV-----SYCAQT----PT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 112 L---TALENVMLPLRLQEKfkyAEAEQKALNLLKRVGL-ERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNL 187
Cdd:PRK10247 92 LfgdTVYDNLIFPWQIRNQ---QPDPAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSAL 168
|
170 180
....*....|....*....|....*....
gi 491113568 188 DGETATEIEQLLFELNRELGTTLVLVTHD 216
Cdd:PRK10247 169 DESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
34-237 |
8.11e-24 |
|
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: 95.63 E-value: 8.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 34 IFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQ-RAEVrlkhiGFVFQSfQLLPHL 112
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWlRRQV-----GVVLQE-NVLFNR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 113 TALENVML-----PL-RLQEKFKYAEAEQKALNLlkRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGN 186
Cdd:cd03252 91 SIRDNIALadpgmSMeRVIEAAKLAGAHDFISEL--PEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491113568 187 LDGETATEIEQLLFELNRelGTTLVLVTHDPKLAAQCQRHYALIDGQLVEQ 237
Cdd:cd03252 169 LDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKNADRIIVMEKGRIVEQ 217
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
12-234 |
9.88e-24 |
|
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: 99.34 E-value: 9.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 12 PQTIISAQNLTqkIQLAQKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQR 91
Cdd:TIGR01842 313 PEGHLSVENVT--IVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETF 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 92 AevrlKHIGFVFQSFQLLPHlTALENVMlplRLQEKF---------KYAEAEQKALNLLKrvGLERQAQQTPKVLSGGEQ 162
Cdd:TIGR01842 391 G----KHIGYLPQDVELFPG-TVAENIA---RFGENAdpekiieaaKLAGVHELILRLPD--GYDTVIGPGGATLSGGQR 460
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491113568 163 QRVAIARALIREPKIIFADEPTGNLDgetaTEIEQLLFELNREL---GTTLVLVTHDPKLAAQCQRHYALIDGQL 234
Cdd:TIGR01842 461 QRIALARALYGDPKLVVLDEPNSNLD----EEGEQALANAIKALkarGITVVVITHRPSLLGCVDKILVLQDGRI 531
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
11-236 |
1.15e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 99.16 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 11 MPQT-------IISAQNLTQKIQLAQKQLTIFENLNFDIQEGEQVAITGRSGSGKS-TLLGILATLDQasSGKLVVCG-- 80
Cdd:PRK10261 1 MPHSdeldardVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ--AGGLVQCDkm 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 81 ------ESIAELNEEQRAE---VRLKHIGFVFQS--FQLLPHLTALENVMLPLRLQEKFKYAEAEQKALNLLKRVGL-ER 148
Cdd:PRK10261 79 llrrrsRQVIELSEQSAAQmrhVRGADMAMIFQEpmTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIpEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 149 QA--QQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDPKLAAQ-CQR 225
Cdd:PRK10261 159 QTilSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEiADR 238
|
250
....*....|.
gi 491113568 226 HYALIDGQLVE 236
Cdd:PRK10261 239 VLVMYQGEAVE 249
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
33-216 |
1.78e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 95.15 E-value: 1.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 33 TIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAevrlKHIGFVFQSFQL--LP 110
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRA----KYIGRVFQDPMMgtAP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 111 HLTALENVMLPLRLQEKFKYAEAEQKAL-----NLLKRV--GLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEP 183
Cdd:COG1101 96 SMTIEENLALAYRRGKRRGLRRGLTKKRrelfrELLATLglGLENRLDTKVGLLSGGQRQALSLLMATLTKPKLLLLDEH 175
|
170 180 190
....*....|....*....|....*....|...
gi 491113568 184 TGNLDGETATEIEQLLFELNRELGTTLVLVTHD 216
Cdd:COG1101 176 TAALDPKTAALVLELTEKIVEENNLTTLMVTHN 208
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
16-237 |
1.90e-23 |
|
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: 93.88 E-value: 1.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 16 ISAQNLTQKIqlaqKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEqraevr 95
Cdd:cd03269 1 LEVENVTKRF----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARN------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 96 lkHIGFVFQSFQLLPHLTALENVMLPLRLQeKFKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREP 175
Cdd:cd03269 71 --RIGYLPEERGLYPKMKVIDQLVYLAQLK-GLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDP 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491113568 176 KIIFADEPTGNLDGETATEIEQLLFELNRElGTTLVLVTHDPKLAAQ-CQRHYALIDGQLVEQ 237
Cdd:cd03269 148 ELLILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEElCDRVLLLNKGRAVLY 209
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
14-234 |
3.37e-23 |
|
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: 92.50 E-value: 3.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 14 TIISAQNLTQKIQlaqkqltiFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAE 93
Cdd:cd03215 3 PVLEVRGLSVKGA--------VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 94 vrlKHIGFV---FQSFQLLPHLTALENVMLPLRLqekfkyaeaeqkalnllkrvglerqaqqtpkvlSGGEQQRVAIARA 170
Cdd:cd03215 75 ---AGIAYVpedRKREGLVLDLSVAENIALSSLL---------------------------------SGGNQQKVVLARW 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491113568 171 LIREPKIIFADEPTGNLDGETATEIEQLLFELNRElGTTLVLVTHD-PKLAAQCQRHYALIDGQL 234
Cdd:cd03215 119 LARDPRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSElDELLGLCDRILVMYEGRI 182
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
33-237 |
4.13e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 97.47 E-value: 4.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 33 TIFENLNFDIQEGEQVAITGRSGSGKSTL-LGILATLdqASSGKLVVCGESIAELNEEQRAEVRlKHIGFVFQ--SFQLL 109
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTTgLALLRLI--NSQGEIWFDGQPLHNLNRRQLLPVR-HRIQVVFQdpNSSLN 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 110 PHLTALENVMLPLRL-QEKFKYAEAEQKALNLLKRVGLERQAQQT-PKVLSGGEQQRVAIARALIREPKIIFADEPTGNL 187
Cdd:PRK15134 377 PRLNVLQIIEEGLRVhQPTLSAAQREQQVIAVMEEVGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEPTSSL 456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491113568 188 DGETATEIEQLLFELNRELGTTLVLVTHDPKLA-AQCQRHYALIDGQLVEQ 237
Cdd:PRK15134 457 DKTVQAQILALLKSLQQKHQLAYLFISHDLHVVrALCHQVIVLRQGEVVEQ 507
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
34-237 |
4.81e-23 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 97.49 E-value: 4.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 34 IFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEeqraeVRL-KHIGFVFQSFQLLPHl 112
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDH-----HYLhRQVALVGQEPVLFSG- 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 113 TALENVMLPLRLQEKFKYAEAEQKA------LNLLKrvGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGN 186
Cdd:TIGR00958 570 SVRENIAYGLTDTPDEEIMAAAKAAnahdfiMEFPN--GYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSA 647
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491113568 187 LDgetaTEIEQLLFELNRELGTTLVLVTHDPKLAAQCQRHYALIDGQLVEQ 237
Cdd:TIGR00958 648 LD----AECEQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEM 694
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
34-237 |
5.18e-23 |
|
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: 93.37 E-value: 5.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 34 IFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRaevrLKHIGFVFQSfqllPHL- 112
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWL----RSQIGLVSQE----PVLf 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 113 --TALENVMLPLRLQEKFKYAEAEQKAlNLLK-----------RVGlERQAQqtpkvLSGGEQQRVAIARALIREPKIIF 179
Cdd:cd03249 90 dgTIAENIRYGKPDATDEEVEEAAKKA-NIHDfimslpdgydtLVG-ERGSQ-----LSGGQKQRIAIARALLRNPKILL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 180 ADEPTGNLDGETATEIEQLLFELNRelGTTLVLVTHdpKLAA--QCQRHYALIDGQLVEQ 237
Cdd:cd03249 163 LDEATSALDAESEKLVQEALDRAMK--GRTTIVIAH--RLSTirNADLIAVLQNGQVVEQ 218
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
13-214 |
5.25e-23 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 94.09 E-value: 5.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 13 QTIISAQNLTQKIQ-----LAQKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELN 87
Cdd:PRK15112 2 ETLLEVRNLSKTFRyrtgwFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 88 EEQRAEvrlkHIGFVFQ--SFQLLPHLTALENVMLPLRLQEKFKYAEAEQKALNLLKRVGLER-QAQQTPKVLSGGEQQR 164
Cdd:PRK15112 82 YSYRSQ----RIRMIFQdpSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPdHASYYPHMLAPGQKQR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491113568 165 VAIARALIREPKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVT 214
Cdd:PRK15112 158 LGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVT 207
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
37-216 |
7.94e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 93.66 E-value: 7.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 37 NLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEqraEVRlKHIGFVFQS--FQLLPHLTA 114
Cdd:PRK13648 27 DVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFE---KLR-KHIGIVFQNpdNQFVGSIVK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 115 ------LENVMLPlrlqekfkYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLD 188
Cdd:PRK13648 103 ydvafgLENHAVP--------YDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLD 174
|
170 180
....*....|....*....|....*...
gi 491113568 189 GETATEIEQLLFELNRELGTTLVLVTHD 216
Cdd:PRK13648 175 PDARQNLLDLVRKVKSEHNITIISITHD 202
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
15-235 |
1.23e-22 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 92.65 E-value: 1.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 15 IISAQNLTQkiqlAQKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAev 94
Cdd:PRK10895 3 TLTAKNLAK----AYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARA-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 95 rLKHIGFVFQSFQLLPHLTALENVMLPLRLQEKFKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIRE 174
Cdd:PRK10895 77 -RRGIGYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAAN 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491113568 175 PKIIFADEPTGNLDGETATEIEQLLFELnRELGTTLVLVTHDPK-LAAQCQRHYALIDGQLV 235
Cdd:PRK10895 156 PKFILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVReTLAVCERAYIVSQGHLI 216
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
34-215 |
1.74e-22 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 91.40 E-value: 1.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 34 IFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAEvrLKHIGfvfqsfqllpH-- 111
Cdd:PRK13538 16 LFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQD--LLYLG----------Hqp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 112 -----LTALENVMLPLRLQEKFKyaeaEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGN 186
Cdd:PRK13538 84 gikteLTALENLRFYQRLHGPGD----DEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTA 159
|
170 180
....*....|....*....|....*....
gi 491113568 187 LDGETATEIEQlLFELNRELGTTLVLVTH 215
Cdd:PRK13538 160 IDKQGVARLEA-LLAQHAEQGGMVILTTH 187
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
16-237 |
2.23e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 95.30 E-value: 2.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 16 ISAQNLTqkIQLAQ-KQLTifENLNFDIQEGEQVAITGRSGSGKSTL----LGILATldqasSGKLVVCGESIAELNEEQ 90
Cdd:PRK11174 350 IEAEDLE--ILSPDgKTLA--GPLNFTLPAGQRIALVGPSGAGKTSLlnalLGFLPY-----QGSLKINGIELRELDPES 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 91 RaevrLKHIGFVFQSFQLlPHLTALENVML--PLRLQEKFKYAEAEQKALNLLKRV--GLERQAQQTPKVLSGGEQQRVA 166
Cdd:PRK11174 421 W----RKHLSWVGQNPQL-PHGTLRDNVLLgnPDASDEQLQQALENAWVSEFLPLLpqGLDTPIGDQAAGLSVGQAQRLA 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491113568 167 IARALIREPKIIFADEPTGNLDGETATEIEQLLFELNRelGTTLVLVTHDPKLAAQCQRHYALIDGQLVEQ 237
Cdd:PRK11174 496 LARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQ 564
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
37-215 |
3.49e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 92.11 E-value: 3.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 37 NLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAEVRLKHIGFVFQ--SFQLLPHlTA 114
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRKKVGLVFQfpESQLFEE-TV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 115 LENVMLPlrlQEKFKYA--EAEQKALNLLKRVGL-ERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGET 191
Cdd:PRK13649 104 LKDVAFG---PQNFGVSqeEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180
|
170 180
....*....|....*....|....
gi 491113568 192 ATEIEQLLFELNrELGTTLVLVTH 215
Cdd:PRK13649 181 RKELMTLFKKLH-QSGMTIVLVTH 203
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
34-237 |
4.12e-22 |
|
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: 91.14 E-value: 4.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 34 IFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELneeQRAEVRlKHIGFVFQSFQLLpHLT 113
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDY---TLASLR-RQIGLVSQDVFLF-NDT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 114 ALENVML------PLRLQEKFKYAEAEQKALNLLKrvGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNL 187
Cdd:cd03251 92 VAENIAYgrpgatREEVEEAARAANAHEFIMELPE--GYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSAL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491113568 188 DGETATEIEQLLFEL--NRelgTTLVlVTHDPKLAAQCQRHYALIDGQLVEQ 237
Cdd:cd03251 170 DTESERLVQAALERLmkNR---TTFV-IAHRLSTIENADRIVVLEDGKIVER 217
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
34-237 |
6.97e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 91.40 E-value: 6.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 34 IFENLNFDIQEGEQVAITGRSGSGKST----LLGILATlDQASSGKLVVCGesiAELNEEQRAEVRLKhIGFVFQS--FQ 107
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTisklINGLLLP-DDNPNSKITVDG---ITLTAKTVWDIREK-VGIVFQNpdNQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 108 LLPHLT------ALENVMLPlrlqekfkYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFAD 181
Cdd:PRK13640 97 FVGATVgddvafGLENRAVP--------RPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491113568 182 EPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDPKLAAQCQRHYALIDGQLVEQ 237
Cdd:PRK13640 169 ESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQ 224
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
37-237 |
9.18e-22 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 93.63 E-value: 9.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 37 NLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELneeQRAEVRlKHIGFVFQSFQLLPHlTALE 116
Cdd:TIGR02203 350 SISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADY---TLASLR-RQVALVSQDVVLFND-TIAN 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 117 NVMLPLRLQEKFKYAEAEQKALNLLKRV-----GLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGET 191
Cdd:TIGR02203 425 NIAYGRTEQADRAEIERALAAAYAQDFVdklplGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNES 504
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491113568 192 ATEIEQLLFELNRELgTTLVlVTHDPKLAAQCQRHYALIDGQLVEQ 237
Cdd:TIGR02203 505 ERLVQAALERLMQGR-TTLV-IAHRLSTIEKADRIVVMDDGRIVER 548
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
13-216 |
2.09e-21 |
|
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: 92.69 E-value: 2.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 13 QTIISAQNLTqKIQLAQKQltIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGklvvcgesiaelneEQRA 92
Cdd:TIGR03719 2 QYIYTMNRVS-KVVPPKKE--ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG--------------EARP 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 93 EVRLKhIGFVFQSFQLLPHLTALENVMLPLR----LQEKF-----KYAE---------AEQKAL-NLLKRVG---LERQ- 149
Cdd:TIGR03719 65 QPGIK-VGYLPQEPQLDPTKTVRENVEEGVAeikdALDRFneisaKYAEpdadfdklaAEQAELqEIIDAADawdLDSQl 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491113568 150 -----AQQTP------KVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETATEIEQLLfelnRELGTTLVLVTHD 216
Cdd:TIGR03719 144 eiamdALRCPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL----QEYPGTVVAVTHD 217
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
36-237 |
2.31e-21 |
|
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: 88.70 E-value: 2.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 36 ENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNeeqRAEVRlKHIGFVFQSfqllPHL--- 112
Cdd:cd03244 21 KNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIG---LHDLR-SRISIIPQD----PVLfsg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 113 TALENvMLPLRlqekfKYAEAEqkALNLLKRVGLERQAQQTPK-----------VLSGGEQQRVAIARALIREPKIIFAD 181
Cdd:cd03244 93 TIRSN-LDPFG-----EYSDEE--LWQALERVGLKEFVESLPGgldtvveeggeNLSVGQRQLLCLARALLRKSKILVLD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491113568 182 EPTGNLDGETATEIEQLLFElnrEL-GTTLVLVTHDPKLAAQCQRHYALIDGQLVEQ 237
Cdd:cd03244 165 EATASVDPETDALIQKTIRE---AFkDCTVLTIAHRLDTIIDSDRILVLDKGRVVEF 218
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
11-237 |
3.18e-21 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 88.99 E-value: 3.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 11 MPQTIiSAQNLTqkiqlAQKQLTIFENLNFDIQEGEQVAITGRSGSGKS----TLLGILATLDQASSGKLVVCGESIAEl 86
Cdd:PRK10418 1 MPQQI-ELRNIA-----LQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAP- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 87 neeqrAEVRLKHIGFVFQ----SFQllPHLTALENVMLPLRLQEKfkyAEAEQKALNLLKRVGLE---RQAQQTPKVLSG 159
Cdd:PRK10418 74 -----CALRGRKIATIMQnprsAFN--PLHTMHTHARETCLALGK---PADDATLTAALEAVGLEnaaRVLKLYPFEMSG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491113568 160 GEQQRVAIARALIREPKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDPKLAAQCQRHYALID-GQLVEQ 237
Cdd:PRK10418 144 GMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMShGRIVEQ 222
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
11-215 |
5.18e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 89.48 E-value: 5.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 11 MPQTIISAQNLTQKIqlaqKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAElneeq 90
Cdd:PRK13537 3 MSVAPIDFRNVEKRY----GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 91 RAEVRLKHIGFVFQSFQLLPHLTALENVMLPLRLqekFKYAEAEQKAL--NLLKRVGLERQAQQTPKVLSGGEQQRVAIA 168
Cdd:PRK13537 74 RARHARQRVGVVPQFDNLDPDFTVRENLLVFGRY---FGLSAAAARALvpPLLEFAKLENKADAKVGELSGGMKRRLTLA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491113568 169 RALIREPKIIFADEPTGNLDGETateiEQLLFELNREL---GTTLVLVTH 215
Cdd:PRK13537 151 RALVNDPDVLVLDEPTTGLDPQA----RHLMWERLRSLlarGKTILLTTH 196
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
15-237 |
5.75e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 89.09 E-value: 5.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 15 IISAQNLTQKIQLAQKQLtifENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEqraEV 94
Cdd:PRK13652 3 LIETRDLCYSYSGSKEAL---NNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIR---EV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 95 RlKHIGFVFQSF--QLLPHLTALENVMLPLRLqeKFKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALI 172
Cdd:PRK13652 77 R-KFVGLVFQNPddQIFSPTVEQDIAFGPINL--GLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491113568 173 REPKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDPKLAAQCQRH-YALIDGQLVEQ 237
Cdd:PRK13652 154 MEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYiYVMDKGRIVAY 219
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
37-237 |
6.25e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 89.07 E-value: 6.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 37 NLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAEVRLKHIGFVFQ--SFQLLPHLTA 114
Cdd:PRK13646 25 DVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPVRKRIGMVFQfpESQLFEDTVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 115 LENVMLPLRLqeKFKYAEAEQKALNLLKRVGLERQA-QQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETAT 193
Cdd:PRK13646 105 REIIFGPKNF--KMNLDEVKNYAHRLLMDLGFSRDVmSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKR 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491113568 194 EIEQLLFELNRELGTTLVLVTHDPKLAAQcqrhYA-----LIDGQLVEQ 237
Cdd:PRK13646 183 QVMRLLKSLQTDENKTIILVSHDMNEVAR----YAdevivMKEGSIVSQ 227
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
7-215 |
6.41e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 89.52 E-value: 6.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 7 ESNIMPQTIISAQNLTQKIQLAQ-KQLTIFENLNFDIQEGEQVAITGRSGSGKSTLL-----------GILATLDQASSG 74
Cdd:PRK13631 13 PNPLSDDIILRVKNLYCVFDEKQeNELVALNNISYTFEKNKIYFIIGNSGSGKSTLVthfnglikskyGTIQVGDIYIGD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 75 KLVVCGESIAELNEEQRAEVRL-KHIGFVFQ--SFQLLPHlTALENVML-PLRLQEKfKYaEAEQKALNLLKRVGL-ERQ 149
Cdd:PRK13631 93 KKNNHELITNPYSKKIKNFKELrRRVSMVFQfpEYQLFKD-TIEKDIMFgPVALGVK-KS-EAKKLAKFYLNKMGLdDSY 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491113568 150 AQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETATEIEQLLFELNRElGTTLVLVTH 215
Cdd:PRK13631 170 LERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITH 234
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
16-217 |
7.79e-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: 86.64 E-value: 7.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 16 ISAQNLTqkiqLAQKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEqraevR 95
Cdd:TIGR01189 1 LAARNLA----CSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDE-----P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 96 LKHIGFVFQSFQLLPHLTALENvmlpLRLQEKFkYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREP 175
Cdd:TIGR01189 72 HENILYLGHLPGLKPELSALEN----LHFWAAI-HGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRR 146
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 491113568 176 KIIFADEPTGNLDGETATEIEQlLFELNRELGTTLVLVTHDP 217
Cdd:TIGR01189 147 PLWILDEPTTALDKAGVALLAG-LLRAHLARGGIVLLTTHQD 187
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
14-249 |
8.33e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 90.46 E-value: 8.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 14 TIISAQNLTQKiqlaqkqlTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGEsiaelneeqraE 93
Cdd:COG1129 255 VVLEVEGLSVG--------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGK-----------P 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 94 VRLKHI------GFVF-----QSFQLLPHLTALENVMLP----------LRLQEKFKYAEAEQKALNLlKRVGLERQAQQ 152
Cdd:COG1129 316 VRIRSPrdairaGIAYvpedrKGEGLVLDLSIRENITLAsldrlsrgglLDRRRERALAEEYIKRLRI-KTPSPEQPVGN 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 153 tpkvLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETATEIEQLLFELNRElGTTLVLVTHD-PKLAAQCQRHYALID 231
Cdd:COG1129 395 ----LSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSElPELLGLSDRILVMRE 469
|
250 260
....*....|....*....|....
gi 491113568 232 GQLVEQFAAKPT------AAITGG 249
Cdd:COG1129 470 GRIVGELDREEAteeaimAAATGG 493
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
35-216 |
2.26e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 87.35 E-value: 2.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 35 FENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQraEVRlKHIGFVFQS--FQLLPHL 112
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQ--GIR-KLVGIVFQNpeTQFVGRT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 113 T------ALENVMLP-LRLQEKFKYAEAEqkalnllkrVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTG 185
Cdd:PRK13644 95 VeedlafGPENLCLPpIEIRKRVDRALAE---------IGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTS 165
|
170 180 190
....*....|....*....|....*....|.
gi 491113568 186 NLDGETATEIEQLLFELNRElGTTLVLVTHD 216
Cdd:PRK13644 166 MLDPDSGIAVLERIKKLHEK-GKTIVYITHN 195
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
16-237 |
2.93e-20 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 86.29 E-value: 2.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 16 ISAQNLTQKIQlaqkQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAevr 95
Cdd:COG4604 2 IEIKNVSKRYG----GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELA--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 96 lKHIGFVFQSFQLLPHLTALENVML---P-----LRLQEKFKYAEAeqkalnlLKRVGLERQAQQTPKVLSGGEQQRVAI 167
Cdd:COG4604 75 -KRLAILRQENHINSRLTVRELVAFgrfPyskgrLTAEDREIIDEA-------IAYLDLEDLADRYLDELSGGQRQRAFI 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491113568 168 ARALIREPKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDPKLAAqcqrHY-----ALIDGQLVEQ 237
Cdd:COG4604 147 AMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFAS----CYadhivAMKDGRVVAQ 217
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
20-215 |
3.38e-20 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 88.01 E-value: 3.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 20 NLTQkiQLAQKQLTIFENLNfdiqeGEQV-AITGRSGSGKSTLLGILATLDQASSGKLVVCG------ESIAELNEEQRa 92
Cdd:PRK11144 5 NFKQ--QLGDLCLTVNLTLP-----AQGItAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdaEKGICLPPEKR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 93 evrlkHIGFVFQSFQLLPHLTALENvmlplrLQEKFKYAEAEQ--KALNLLkrvGLERQAQQTPKVLSGGEQQRVAIARA 170
Cdd:PRK11144 77 -----RIGYVFQDARLFPHYKVRGN------LRYGMAKSMVAQfdKIVALL---GIEPLLDRYPGSLSGGEKQRVAIGRA 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 491113568 171 LIREPKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTH 215
Cdd:PRK11144 143 LLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSH 187
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
34-233 |
4.06e-20 |
|
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: 84.83 E-value: 4.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 34 IFENLNFDIQEGEQVAITGRSGSGKSTLL-GILATLdQASSGKLVVCGesiaelneeqraevrlkHIGFVFQSFQLLPhL 112
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLsALLGEL-EKLSGSVSVPG-----------------SIAYVSQEPWIQN-G 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 113 TALENVMLPLRLQEKfKYAEAeqkalnlLKRVGLERQAQQTPK-----------VLSGGEQQRVAIARALIREPKIIFAD 181
Cdd:cd03250 81 TIRENILFGKPFDEE-RYEKV-------IKACALEPDLEILPDgdlteigekgiNLSGGQKQRISLARAVYSDADIYLLD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491113568 182 EPTGNLDGETATEI-EQLLFELNRElGTTLVLVTHDPKLAAQCQRHYALIDGQ 233
Cdd:cd03250 153 DPLSAVDAHVGRHIfENCILGLLLN-NKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
37-215 |
4.27e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 86.71 E-value: 4.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 37 NLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAEVRLKHIGFVFQ--SFQLLPHlTA 114
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQfpESQLFEE-TV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 115 LENVMLPlrlQEKFKYA--EAEQKALNLLKRVGLERQA-QQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGET 191
Cdd:PRK13643 103 LKDVAFG---PQNFGIPkeKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180
....*....|....*....|....
gi 491113568 192 ATEIEQlLFELNRELGTTLVLVTH 215
Cdd:PRK13643 180 RIEMMQ-LFESIHQSGQTVVLVTH 202
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
15-214 |
5.31e-20 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 85.47 E-value: 5.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 15 IISAQNLTQKIqlaqKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAev 94
Cdd:COG1137 3 TLEAENLVKSY----GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRA-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 95 RLKhIGF------VFQsfqllpHLTALENVMLPLRLQEKFKyAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIA 168
Cdd:COG1137 77 RLG-IGYlpqeasIFR------KLTVEDNILAVLELRKLSK-KEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491113568 169 RALIREPKIIFADEPTGNLDGETATEIEQLLFEL-NRELGttlVLVT 214
Cdd:COG1137 149 RALATNPKFILLDEPFAGVDPIAVADIQKIIRHLkERGIG---VLIT 192
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
33-217 |
8.27e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 84.16 E-value: 8.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 33 TIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAeVRLKHIGFvfqsfqLLPHL 112
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEAC-HYLGHRNA------MKPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 113 TALENvmlpLRLQEKFkYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETA 192
Cdd:PRK13539 89 TVAEN----LEFWAAF-LGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAV 163
|
170 180
....*....|....*....|....*
gi 491113568 193 TEIEQLLFElNRELGTTLVLVTHDP 217
Cdd:PRK13539 164 ALFAELIRA-HLAQGGIVIAATHIP 187
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
34-215 |
9.45e-20 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 84.44 E-value: 9.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 34 IFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAEVrlkhIGFVFQSFQLLPHlT 113
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK----VSLVGQEPVLFAR-S 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 114 ALENVMLPLRLQEKFKYAEAEQKA-----LNLLKRvGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLD 188
Cdd:cd03248 104 LQDNIAYGLQSCSFECVKEAAQKAhahsfISELAS-GYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALD 182
|
170 180
....*....|....*....|....*..
gi 491113568 189 GETATEIEQLLFELNRElgTTLVLVTH 215
Cdd:cd03248 183 AESEQQVQQALYDWPER--RTVLVIAH 207
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
25-219 |
1.08e-19 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 84.24 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 25 IQLAQKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILAtldQASSGKLVVCgesiaelneeqRAEVRLKHIGfvfQ 104
Cdd:COG2401 36 VELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLA---GALKGTPVAG-----------CVDVPDNQFG---R 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 105 SFQLLPHLTALENVMLplrlqekfkyaeaeqkALNLLKRVGLErQAQ---QTPKVLSGGEQQRVAIARALIREPKIIFAD 181
Cdd:COG2401 99 EASLIDAIGRKGDFKD----------------AVELLNAVGLS-DAVlwlRRFKELSTGQKFRFRLALLLAERPKLLVID 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 491113568 182 EPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDPKL 219
Cdd:COG2401 162 EFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDV 199
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
16-233 |
1.09e-19 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 82.11 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 16 ISAQNLTqkiqLAQKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLvvcgESIAELNeeqraevr 95
Cdd:cd03221 1 IELENLS----KTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV----TWGSTVK-------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 96 lkhIGFVFQsfqllphltalenvmlplrlqekfkyaeaeqkalnllkrvglerqaqqtpkvLSGGEQQRVAIARALIREP 175
Cdd:cd03221 65 ---IGYFEQ----------------------------------------------------LSGGEKMRLALAKLLLENP 89
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491113568 176 KIIFADEPTGNLDGETATEIEQLLFELNRelgtTLVLVTHDPKLAAQ-CQRHYALIDGQ 233
Cdd:cd03221 90 NLLLLDEPTNHLDLESIEALEEALKEYPG----TVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
22-237 |
1.33e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 84.68 E-value: 1.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 22 TQKIQLAQKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAevrlKHIGF 101
Cdd:PRK11231 5 TENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA----RRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 102 VFQsfqllpHLTALENVmlplRLQEKFKY-------------AEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIA 168
Cdd:PRK11231 81 LPQ------HHLTPEGI----TVRELVAYgrspwlslwgrlsAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 169 RALIREPKIIFADEPTGNLDGETATEIEQLLFELNRElGTTLVLVTHDPKLAAQ-CQRHYALIDGQLVEQ 237
Cdd:PRK11231 151 MVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRyCDHLVVLANGHVMAQ 219
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
31-235 |
1.44e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 84.55 E-value: 1.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 31 QLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELneeQRAEVRLKHIGFVFQSFQLLP 110
Cdd:PRK11614 17 KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDW---QTAKIMREAVAIVPEGRRVFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 111 HLTALENVMLPLRLQEKFKYAEAEQKALNLLKRVgLERQAQQTpKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGE 190
Cdd:PRK11614 94 RMTVEENLAMGGFFAERDQFQERIKWVYELFPRL-HERRIQRA-GTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPI 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491113568 191 TATEIEQLLFELnRELGTTLVLVTHDPKLAAQ-CQRHYALIDGQLV 235
Cdd:PRK11614 172 IIQQIFDTIEQL-REQGMTIFLVEQNANQALKlADRGYVLENGHVV 216
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
36-212 |
1.60e-19 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 87.32 E-value: 1.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 36 ENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNeeqRAEVRlKHIGFVFQSfQLLPHLTAL 115
Cdd:PRK13657 352 EDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT---RASLR-RNIAVVFQD-AGLFNRSIE 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 116 ENVML------PLRLQEKFKYAEA----EQKALNLLKRVGlERQAQqtpkvLSGGEQQRVAIARALIREPKIIFADEPTG 185
Cdd:PRK13657 427 DNIRVgrpdatDEEMRAAAERAQAhdfiERKPDGYDTVVG-ERGRQ-----LSGGERQRLAIARALLKDPPILILDEATS 500
|
170 180
....*....|....*....|....*....
gi 491113568 186 NLDGETATEIEQLLFEL--NRelgTTLVL 212
Cdd:PRK13657 501 ALDVETEAKVKAALDELmkGR---TTFII 526
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
11-216 |
1.61e-19 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 87.10 E-value: 1.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 11 MPQTIISAQNLTqKIQLAQKQltIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGklvvcgesiaelneeq 90
Cdd:PRK11819 2 MAQYIYTMNRVS-KVVPPKKQ--ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG---------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 91 raEVRLK---HIGFVFQSFQLLPHLTALENVMLPLR----LQEKF-----KYAEAEQKALNLLKRVG------------- 145
Cdd:PRK11819 63 --EARPApgiKVGYLPQEPQLDPEKTVRENVEEGVAevkaALDRFneiyaAYAEPDADFDALAAEQGelqeiidaadawd 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 146 LERQ------AQQTP------KVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETATEIEQLLfelnRELGTTLVLV 213
Cdd:PRK11819 141 LDSQleiamdALRCPpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFL----HDYPGTVVAV 216
|
...
gi 491113568 214 THD 216
Cdd:PRK11819 217 THD 219
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
45-247 |
2.33e-19 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 86.60 E-value: 2.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 45 GEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAEVrlkHIGFVFQSFQLLPHLTALENVMLPL-- 122
Cdd:PRK10762 30 GRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEA---GIGIIHQELNLIPQLTIAENIFLGRef 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 123 -----RLQEKFKYAEAEQkalnLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTgnlDGETATEIEQ 197
Cdd:PRK10762 107 vnrfgRIDWKKMYAEADK----LLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPT---DALTDTETES 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491113568 198 lLFELNREL---GTTLVLVTHDPKLAAQ-CQRHYALIDGQLVeqfAAKPTAAIT 247
Cdd:PRK10762 180 -LFRVIRELksqGRGIVYISHRLKEIFEiCDDVTVFRDGQFI---AEREVADLT 229
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
33-236 |
2.91e-19 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 83.35 E-value: 2.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 33 TIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGE--SIAELNeeqraevrlkhIGFvfqsfqlLP 110
Cdd:cd03220 36 WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRvsSLLGLG-----------GGF-------NP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 111 HLTALENVMLPLRLQeKFKYAEAEQKALNLLKRVGLErQAQQTP-KVLSGGEQQRVAIARALIREPKIIFADEPTGNLDG 189
Cdd:cd03220 98 ELTGRENIYLNGRLL-GLSRKEIDEKIDEIIEFSELG-DFIDLPvKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491113568 190 ETATEIEQLLFELNRElGTTLVLVTHDPKLAAQ-CQRHYALIDGQLVE 236
Cdd:cd03220 176 AFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRlCDRALVLEKGKIRF 222
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
35-216 |
3.34e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 84.29 E-value: 3.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 35 FENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESI-AELNEEQRAEVRLKHIGFVFQ--SFQLLPH 111
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpANLKKIKEVKRLRKEIGLVFQfpEYQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 112 LTALENVMLPLRLQEKFKyaEAEQKALNLLKRVGLERQ-AQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGE 190
Cdd:PRK13645 107 TIEKDIAFGPVNLGENKQ--EAYKKVPELLKLVQLPEDyVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPK 184
|
170 180
....*....|....*....|....*.
gi 491113568 191 TATEIEQLLFELNRELGTTLVLVTHD 216
Cdd:PRK13645 185 GEEDFINLFERLNKEYKKRIIMVTHN 210
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-237 |
5.49e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 83.61 E-value: 5.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 16 ISAQNLTqkIQLAQKqlTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATL-DQAS----SGKLVVCGESIaeLNEEQ 90
Cdd:PRK14271 22 MAAVNLT--LGFAGK--TVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMnDKVSgyrySGDVLLGGRSI--FNYRD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 91 RAEVRlKHIGFVFQSFQLLPhLTALENVMLPLRLQEKFKYAEAEQKALNLLKRVGL----ERQAQQTPKVLSGGEQQRVA 166
Cdd:PRK14271 96 VLEFR-RRVGMLFQRPNPFP-MSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLC 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491113568 167 IARALIREPKIIFADEPTGNLDGETATEIEQLLFELNRELgtTLVLVTHDPKLAAQCQRHYAL-IDGQLVEQ 237
Cdd:PRK14271 174 LARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALfFDGRLVEE 243
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
34-237 |
1.22e-18 |
|
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: 84.79 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 34 IFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNeeqRAEVRlKHIGFVFQSfqllPHL- 112
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDID---RHTLR-QFINYLPQE----PYIf 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 113 --TALENVML---PLRLQEKFKYAE--AEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTG 185
Cdd:TIGR01193 561 sgSILENLLLgakENVSQDEIWAACeiAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTS 640
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491113568 186 NLDGETATEIEQLLFELNRElgtTLVLVTHDPKLAAQCQRHYALIDGQLVEQ 237
Cdd:TIGR01193 641 NLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQSDKIIVLDHGKIIEQ 689
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
33-235 |
1.25e-18 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 84.55 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 33 TIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASS--GKLVVcgesiaelNEEQRAEVRLKHIGFVFQSFQLLP 110
Cdd:PLN03211 82 TILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILA--------NNRKPTKQILKRTGFVTQDDILYP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 111 HLTALENVM------LP--LRLQEKFKYAEAEQKALNLLKrVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADE 182
Cdd:PLN03211 154 HLTVRETLVfcsllrLPksLTKQEKILVAESVISELGLTK-CENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDE 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491113568 183 PTGNLDGETATEIEQLLFELNRElGTTLVLVTHDPKlaaqcQRHYALIDGQLV 235
Cdd:PLN03211 233 PTSGLDATAAYRLVLTLGSLAQK-GKTIVTSMHQPS-----SRVYQMFDSVLV 279
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
34-216 |
1.49e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 82.01 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 34 IFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASS-----GKLVVCGESIAElneeQRAEV-RLK-HIGFVFQSF 106
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYE----RRVNLnRLRrQVSMVHPKP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 107 QLLPhLTALENVMLPLRL------QEKFKYAEAEQKALNLLKRVglERQAQQTPKVLSGGEQQRVAIARALIREPKIIFA 180
Cdd:PRK14258 98 NLFP-MSVYDNVAYGVKIvgwrpkLEIDDIVESALKDADLWDEI--KHKIHKSALDLSGGQQQRLCIARALAVKPKVLLM 174
|
170 180 190
....*....|....*....|....*....|....*.
gi 491113568 181 DEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHD 216
Cdd:PRK14258 175 DEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHN 210
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
36-216 |
1.91e-18 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 83.85 E-value: 1.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 36 ENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGE-SIAELNEEQRAEVR----------LKHIGFVFQ 104
Cdd:PRK11147 20 DNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDlIVARLQQDPPRNVEgtvydfvaegIEEQAEYLK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 105 SFQLLPHLTALE----NVMLPLRLQEKFKYAEA---EQKALNLLKRVGLERQAQQTPkvLSGGEQQRVAIARALIREPKI 177
Cdd:PRK11147 100 RYHDISHLVETDpsekNLNELAKLQEQLDHHNLwqlENRINEVLAQLGLDPDAALSS--LSGGWLRKAALGRALVSNPDV 177
|
170 180 190
....*....|....*....|....*....|....*....
gi 491113568 178 IFADEPTGNLDGETATEIEQLLfelnRELGTTLVLVTHD 216
Cdd:PRK11147 178 LLLDEPTNHLDIETIEWLEGFL----KTFQGSIIFISHD 212
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
34-215 |
2.84e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 82.57 E-value: 2.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 34 IFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAElneeqRAEVRLKHIGFVFQSFQLLPHLT 113
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-----RARLARARIGVVPQFDNLDLEFT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 114 ALENVMLPLRLQeKFKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETat 193
Cdd:PRK13536 131 VRENLLVFGRYF-GMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHA-- 207
|
170 180
....*....|....*....|....*
gi 491113568 194 eiEQLLFELNREL---GTTLVLVTH 215
Cdd:PRK13536 208 --RHLIWERLRSLlarGKTILLTTH 230
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
14-216 |
2.98e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 83.15 E-value: 2.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 14 TIISAQNLTQKiqlAQKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNeeqRAE 93
Cdd:COG3845 256 VVLEVENLSVR---DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLS---PRE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 94 VRLKHIGFV---FQSFQLLPHLTALENVMLPLRLQEKF------KYAEAEQKALNLLKRVGLERQAQQTP-KVLSGGEQQ 163
Cdd:COG3845 330 RRRLGVAYIpedRLGRGLVPDMSVAENLILGRYRRPPFsrggflDRKAIRAFAEELIEEFDVRTPGPDTPaRSLSGGNQQ 409
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491113568 164 RVAIARALIREPKIIFADEPTGNLDGETATEIEQLLFELnRELGTTLVLVTHD 216
Cdd:COG3845 410 KVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISED 461
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
37-216 |
4.05e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 81.31 E-value: 4.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 37 NLNFDIQEGEQVAITGRSGSGKSTL----LGILAtldqASSGKLVVCGEsiaELNEEQRAevrlkHIGFvfqsfqlLPH- 111
Cdd:COG4152 19 DVSFTVPKGEIFGLLGPNGAGKTTTiriiLGILA----PDSGEVLWDGE---PLDPEDRR-----RIGY-------LPEe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 112 ------LTALENVMLPLRL--QEKfkyAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEP 183
Cdd:COG4152 80 rglypkMKVGEQLVYLARLkgLSK---AEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEP 156
|
170 180 190
....*....|....*....|....*....|...
gi 491113568 184 TGNLDGETATEIEQLLFELNRElGTTLVLVTHD 216
Cdd:COG4152 157 FSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQ 188
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
34-236 |
1.01e-17 |
|
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: 78.34 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 34 IFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLD--QASSGKLVVCGESIAELNEEQRAevRLkhiGfVFQSFQLLPH 111
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERA--RL---G-IFLAFQYPPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 112 LTALENVMLpLR-LQEKFkyaeaeqkalnllkrvglerqaqqtpkvlSGGEQQRVAIARALIREPKIIFADEPTGNLDGE 190
Cdd:cd03217 89 IPGVKNADF-LRyVNEGF-----------------------------SGGEKKRNEILQLLLLEPDLAILDEPDSGLDID 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491113568 191 TATEIEQLLFELnRELGTTLVLVTHDPKLAAQCQ--RHYALIDGQLVE 236
Cdd:cd03217 139 ALRLVAEVINKL-REEGKSVLIITHYQRLLDYIKpdRVHVLYDGRIVK 185
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
36-215 |
1.70e-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: 81.60 E-value: 1.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 36 ENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIaelneEQRAEVRLKHIGFVFQSFQLLPHLTAL 115
Cdd:TIGR01257 947 DRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-----ETNLDAVRQSLGMCPQHNILFHHLTVA 1021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 116 ENVMLPLRLQEKfKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETATEI 195
Cdd:TIGR01257 1022 EHILFYAQLKGR-SWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSI 1100
|
170 180
....*....|....*....|
gi 491113568 196 EQLLfeLNRELGTTLVLVTH 215
Cdd:TIGR01257 1101 WDLL--LKYRSGRTIIMSTH 1118
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
36-212 |
5.34e-17 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 79.68 E-value: 5.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 36 ENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGEsiaELNEEQRAEVRlKHIGFVFQSFQLLpHLTAL 115
Cdd:PRK11176 360 RNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGH---DLRDYTLASLR-NQVALVSQNVHLF-NDTIA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 116 ENVMLPLrlQEKFKYAEAEQKA--------LNLLKRvGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNL 187
Cdd:PRK11176 435 NNIAYAR--TEQYSREQIEEAArmayamdfINKMDN-GLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSAL 511
|
170 180
....*....|....*....|....*..
gi 491113568 188 DGETATEIEQLLFEL--NRelgTTLVL 212
Cdd:PRK11176 512 DTESERAIQAALDELqkNR---TSLVI 535
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
33-249 |
8.72e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 78.73 E-value: 8.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 33 TIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNE----EQRAEV-RLKHIGFVFQSFQ 107
Cdd:PRK09536 17 TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSAraasRRVASVpQDTSLSFEFDVRQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 108 LL-----PHLTALEnvmlplrlqekfKYAEAEQKALN-LLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFAD 181
Cdd:PRK09536 97 VVemgrtPHRSRFD------------TWTETDRAAVErAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLD 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491113568 182 EPTGNLDGETAteIEQLlfELNREL---GTTLVLVTHDPKLAAQ-CQRHYALIDGQLVEqfAAKPTAAITGG 249
Cdd:PRK09536 165 EPTASLDINHQ--VRTL--ELVRRLvddGKTAVAAIHDLDLAARyCDELVLLADGRVRA--AGPPADVLTAD 230
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
36-236 |
9.28e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 77.13 E-value: 9.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 36 ENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQ-----ASSGKLVVCGESIAElNEEQRAEVRlKHIGFVFQSFQLLP 110
Cdd:PRK14243 27 KNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLYA-PDVDPVEVR-RRIGMVFQKPNPFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 111 HlTALENVMLPLRLQE-KFKYAEAEQKALnllkrvgleRQA----------QQTPKVLSGGEQQRVAIARALIREPKIIF 179
Cdd:PRK14243 105 K-SIYDNIAYGARINGyKGDMDELVERSL---------RQAalwdevkdklKQSGLSLSGGQQQRLCIARAIAVQPEVIL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491113568 180 ADEPTGNLDGETATEIEQLLFELNRELgtTLVLVTHDPKLAAQCQRHYALIDGQLVE 236
Cdd:PRK14243 175 MDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDMTAFFNVELTE 229
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
33-237 |
1.10e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 76.66 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 33 TIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGE--SIAELNeeqraevrlkhIGFVfqsfqllP 110
Cdd:COG1134 40 WALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRvsALLELG-----------AGFH-------P 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 111 HLTALENVMLPLRLQeKFKYAEAEQKalnlLKRV----GLERQAQQtP-KVLSGGEQQRVAIARALIREPKIIFADEPTG 185
Cdd:COG1134 102 ELTGRENIYLNGRLL-GLSRKEIDEK----FDEIvefaELGDFIDQ-PvKTYSSGMRARLAFAVATAVDPDILLVDEVLA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491113568 186 NLDGETATEIEQLLFELnRELGTTLVLVTHDPKLAAQ-CQRhyALI--DGQLVEQ 237
Cdd:COG1134 176 VGDAAFQKKCLARIREL-RESGRTVIFVSHSMGAVRRlCDR--AIWleKGRLVMD 227
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
23-216 |
1.14e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 76.69 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 23 QKIQLAQKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLvvcgesiaelneEQRAEVRlkhIGFV 102
Cdd:PRK09544 8 ENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------------KRNGKLR---IGYV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 103 FQSFQLLPhltalenvMLPLRLQEKFKYAEAEQKA--LNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFA 180
Cdd:PRK09544 73 PQKLYLDT--------TLPLTVNRFLRLRPGTKKEdiLPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVL 144
|
170 180 190
....*....|....*....|....*....|....*.
gi 491113568 181 DEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHD 216
Cdd:PRK09544 145 DEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHD 180
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
33-219 |
1.27e-16 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 76.26 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 33 TIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLD--QASSGKLVVCGESIAELNEEQRAevrLKHIGFVFQS----- 105
Cdd:COG0396 14 EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDERA---RAGIFLAFQYpveip 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 106 ----FQLLphLTALENvmlplRLQEKFKYAEAEQKALNLLKRVG-----LERQAQQTpkvLSGGEQQRVAIARALIREPK 176
Cdd:COG0396 91 gvsvSNFL--RTALNA-----RRGEELSAREFLKLLKEKMKELGldedfLDRYVNEG---FSGGEKKRNEILQMLLLEPK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491113568 177 IIFADEPTGNLDGET----ATEIEQLlfelnRELGTTLVLVTHDPKL 219
Cdd:COG0396 161 LAILDETDSGLDIDAlrivAEGVNKL-----RSPDRGILIITHYQRI 202
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
15-239 |
1.82e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 76.67 E-value: 1.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 15 IISAQNLTQKIQlAQKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGEsiaELNEEQRAEV 94
Cdd:PRK13642 4 ILEVENLVFKYE-KESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE---LLTAENVWNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 95 RLKhIGFVFQS--FQLLPHLT------ALENVMLPLrlQEKFKYAEAEQKALNLLKRVGLErqaqqtPKVLSGGEQQRVA 166
Cdd:PRK13642 80 RRK-IGMVFQNpdNQFVGATVeddvafGMENQGIPR--EEMIKRVDEALLAVNMLDFKTRE------PARLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491113568 167 IARALIREPKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDPKLAAQCQRHYALIDGQLVEQFA 239
Cdd:PRK13642 151 VAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAA 223
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
8-244 |
2.30e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 77.90 E-value: 2.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 8 SNIMPQTIISAQNLTQKiqlAQKQLtifENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELN 87
Cdd:PRK09700 258 SNLAHETVFEVRNVTSR---DRKKV---RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRS 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 88 EEQRAEvrlKHIGFVFQSFQ---LLPHLTALENVMLPLRLQ--------------EKFKYAEAEQKALNLlKRVGLErqa 150
Cdd:PRK09700 332 PLDAVK---KGMAYITESRRdngFFPNFSIAQNMAISRSLKdggykgamglfhevDEQRTAENQRELLAL-KCHSVN--- 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 151 qQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDPKLAAQCQRHYALI 230
Cdd:PRK09700 405 -QNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFC 483
|
250
....*....|....
gi 491113568 231 DGQLVEQFAAKPTA 244
Cdd:PRK09700 484 EGRLTQILTNRDDM 497
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
15-211 |
2.92e-16 |
|
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: 74.61 E-value: 2.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 15 IISAQNLTQKIQLAQKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATL---DQASSGKLVVCGESIAELNEEQR 91
Cdd:cd03233 3 TLSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtegNVSVEGDIHYNGIPYKEFAEKYP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 92 AEvrlkhIGFVFQSFQLLPHLTalenvmlplrLQEKFKYAeaeqkalnllkrvgLERQAQQTPKVLSGGEQQRVAIARAL 171
Cdd:cd03233 83 GE-----IIYVSEEDVHFPTLT----------VRETLDFA--------------LRCKGNEFVRGISGGERKRVSIAEAL 133
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 491113568 172 IREPKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLV 211
Cdd:cd03233 134 VSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTF 173
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
38-235 |
3.75e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 77.01 E-value: 3.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 38 LNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAEVrlkHIGFVFQSFQLLPHLTALEN 117
Cdd:PRK15439 30 IDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQL---GIYLVPQEPLLFPNLSVKEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 118 VMLPLRlqekfKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLdgeTATEIEQ 197
Cdd:PRK15439 107 ILFGLP-----KRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASL---TPAETER 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 491113568 198 LLFELN--RELGTTLVLVTHD-PKLAAQCQRHYALIDGQLV 235
Cdd:PRK15439 179 LFSRIRelLAQGVGIVFISHKlPEIRQLADRISVMRDGTIA 219
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
15-215 |
3.90e-16 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 74.50 E-value: 3.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 15 IISAQNLTqkiqLAQKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIaelneeQRAEv 94
Cdd:PRK13543 11 LLAAHALA----FSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTA------TRGD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 95 RLKHIGFVFQSFQLLPHLTALENVMLPLRLQEKfkyaEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIRE 174
Cdd:PRK13543 80 RSRFMAYLGHLPGLKADLSTLENLHFLCGLHGR----RAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 491113568 175 PKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVlVTH 215
Cdd:PRK13543 156 APLWLLDEPYANLDLEGITLVNRMISAHLRGGGAALV-TTH 195
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
11-236 |
4.04e-16 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 76.38 E-value: 4.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 11 MPqtIISAQNLTQKIQLAQKQLTIFENLNFDIQEGEQVAITGRSGSGKS----TLLGILATLDQASSGKLVVCGESIAEL 86
Cdd:PRK15093 1 MP--LLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSliakAICGVTKDNWRVTADRMRFDDIDLLRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 87 NEEQRAEVRLKHIGFVFQSFQLLphLTALENVMLPL-----------RLQEKFKYAEaeQKALNLLKRVGLERQA---QQ 152
Cdd:PRK15093 79 SPRERRKLVGHNVSMIFQEPQSC--LDPSERVGRQLmqnipgwtykgRWWQRFGWRK--RRAIELLHRVGIKDHKdamRS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 153 TPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDPKLAAQ-CQRHYALID 231
Cdd:PRK15093 155 FPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQwADKINVLYC 234
|
....*
gi 491113568 232 GQLVE 236
Cdd:PRK15093 235 GQTVE 239
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
27-215 |
7.80e-16 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 76.61 E-value: 7.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 27 LAQKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATL-DQASSGKLVVCGESIAELNEEQRAE------VRLKHI 99
Cdd:PTZ00265 1176 ISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFyDLKNDHHIVFKNEHTNDMTNEQDYQgdeeqnVGMKNV 1255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 100 G--------------------------------FVFQSFQLLPHLTALENVMLPLRLQEKFKYAEaEQKALNLLKRV--- 144
Cdd:PTZ00265 1256 NefsltkeggsgedstvfknsgkilldgvdicdYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGK-EDATREDVKRAckf 1334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 145 -GLERQAQQTP-----------KVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVL 212
Cdd:PTZ00265 1335 aAIDEFIESLPnkydtnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIIT 1414
|
...
gi 491113568 213 VTH 215
Cdd:PTZ00265 1415 IAH 1417
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
37-215 |
1.08e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 75.74 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 37 NLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASS--GKLVVCGESIAELN--EEQRAEVRLKHigfvfQSFQLLPHL 112
Cdd:PRK13549 23 NVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELQASNirDTERAGIAIIH-----QELALVKEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 113 TALENVMLPLRLQEK--FKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLdge 190
Cdd:PRK13549 98 SVLENIFLGNEITPGgiMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASL--- 174
|
170 180
....*....|....*....|....*...
gi 491113568 191 TATEIEQLLfELNREL---GTTLVLVTH 215
Cdd:PRK13549 175 TESETAVLL-DIIRDLkahGIACIYISH 201
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
33-237 |
1.34e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 74.05 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 33 TIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAevrlKHIGFVFQSFQLLPHL 112
Cdd:PRK10575 25 TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFA----RKVAYLPQQLPAAEGM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 113 TALENVML---PLRLQEKFKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDG 189
Cdd:PRK10575 101 TVRELVAIgryPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDI 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491113568 190 ETATEIEQLLFELNRELGTTLVLVTHDPKLAAQ-CQRHYALIDGQLVEQ 237
Cdd:PRK10575 181 AHQVDVLALVHRLSQERGLTVIAVLHDINMAARyCDYLVALRGGEMIAQ 229
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
33-211 |
1.35e-15 |
|
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: 75.63 E-value: 1.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 33 TIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELneeQRAEVRlKHIGFVfqsfqllPHL 112
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDV---TQASLR-AAIGIV-------PQD 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 113 TAL------ENVmlplrlqekfKY-------AEAEQKAlnllkrvgleRQAQ------QTPK-----V------LSGGEQ 162
Cdd:COG5265 441 TVLfndtiaYNI----------AYgrpdaseEEVEAAA----------RAAQihdfieSLPDgydtrVgerglkLSGGEK 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491113568 163 QRVAIARALIREPKIIFADEPTGNLDGETATEIEQLLFEL--NRelgTTLV 211
Cdd:COG5265 501 QRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVarGR---TTLV 548
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
32-217 |
4.65e-15 |
|
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: 71.37 E-value: 4.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 32 LTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEE-QRAEVRLKHIGFVFQSfqllp 110
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiARGLLYLGHAPGIKTT----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 111 hLTALENvmlpLRLQEKFKYAEAEQKALNLLKRVGLERQAQQTpkvLSGGEQQRVAIARALIREPKIIFADEPTGNLDGE 190
Cdd:cd03231 88 -LSVLEN----LRFWHADHSDEQVEEALARVGLNGFEDRPVAQ---LSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
170 180
....*....|....*....|....*..
gi 491113568 191 TATEIEQlLFELNRELGTTLVLVTHDP 217
Cdd:cd03231 160 GVARFAE-AMAGHCARGGMVVLTTHQD 185
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
34-236 |
7.72e-15 |
|
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: 70.90 E-value: 7.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 34 IFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEqraevRLKhigfvfQSFQLLPHLT 113
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLE-----DLR------SSLTIIPQDP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 114 ALENVMLPLRLQEKFKYAEAEQKALNLLKRVGLErqaqqtpkvLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETAT 193
Cdd:cd03369 92 TLFSGTIRSNLDPFDEYSDEEIYGALRVSEGGLN---------LSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 491113568 194 EIEQLLFELNRelGTTLVLVTHDPKLAAQCQRHYALIDGQLVE 236
Cdd:cd03369 163 LIQKTIREEFT--NSTILTIAHRLRTIIDYDKILVMDAGEVKE 203
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
16-225 |
9.59e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 73.24 E-value: 9.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 16 ISAQNLTQKiqlaqkqltiF------ENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEE 89
Cdd:NF033858 267 IEARGLTMR----------FgdftavDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 90 QRaevrlKHIGFVFQSFQLLPHLTALENVMLPLRLqekFKYAEAEQKAL--NLLKRVGLERQAQQTPKVLSGGEQQRVAI 167
Cdd:NF033858 337 TR-----RRVGYMSQAFSLYGELTVRQNLELHARL---FHLPAAEIAARvaEMLERFDLADVADALPDSLPLGIRQRLSL 408
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491113568 168 ARALIREPKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDPKLAAQCQR 225
Cdd:NF033858 409 AVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEAERCDR 466
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
36-219 |
9.63e-15 |
|
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: 73.24 E-value: 9.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 36 ENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVcgesiaelNEEQRaevrlkhIGFVFQSfqllPHL--- 112
Cdd:TIGR00954 469 ESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTK--------PAKGK-------LFYVPQR----PYMtlg 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 113 TALENVMLPLRLQEKFK--YAEAEQKAL-------NLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEP 183
Cdd:TIGR00954 530 TLRDQIIYPDSSEDMKRrgLSDKDLEQIldnvqltHILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDEC 609
|
170 180 190
....*....|....*....|....*....|....*.
gi 491113568 184 TGNLdgetATEIEQLLFELNRELGTTLVLVTHDPKL 219
Cdd:TIGR00954 610 TSAV----SVDVEGYMYRLCREFGITLFSVSHRKSL 641
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
32-247 |
1.22e-14 |
|
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: 72.94 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 32 LTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASS--GKLVVCGEsiaELNEEQRAEVRLKHIGFVFQSFQLL 109
Cdd:TIGR02633 14 VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGS---PLKASNIRDTERAGIVIIHQELTLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 110 PHLTALENVMLPLRLQEK---FKYAEAEQKALNLLKRVGLERQAQQTPKV-LSGGEQQRVAIARALIREPKIIFADEPTG 185
Cdd:TIGR02633 91 PELSVAENIFLGNEITLPggrMAYNAMYLRAKNLLRELQLDADNVTRPVGdYGGGQQQLVEIAKALNKQARLLILDEPSS 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491113568 186 NLdgeTATEIEQLLfELNREL---GTTLVLVTHD-PKLAAQCQRHYALIDGQLVeqfAAKPTAAIT 247
Cdd:TIGR02633 171 SL---TEKETEILL-DIIRDLkahGVACVYISHKlNEVKAVCDTICVIRDGQHV---ATKDMSTMS 229
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
36-219 |
1.68e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 72.13 E-value: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 36 ENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASS--GKLVVCGEsiaelneeqraEVRLKHI------GFVF--QS 105
Cdd:NF040905 18 DDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGE-----------VCRFKDIrdsealGIVIihQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 106 FQLLPHLTALENVMLPlrlQEKFKY-----AEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFA 180
Cdd:NF040905 87 LALIPYLSIAENIFLG---NERAKRgvidwNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLIL 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 491113568 181 DEPTGNLDGETATEIEQLLFELnRELGTTLVLVTHdpKL 219
Cdd:NF040905 164 DEPTAALNEEDSAALLDLLLEL-KAQGITSIIISH--KL 199
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
23-237 |
3.19e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 70.24 E-value: 3.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 23 QKIQLAQKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILA--------TLDQASSGKLVVCGESIAELNEEQRAEV 94
Cdd:PRK13547 5 DHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgdltgggaPRGARVTGDVTLNGEPLAAIDAPRLARL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 95 RlkhiGFVFQSFQLLPHLTALENVMLplrlqEKFKYAEAEQK--------ALNLLKRVGLERQAQQTPKVLSGGEQQRVA 166
Cdd:PRK13547 85 R----AVLPQAAQPAFAFSAREIVLL-----GRYPHARRAGAlthrdgeiAWQALALAGATALVGRDVTTLSGGELARVQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 167 IARAL---------IREPKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDPKLAAQCQRHYALI-DGQLVE 236
Cdd:PRK13547 156 FARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLaDGAIVA 235
|
.
gi 491113568 237 Q 237
Cdd:PRK13547 236 H 236
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
34-219 |
4.91e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 69.29 E-value: 4.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 34 IFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLD--QASSGKLVVCGESIAELNEEQRAevrlkHIGfVFQSFQLLPH 111
Cdd:CHL00131 22 ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEERA-----HLG-IFLAFQYPIE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 112 LTALENVMLpLRLQEKfkyaeAEQKALNL---------------LKRVGLErqaqqtPKVL--------SGGEQQRVAIA 168
Cdd:CHL00131 96 IPGVSNADF-LRLAYN-----SKRKFQGLpeldplefleiinekLKLVGMD------PSFLsrnvnegfSGGEKKRNEIL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491113568 169 RALIREPKIIFADEPTGNLD----GETATEIEQLlfelnRELGTTLVLVTHDPKL 219
Cdd:CHL00131 164 QMALLDSELAILDETDSGLDidalKIIAEGINKL-----MTSENSIILITHYQRL 213
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
38-236 |
6.81e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 70.39 E-value: 6.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 38 LNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGEsiaELNEEQRAEVRlKHIGFVFQSFQLLPHLTALEN 117
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGK---PVTAEQPEDYR-KLFSAVFTDFHLFDQLLGPEG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 118 vmlplrLQEKFKYAEAEQKALNLLKRVGLERQAQQTPKvLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETATEIEQ 197
Cdd:PRK10522 418 ------KPANPALVEKWLERLKMAHKLELEDGRISNLK-LSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQ 490
|
170 180 190
....*....|....*....|....*....|....*....
gi 491113568 198 LLFELNRELGTTLVLVTHDPKLAAQCQRHYALIDGQLVE 236
Cdd:PRK10522 491 VLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
38-237 |
2.01e-13 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 67.56 E-value: 2.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 38 LNFDIQEGEQVAITGRSGSGKSTLLGILATLdQASSGKLVVCGESIAELNEEQRAEVR--------LKHIGFVFQSFQL- 108
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAELARHRaylsqqqsPPFAMPVFQYLALh 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 109 LPHLTALENV-MLPLRLQEKFKyaeaeqkaLNLLkrvgLERQAQQtpkvLSGGEQQRVAIARALIR-------EPKIIFA 180
Cdd:COG4138 94 QPAGASSEAVeQLLAQLAEALG--------LEDK----LSRPLTQ----LSGGEWQRVRLAAVLLQvwptinpEGQLLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491113568 181 DEPTGNLDGETATEIEQLLFELnRELGTTLVLVTHDPKLAAQ-CQRHYALIDGQLVEQ 237
Cdd:COG4138 158 DEPMNSLDVAQQAALDRLLREL-CQQGITVVMSSHDLNHTLRhADRVWLLKQGKLVAS 214
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
15-217 |
3.67e-13 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 66.11 E-value: 3.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 15 IISAQNLTQKIQLAQKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILAtlDQASSGklVVCGESIaeLNEEQRAEV 94
Cdd:cd03232 3 VLTWKNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLA--GRKTAG--VITGEIL--INGRPLDKN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 95 RLKHIGFVFQSFQLLPHLTALENVMLPLRLQEkfkyaeaeqkalnllkrvglerqaqqtpkvLSGGEQQRVAIARALIRE 174
Cdd:cd03232 77 FQRSTGYVEQQDVHSPNLTVREALRFSALLRG------------------------------LSVEQRKRLTIGVELAAK 126
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 491113568 175 PKIIFADEPTGNLDGETATEIEQLLFELNRElGTTLVLVTHDP 217
Cdd:cd03232 127 PSILFLDEPTSGLDSQAAYNIVRFLKKLADS-GQAILCTIHQP 168
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
34-226 |
8.17e-13 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 67.35 E-value: 8.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 34 IFENLNFDIQEGEQVAITGRSGSGKSTLLGILaTLD--QASSGKLVV------CGESIAELNeeqraevrlKHIGFVFQS 105
Cdd:PRK10938 275 ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI-TGDhpQGYSNDLTLfgrrrgSGETIWDIK---------KHIGYVSSS 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 106 FqllpHL-----TALENVML-------------PLRLQekfkyaeaeQKALNLLKRVGLERQAQQTP-KVLSGGEQQRVA 166
Cdd:PRK10938 345 L----HLdyrvsTSVRNVILsgffdsigiyqavSDRQQ---------KLAQQWLDILGIDKRTADAPfHSLSWGQQRLAL 411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 167 IARALIREPKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDPKLAAQCQRH 226
Cdd:PRK10938 412 IVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDAPACITH 471
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
34-237 |
8.52e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 67.44 E-value: 8.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 34 IFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEqraeVRLKHIGFVFQSFQLLPHlT 113
Cdd:PRK10790 356 VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHS----VLRQGVAMVQQDPVVLAD-T 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 114 ALENVMLPLRLQEKFKYAEAEQKALNLLKRV---GLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGE 190
Cdd:PRK10790 431 FLANVTLGRDISEEQVWQALETVQLAELARSlpdGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSG 510
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491113568 191 TATEIEQLLFELNRElgTTLVLVTHDPKLAAQCQRHYALIDGQLVEQ 237
Cdd:PRK10790 511 TEQAIQQALAAVREH--TTLVVIAHRLSTIVEADTILVLHRGQAVEQ 555
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
15-216 |
1.00e-12 |
|
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: 67.27 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 15 IISAQNLTQKiqLAQKQLtiFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVcGESIaelneeqraev 94
Cdd:TIGR03719 322 VIEAENLTKA--FGDKLL--IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV----------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 95 rlkHIGFVFQSFQLL-PHLTALENVMLPLRLQEKFKYaeaEQKALNLLKRVGLERQAQQTP-KVLSGGEQQRVAIARALI 172
Cdd:TIGR03719 386 ---KLAYVDQSRDALdPNKTVWEEISGGLDIIKLGKR---EIPSRAYVGRFNFKGSDQQKKvGQLSGGERNRVHLAKTLK 459
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491113568 173 REPKIIFADEPTGNLDGETATEIEQLLFELNrelGTTLVlVTHD 216
Cdd:TIGR03719 460 SGGNVLLLDEPTNDLDVETLRALEEALLNFA---GCAVV-ISHD 499
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
32-215 |
1.83e-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: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 32 LTIFENLNFDIQEGEQVAITGRSGSGKSTLLgiLATLD--QASSGKLVVCGESIAELNEEQRAEVRLKHIGFVFQSFQLL 109
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLL--LAILGemQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 110 pHLTALENVML--PLRLQEKFKYAEA--EQKALNLLKrVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTG 185
Cdd:cd03290 92 -NATVEENITFgsPFNKQRYKAVTDAcsLQPDIDLLP-FGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
170 180 190
....*....|....*....|....*....|.
gi 491113568 186 NLDGETATEIEQL-LFELNRELGTTLVLVTH 215
Cdd:cd03290 170 ALDIHLSDHLMQEgILKFLQDDKRTLVLVTH 200
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
33-216 |
2.40e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 64.90 E-value: 2.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 33 TIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIaelneeqRAEVRLKHIGFVFQSFQL---L 109
Cdd:PRK15056 21 TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT-------RQALQKNLVAYVPQSEEVdwsF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 110 PHLtaLENVMLPLRLQE----KFKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTG 185
Cdd:PRK15056 94 PVL--VEDVVMMGRYGHmgwlRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFT 171
|
170 180 190
....*....|....*....|....*....|.
gi 491113568 186 NLDGETATEIEQLLFELnRELGTTLVLVTHD 216
Cdd:PRK15056 172 GVDVKTEARIISLLREL-RDEGKTMLVSTHN 201
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
34-196 |
2.50e-12 |
|
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: 66.12 E-value: 2.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 34 IFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAElneeqraevrlkhIGFVFQSFQL--LPH 111
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAK-------------IGLHDLRFKItiIPQ 1367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 112 LTALENVMLPLRLQEKFKYAEAE-QKALNL--LKRV------GLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADE 182
Cdd:TIGR00957 1368 DPVLFSGSLRMNLDPFSQYSDEEvWWALELahLKTFvsalpdKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDE 1447
|
170
....*....|....
gi 491113568 183 PTGNLDGETATEIE 196
Cdd:TIGR00957 1448 ATAAVDLETDNLIQ 1461
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
26-216 |
3.59e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 65.36 E-value: 3.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 26 QLAQKQLTifENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKlVVCGE--SIAELnEEQRAEvrlkhigfvf 103
Cdd:PRK11147 328 QIDGKQLV--KDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGR-IHCGTklEVAYF-DQHRAE---------- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 104 qsfqLLPHLTALENVmlplrlqekfkyAEAEQKAL-NLLKRVGL---------ERQAQQTPKVLSGGEQQRVAIARALIR 173
Cdd:PRK11147 394 ----LDPEKTVMDNL------------AEGKQEVMvNGRPRHVLgylqdflfhPKRAMTPVKALSGGERNRLLLARLFLK 457
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 491113568 174 EPKIIFADEPTGNLDGETAteieQLLFELNRELGTTLVLVTHD 216
Cdd:PRK11147 458 PSNLLILDEPTNDLDVETL----ELLEELLDSYQGTVLLVSHD 496
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
35-199 |
4.25e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.07 E-value: 4.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 35 FENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQRAEVRLKHIGFVFQSFQLlpHLTA 114
Cdd:PRK15439 279 FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVYLPEDRQSSGL--YLDA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 115 --------LENVMLPLRLQEKFKYAEAEQ--KALNllkrVGLErQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPT 184
Cdd:PRK15439 357 plawnvcaLTHNRRGFWIKPARENAVLERyrRALN----IKFN-HAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPT 431
|
170
....*....|....*
gi 491113568 185 GNLDGETATEIEQLL 199
Cdd:PRK15439 432 RGVDVSARNDIYQLI 446
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
41-216 |
4.73e-12 |
|
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: 65.19 E-value: 4.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 41 DIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVcGESIA----ELNEEQRAEVRlkhigfvfqsfqllphlTALE 116
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDE-DLKISykpqYISPDYDGTVE-----------------EFLR 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 117 NVmLPLRLQEKFKYAEaeqkalnLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETATEIE 196
Cdd:COG1245 424 SA-NTDDFGSSYYKTE-------IIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVA 495
|
170 180
....*....|....*....|
gi 491113568 197 QLLFELNRELGTTLVLVTHD 216
Cdd:COG1245 496 KAIRRFAENRGKTAMVVDHD 515
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-240 |
6.02e-12 |
|
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: 65.32 E-value: 6.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 19 QNLTQKIQLAQKqlTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLdQASSGKLVVCGESIAELNEEQRAevrlkh 98
Cdd:TIGR01271 1221 QGLTAKYTEAGR--AVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVSWNSVTLQTWR------ 1291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 99 igfvfQSFQLLPHLTALENVMLPLRLQEKFKYaeAEQKALNLLKRVGLERQAQQTPK-----------VLSGGEQQRVAI 167
Cdd:TIGR01271 1292 -----KAFGVIPQKVFIFSGTFRKNLDPYEQW--SDEEIWKVAEEVGLKSVIEQFPDkldfvlvdggyVLSNGHKQLMCL 1364
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491113568 168 ARALIREPKIIFADEPTGNLDGETATEIEQLLFELNRElgTTLVLVTHDPKLAAQCQRhYALIDGQLVEQFAA 240
Cdd:TIGR01271 1365 ARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSN--CTVILSEHRVEALLECQQ-FLVIEGSSVKQYDS 1434
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
38-216 |
1.97e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 61.87 E-value: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 38 LNFDIQEGEQVAITGRSGSGKSTLLGILATLdQASSGKLVVCGESIAELNEEQRAEVRlkhiGF------------VFQS 105
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELARHR----AYlsqqqtppfampVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 106 FQLlpHLTALENVmlplrlqekfkyaEAEQKALNLL-KRVG----LERQAQQtpkvLSGGEQQRVAIARALIR------- 173
Cdd:PRK03695 90 LTL--HQPDKTRT-------------EAVASALNEVaEALGlddkLGRSVNQ----LSGGEWQRVRLAAVVLQvwpdinp 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 491113568 174 EPKIIFADEPTGNLDGETATEIEQLLFELNReLGTTLVLVTHD 216
Cdd:PRK03695 151 AGQLLLLDEPMNSLDVAQQAALDRLLSELCQ-QGIAVVMSSHD 192
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
15-227 |
2.45e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 62.99 E-value: 2.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 15 IISAQNLTqkIQLAQKQLtiFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVV-CGESIAELNEEQrae 93
Cdd:PRK15064 1 MLSTANIT--MQFGAKPL--FENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLdPNERLGKLRQDQ--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 94 vrlkhigFVFQSFQLLP-----HlTALENVM--------LP-------LRLQE-KFKYAE-----AEQKALNLLKRVGL- 146
Cdd:PRK15064 74 -------FAFEEFTVLDtvimgH-TELWEVKqerdriyaLPemseedgMKVADlEVKFAEmdgytAEARAGELLLGVGIp 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 147 ERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETATEIEQLLFELNrelgTTLVLVTHDpklaaqcqRH 226
Cdd:PRK15064 146 EEQHYGLMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERN----STMIIISHD--------RH 213
|
.
gi 491113568 227 Y 227
Cdd:PRK15064 214 F 214
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
34-236 |
2.48e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.46 E-value: 2.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 34 IFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAE--LNEEQRAevrlkhIGFVFQSFQLLPH 111
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfgLTDLRRV------LSIIPQSPVLFSG 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 112 LTALEnvMLPLRLQEKFKYAEAEQKA--LNLLKR--VGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNL 187
Cdd:PLN03232 1325 TVRFN--IDPFSEHNDADLWEALERAhiKDVIDRnpFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASV 1402
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491113568 188 DGETATEIEQLLFELNRElgTTLVLVTHDPKLAAQCQRHYALIDGQLVE 236
Cdd:PLN03232 1403 DVRTDSLIQRTIREEFKS--CTMLVIAHRLNTIIDCDKILVLSSGQVLE 1449
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
33-219 |
2.64e-11 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 62.96 E-value: 2.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 33 TIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVvcgesiaelneeQRAEVRLKhigfVFQSFqllpHL 112
Cdd:PLN03073 523 LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF------------RSAKVRMA----VFSQH----HV 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 113 TALENVMLPLRLQEKFKYAEAEQKALNLLKRVGLERQ-AQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGET 191
Cdd:PLN03073 583 DGLDLSSNPLLYMMRCFPGVPEQKLRAHLGSFGVTGNlALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDA 662
|
170 180 190
....*....|....*....|....*....|
gi 491113568 192 ATEIEQ--LLFElnrelGTTLvLVTHDPKL 219
Cdd:PLN03073 663 VEALIQglVLFQ-----GGVL-MVSHDEHL 686
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
15-217 |
4.32e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 62.43 E-value: 4.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 15 IISAQNLTQKIQLAQKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILAtldQASSGKLVVCGESIaeLNEEQRAEV 94
Cdd:TIGR00956 759 IFHWRNLTYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLA---ERVTTGVITGGDRL--VNGRPLDSS 833
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 95 RLKHIGFVFQSFQLLPHLTALENVMLPLRLQ--------EKFKYAEAeqkalnLLKRVGLERQAQQTPKVLSGG---EQ- 162
Cdd:TIGR00956 834 FQRSIGYVQQQDLHLPTSTVRESLRFSAYLRqpksvsksEKMEYVEE------VIKLLEMESYADAVVGVPGEGlnvEQr 907
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491113568 163 QRVAIARALIREPK-IIFADEPTGNLDGETATEIEQLLfelnREL---GTTLVLVTHDP 217
Cdd:TIGR00956 908 KRLTIGVELVAKPKlLLFLDEPTSGLDSQTAWSICKLM----RKLadhGQAILCTIHQP 962
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
29-215 |
6.09e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 61.97 E-value: 6.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 29 QKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCgesiaelNEEQRAEVRLK----HIGFVFQ 104
Cdd:PTZ00265 395 RKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN-------DSHNLKDINLKwwrsKIGVVSQ 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 105 ---------------SFQLLPHLTALE----------------------------NVMLP-------LRLQEKFKYAEaE 134
Cdd:PTZ00265 468 dpllfsnsiknnikySLYSLKDLEALSnyynedgndsqenknkrnscrakcagdlNDMSNttdsnelIEMRKNYQTIK-D 546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 135 QKALNLLKRVGLERQAQQTP-----------KVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETATEIEQLLFELN 203
Cdd:PTZ00265 547 SEVVDVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLK 626
|
250
....*....|..
gi 491113568 204 RELGTTLVLVTH 215
Cdd:PTZ00265 627 GNENRITIIIAH 638
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
13-232 |
7.24e-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: 61.95 E-value: 7.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 13 QTIISAQNLTQKIQLaqKQLT---------IFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESI 83
Cdd:TIGR01257 1926 QRIISGGNKTDILRL--NELTkvysgtsspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI 2003
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 84 aelneeqraevrLKHIGFVFQSFQLLPHLTALENVMLP---LRLQEKFKYAEAEQ--KALNL-LKRVGLERQAQQTPKVL 157
Cdd:TIGR01257 2004 ------------LTNISDVHQNMGYCPQFDAIDDLLTGrehLYLYARLRGVPAEEieKVANWsIQSLGLSLYADRLAGTY 2071
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491113568 158 SGGEQQRVAIARALIREPKIIFADEPTGNLDGETATEIEQLLFELNRElGTTLVLVTHD-PKLAAQCQRHYALIDG 232
Cdd:TIGR01257 2072 SGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSmEECEALCTRLAIMVKG 2146
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
28-236 |
7.66e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 61.89 E-value: 7.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 28 AQKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLL-GILATLDQASsGKLVVCGeSIAELneEQRAEVRlkhigfvfqsf 106
Cdd:TIGR00957 647 ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLsALLAEMDKVE-GHVHMKG-SVAYV--PQQAWIQ----------- 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 107 qllpHLTALENVMLPLRLQEKfkYAEAEQKALNLLKRVGLERQAQQTP-----KVLSGGEQQRVAIARALIREPKIIFAD 181
Cdd:TIGR00957 712 ----NDSLRENILFGKALNEK--YYQQVLEACALLPDLEILPSGDRTEigekgVNLSGGQKQRVSLARAVYSNADIYLFD 785
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491113568 182 EPTGNLDGETATEI-EQLLFELNRELGTTLVLVTHDPKLAAQCQRHYALIDGQLVE 236
Cdd:TIGR00957 786 DPLSAVDAHVGKHIfEHVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISE 841
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
34-195 |
2.77e-10 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 59.10 E-value: 2.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 34 IFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGEsiaelneeqraevrlkhIGFVFQSFQLLPHlT 113
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-----------------ISFSSQFSWIMPG-T 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 114 ALENVMLPLRLQEkFKYaeaeqkaLNLLKRVGLERQAQQTPK-----------VLSGGEQQRVAIARALIREPKIIFADE 182
Cdd:cd03291 114 IKENIIFGVSYDE-YRY-------KSVVKACQLEEDITKFPEkdntvlgeggiTLSGGQRARISLARAVYKDADLYLLDS 185
|
170
....*....|...
gi 491113568 183 PTGNLDGETATEI 195
Cdd:cd03291 186 PFGYLDVFTEKEI 198
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
34-237 |
3.21e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 58.87 E-value: 3.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 34 IFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESiaeLNEEQRAEVRLKH-IGFVFQSFQLLPHL 112
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKP---LDYSKRGLLALRQqVATVFQDPEQQIFY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 113 TALE-NVMLPLRlqeKFKYAEAE--QKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDG 189
Cdd:PRK13638 93 TDIDsDIAFSLR---NLGVPEAEitRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491113568 190 ETATEIEQLLFELNRElGTTLVLVTHDPKLAAQCQRH-YALIDGQLVEQ 237
Cdd:PRK13638 170 AGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAvYVLRQGQILTH 217
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
38-236 |
3.26e-10 |
|
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: 59.81 E-value: 3.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 38 LNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIaelNEEQRAEVRlKHIGFVFQSFQLLPHLTALEN 117
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV---TADNREAYR-QLFSAVFSDFHLFDRLLGLDG 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 118 VMLPLRLQEkfkyaeaeqkalnLLKRVGLERqaqqtpKV-----------LSGGEQQRVAIARALIRE-PKIIFaDE--- 182
Cdd:COG4615 427 EADPARARE-------------LLERLELDH------KVsvedgrfsttdLSQGQRKRLALLVALLEDrPILVF-DEwaa 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491113568 183 ---PtgnldgeTATEI--EQLLFELnRELGTTLVLVTHDPKLAAQCQRHYALIDGQLVE 236
Cdd:COG4615 487 dqdP-------EFRRVfyTELLPEL-KARGKTVIAISHDDRYFDLADRVLKMDYGKLVE 537
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
33-216 |
3.83e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 59.52 E-value: 3.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 33 TIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKlVVCGESIAelneeqraevrlkhIGFVFQSfqllpHL 112
Cdd:PRK15064 333 PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGT-VKWSENAN--------------IGYYAQD-----HA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 113 TALENVMLPLRLQEKFKYAEAEQKALnllkRVGLER------QAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGN 186
Cdd:PRK15064 393 YDFENDLTLFDWMSQWRQEGDDEQAV----RGTLGRllfsqdDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNH 468
|
170 180 190
....*....|....*....|....*....|
gi 491113568 187 LDGETateIEQLLFELNRELGtTLVLVTHD 216
Cdd:PRK15064 469 MDMES---IESLNMALEKYEG-TLIFVSHD 494
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
29-231 |
3.96e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 59.74 E-value: 3.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 29 QKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILA-TLDQ---ASSGKLVVCGESIAELNEEQRAEVrlkhiGFVFQ 104
Cdd:TIGR00956 71 TKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsNTDGfhiGVEGVITYDGITPEEIKKHYRGDV-----VYNAE 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 105 SFQLLPHLTALENVMLPLRLQ---------EKFKYAEAEQKALnlLKRVGLeRQAQQTpKV-------LSGGEQQRVAIA 168
Cdd:TIGR00956 146 TDVHFPHLTVGETLDFAARCKtpqnrpdgvSREEYAKHIADVY--MATYGL-SHTRNT-KVgndfvrgVSGGERKRVSIA 221
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491113568 169 RALIREPKIIFADEPTGNLDGETATEIEQLLFELNRELGTTlVLVThdpklAAQC-QRHYALID 231
Cdd:TIGR00956 222 EASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTT-PLVA-----IYQCsQDAYELFD 279
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
34-195 |
4.67e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 59.54 E-value: 4.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 34 IFENLNFDIQEGEQVAITGRSGSGKSTLLGILatldqassgklvvcgesiaeLNEEQRAEVRLKH---IGFVFQSFQLLP 110
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMI--------------------MGELEPSEGKIKHsgrISFSPQTSWIMP 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 111 HlTALENVMLPLRLQEkFKYAEAeQKALNLLKRVGLERQAQQTPK-----VLSGGEQQRVAIARALIREPKIIFADEPTG 185
Cdd:TIGR01271 501 G-TIKDNIIFGLSYDE-YRYTSV-IKACQLEEDIALFPEKDKTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFT 577
|
170
....*....|
gi 491113568 186 NLDGETATEI 195
Cdd:TIGR01271 578 HLDVVTEKEI 587
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
36-241 |
5.88e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.86 E-value: 5.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 36 ENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEEQR--------AEVRlKHIGFVF-QSF 106
Cdd:PRK10762 269 NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGlangivyiSEDR-KRDGLVLgMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 107 QLLPHLTALE---NVMLPLRLQEKFKYAEAEQKALNLlKRVGLErqaqQTPKVLSGGEQQRVAIARALIREPKIIFADEP 183
Cdd:PRK10762 348 KENMSLTALRyfsRAGGSLKHADEQQAVSDFIRLFNI-KTPSME----QAIGLLSGGNQQKVAIARGLMTRPKVLILDEP 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491113568 184 TGNLDGETATEIEQLLFELNRElGTTLVLVTHD-PKLAAQCQRHYALIDGQLVEQFAAK 241
Cdd:PRK10762 423 TRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEmPEVLGMSDRILVMHEGRISGEFTRE 480
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
43-216 |
6.07e-10 |
|
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: 59.03 E-value: 6.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 43 QEGEQVAITGRSGSGKSTLLGILAtldqassgklvvcGESIAELNEEQRA----EVrLKHigfvFQSFQLLPHLTALEN- 117
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILS-------------GELKPNLGDYDEEpswdEV-LKR----FRGTELQDYFKKLANg 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 118 ----------V-MLPLRLQ----EKFKYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADE 182
Cdd:COG1245 159 eikvahkpqyVdLIPKVFKgtvrELLEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190
....*....|....*....|....*....|....
gi 491113568 183 PTGNLDGETATEIEQLLFELNRElGTTLVLVTHD 216
Cdd:COG1245 239 PSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHD 271
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
29-215 |
6.73e-10 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 58.57 E-value: 6.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 29 QKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELN-EEQRAevRLKHIG---FVFQ 104
Cdd:PRK10789 325 QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQlDSWRS--RLAVVSqtpFLFS 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 105 SfqllphlTALENVML------PLRLQEKFKYAEAEQKALNLLKrvGLERQAQQTPKVLSGGEQQRVAIARALIREPKII 178
Cdd:PRK10789 403 D-------TVANNIALgrpdatQQEIEHVARLASVHDDILRLPQ--GYDTEVGERGVMLSGGQKQRISIARALLLNAEIL 473
|
170 180 190
....*....|....*....|....*....|....*..
gi 491113568 179 FADEPTGNLDGETATEIEQLLFELNRelGTTLVLVTH 215
Cdd:PRK10789 474 ILDDALSAVDGRTEHQILHNLRQWGE--GRTVIISAH 508
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
43-216 |
7.06e-10 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 57.76 E-value: 7.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 43 QEGEQVAITGRSGSGKSTLLGILAtldqassGKLVvcgESIAELNEEQRAEVRLKHigfvFQSFQLLPHLTALENVmlPL 122
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILA-------GKLK---PNLGKFDDPPDWDEILDE----FRGSELQNYFTKLLEG--DV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 123 RLQEKFKY-----AEAEQKALNLLKRVG-----------------LERQAQQtpkvLSGGEQQRVAIARALIREPKIIFA 180
Cdd:cd03236 88 KVIVKPQYvdlipKAVKGKVGELLKKKDergkldelvdqlelrhvLDRNIDQ----LSGGELQRVAIAAALARDADFYFF 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 491113568 181 DEPTGNLDGETATEIEQLLFELNRELGTTLVlVTHD 216
Cdd:cd03236 164 DEPSSYLDIKQRLNAARLIRELAEDDNYVLV-VEHD 198
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
6-243 |
7.46e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.59 E-value: 7.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 6 KESNIMPQTIISAQNLTqkiqlAQKQLTIfENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESI-- 83
Cdd:PRK10982 241 DKENKPGEVILEVRNLT-----SLRQPSI-RDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKInn 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 84 -----------AELNEEQRAEVRLKHIGFVFQSFqllphLTALENVMLPLRLQEKFKYAEAEQKALNLLKrvgLERQAQQ 152
Cdd:PRK10982 315 hnaneainhgfALVTEERRSTGIYAYLDIGFNSL-----ISNIRNYKNKVGLLDNSRMKSDTQWVIDSMR---VKTPGHR 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 153 TP-KVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHDPKLAAQCQRHYALID 231
Cdd:PRK10982 387 TQiGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSN 466
|
250
....*....|..
gi 491113568 232 GQLVEQFAAKPT 243
Cdd:PRK10982 467 GLVAGIVDTKTT 478
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
42-216 |
9.14e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 58.28 E-value: 9.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 42 IQEGEQVAITGRSGSGKSTLLGILAtldqassgklvvcGESIAELNEEQRA----EVrLKHigfvFQSFQLLPHLTALEN 117
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILS-------------GELIPNLGDYEEEpswdEV-LKR----FRGTELQNYFKKLYN 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 118 VmlPLRLQEKFKYAEAEQKALN-----LLKRV-------------GLERQAQQTPKVLSGGEQQRVAIARALIREPKIIF 179
Cdd:PRK13409 158 G--EIKVVHKPQYVDLIPKVFKgkvreLLKKVdergkldevverlGLENILDRDISELSGGELQRVAIAAALLRDADFYF 235
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 491113568 180 ADEPTGNLDgetateIEQLL--FELNREL--GTTLVLVTHD 216
Cdd:PRK13409 236 FDEPTSYLD------IRQRLnvARLIRELaeGKYVLVVEHD 270
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
35-216 |
1.08e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.21 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 35 FENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVcGESIaelneeqraevrlkHIGFVFQSFQLL-PHLT 113
Cdd:PRK11819 340 IDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV--------------KLAYVDQSRDALdPNKT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 114 ALENV-----MLPLRLQE--------KFKYAEAEQKalnllKRVGlerqaqqtpkVLSGGEQQRVAIARALIREPKIIFA 180
Cdd:PRK11819 405 VWEEIsggldIIKVGNREipsrayvgRFNFKGGDQQ-----KKVG----------VLSGGERNRLHLAKTLKQGGNVLLL 469
|
170 180 190
....*....|....*....|....*....|....*.
gi 491113568 181 DEPTGNLDGETATEIEQLLFELNrelGTTLVlVTHD 216
Cdd:PRK11819 470 DEPTNDLDVETLRALEEALLEFP---GCAVV-ISHD 501
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
33-234 |
1.13e-09 |
|
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: 57.17 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 33 TIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLdQASSGKLVVCGES--IAELNEEQRAEVRLKHIGFVFQSfqllp 110
Cdd:cd03289 18 AVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGVSwnSVPLQKWRKAFGVIPQKVFIFSG----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 111 hltalenvmlPLRLQEKFKYAEAEQKALNLLKRVGLERQAQQTPK-----------VLSGGEQQRVAIARALIREPKIIF 179
Cdd:cd03289 92 ----------TFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGqldfvlvdggcVLSHGHKQLMCLARSVLSKAKILL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491113568 180 ADEPTGNLDGETATEIEQLLFELNRelGTTLVLVTHDPKLAAQCQRHYALIDGQL 234
Cdd:cd03289 162 LDEPSAHLDPITYQVIRKTLKQAFA--DCTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
41-216 |
3.58e-09 |
|
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: 55.49 E-value: 3.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 41 DIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIA----ELNEEQRAEVRlkhigfvfqsfQLLPHLTale 116
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpqYIKADYEGTVR-----------DLLSSIT--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 117 nvmlplrlqeKFKYAEAEQKAlNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETATEIE 196
Cdd:cd03237 87 ----------KDFYTHPYFKT-EIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMAS 155
|
170 180
....*....|....*....|..
gi 491113568 197 QLL--FELNRElgTTLVLVTHD 216
Cdd:cd03237 156 KVIrrFAENNE--KTAFVVEHD 175
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
37-223 |
3.79e-09 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 55.70 E-value: 3.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 37 NLNFDIQEGEQVAITGRSGSGKSTLLG--ILATLDQASSGKLVVCGEsiaelneeQRAEVRLKHIGFVFQSFQLLPHLTA 114
Cdd:cd03271 13 NIDVDIPLGVLTCVTGVSGSGKSSLINdtLYPALARRLHLKKEQPGN--------HDRIEGLEHIDKVIVIDQSPIGRTP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 115 LEN------VMLPLR----------------LQEKFK-----------YAEAEQ---------KALNLLKRVGLE--RQA 150
Cdd:cd03271 85 RSNpatytgVFDEIRelfcevckgkrynretLEVRYKgksiadvldmtVEEALEffenipkiaRKLQTLCDVGLGyiKLG 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491113568 151 QQTPkVLSGGEQQRVAIARALIRE---PKIIFADEPTGNLDGEtatEIEQLLFELNR--ELGTTLVLVTHDPKLAAQC 223
Cdd:cd03271 165 QPAT-TLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFH---DVKKLLEVLQRlvDKGNTVVVIEHNLDVIKCA 238
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
42-190 |
4.56e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.36 E-value: 4.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 42 IQEGEQVAITGRSGSGKSTLLGILATLDQASSGKlVVCGESIA----ELNEEQRAEVRlkhigfvfqsfQLLPHLTAlen 117
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGE-VDPELKISykpqYIKPDYDGTVE-----------DLLRSITD--- 426
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491113568 118 vmlplRLQEKFKYAEaeqkalnLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGE 190
Cdd:PRK13409 427 -----DLGSSYYKSE-------IIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE 487
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
49-219 |
6.81e-09 |
|
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: 54.15 E-value: 6.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 49 AITGRSGSGKSTLL-GILATL--DQASSGKLVVCGESIAELNEEqRAEVRLKhigfvfqsfqllphltalenvmlpLRLQ 125
Cdd:cd03240 26 LIVGQNGAGKTTIIeALKYALtgELPPNSKGGAHDPKLIREGEV-RAQVKLA------------------------FENA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 126 EKFKYaEAEQKaLNLLKRVGLERQAQ------QTPKVLSGGEQQ------RVAIARALIREPKIIFADEPTGNLDGETAT 193
Cdd:cd03240 81 NGKKY-TITRS-LAILENVIFCHQGEsnwpllDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIE 158
|
170 180
....*....|....*....|....*..
gi 491113568 194 E-IEQLLFELNRELGTTLVLVTHDPKL 219
Cdd:cd03240 159 EsLAEIIEERKSQKNFQLIVITHDEEL 185
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
29-215 |
9.20e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 53.80 E-value: 9.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 29 QKQLtIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIaelnEEQRAEVRlKHIGFVFQSFQL 108
Cdd:PRK13540 12 HDQP-LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCTYQ-KQLCFVGHRSGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 109 LPHLTALENVMLPLRlqekfkYAEAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLD 188
Cdd:PRK13540 86 NPYLTLRENCLYDIH------FSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
170 180
....*....|....*....|....*..
gi 491113568 189 gETATEIEQLLFELNRELGTTLVLVTH 215
Cdd:PRK13540 160 -ELSLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
37-237 |
1.34e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 55.13 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 37 NLNFDIQEGEQVAITGRSGSGKSTLL-GILATLDQASSGKLVVCGeSIAELNEeqraevrlkhIGFVFQSfqllphlTAL 115
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLIsAMLGELPPRSDASVVIRG-TVAYVPQ----------VSWIFNA-------TVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 116 ENVMLPLRLQ----EKFKYAEAEQKALNLL-----KRVGlERQAQqtpkvLSGGEQQRVAIARALIREPKIIFADEPTGN 186
Cdd:PLN03130 697 DNILFGSPFDperyERAIDVTALQHDLDLLpggdlTEIG-ERGVN-----ISGGQKQRVSMARAVYSNSDVYIFDDPLSA 770
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491113568 187 LDGETATEIeqllFE--LNREL-GTTLVLVTHDPKLAAQCQRHYALIDGQLVEQ 237
Cdd:PLN03130 771 LDAHVGRQV----FDkcIKDELrGKTRVLVTNQLHFLSQVDRIILVHEGMIKEE 820
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
36-184 |
2.14e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 54.36 E-value: 2.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 36 ENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAelNEEQRAEVrLKHIGFVFQSF--QLLPHLT 113
Cdd:NF033858 18 DDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA--DARHRRAV-CPRIAYMPQGLgkNLYPTLS 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491113568 114 ALENVMLPLRL--QEKfkyAEAEQKALNLLKRVGL----ERQAQQtpkvLSGGEQQRVAIARALIREPKIIFADEPT 184
Cdd:NF033858 95 VFENLDFFGRLfgQDA---AERRRRIDELLRATGLapfaDRPAGK----LSGGMKQKLGLCCALIHDPDLLILDEPT 164
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
12-237 |
2.14e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.60 E-value: 2.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 12 PQTIISAQNLTQKIQLAQKQLTifeNLNFDIQEGEQVAITGRSGSGKSTLL-GILATLDQASSGKLVVCGeSIAELNEeq 90
Cdd:PLN03232 613 PAISIKNGYFSWDSKTSKPTLS---DINLEIPVGSLVAIVGGTGEGKTSLIsAMLGELSHAETSSVVIRG-SVAYVPQ-- 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 91 raevrlkhIGFVFQSfqllphlTALENVMLPLRLqEKFKY-----AEAEQKALNLLKRVGLERQAQQTPKVlSGGEQQRV 165
Cdd:PLN03232 687 --------VSWIFNA-------TVRENILFGSDF-ESERYwraidVTALQHDLDLLPGRDLTEIGERGVNI-SGGQKQRV 749
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491113568 166 AIARALIREPKIIFADEPTGNLDGETATEIeqllFE--LNREL-GTTLVLVTHDPKLAAQCQRHYALIDGQLVEQ 237
Cdd:PLN03232 750 SMARAVYSNSDIYIFDDPLSALDAHVAHQV----FDscMKDELkGKTRVLVTNQLHFLPLMDRIILVSEGMIKEE 820
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
36-214 |
2.15e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 54.06 E-value: 2.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 36 ENLNFDIQEGEQVAITGRSGSGKSTLL-GILATLDQASSGKLVVCGESIAELNEEQRAEVRLKHIGFVFQSFQLLPHLTA 114
Cdd:TIGR02633 277 DDVSFSLRRGEILGVAGLVGAGRTELVqALFGAYPGKFEGNVFINGKPVDIRNPAQAIRAGIAMVPEDRKRHGIVPILGV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 115 LENVMLPLRLQEKFKY---AEAEQKALNL-LKRVGLERQAQQTP-KVLSGGEQQRVAIARALIREPKIIFADEPTGNLDG 189
Cdd:TIGR02633 357 GKNITLSVLKSFCFKMridAAAELQIIGSaIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDV 436
|
170 180
....*....|....*....|....*
gi 491113568 190 ETATEIEQLLFELNRElGTTLVLVT 214
Cdd:TIGR02633 437 GAKYEIYKLINQLAQE-GVAIIVVS 460
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
37-219 |
2.15e-08 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 52.33 E-value: 2.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 37 NLNFDIQEGEQVAITGRSGSGKSTLLgilatldqassgklvvcgesiaelNEEQRAEVRLKHIGFvfqsfqlLPHLTALE 116
Cdd:cd03238 13 NLDVSIPLNVLVVVTGVSGSGKSTLV------------------------NEGLYASGKARLISF-------LPKFSRNK 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 117 NVMLplrlqekfkyaeaeqKALNLLKRVGLE----RQAQQTpkvLSGGEQQRVAIARALIREPK--IIFADEPTGNLDGE 190
Cdd:cd03238 62 LIFI---------------DQLQFLIDVGLGyltlGQKLST---LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQ 123
|
170 180 190
....*....|....*....|....*....|.
gi 491113568 191 TateIEQLLFELNR--ELGTTLVLVTHDPKL 219
Cdd:cd03238 124 D---INQLLEVIKGliDLGNTVILIEHNLDV 151
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
26-227 |
2.20e-08 |
|
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to 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 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: 213208 [Multi-domain] Cd Length: 276 Bit Score: 53.36 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 26 QLAQKQLTIFENLNFDIQEGEQVaITGRSGSGKSTLL-GILATLDQASSGKLVVCGESIA------ELNEEQRAEVRLKH 98
Cdd:cd03241 3 ELSIKNFALIEELELDFEEGLTV-LTGETGAGKSILLdALSLLLGGRASADLIRSGAEKAvvegvfDISDEEEAKALLLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 99 IGFVFQSFQLLPHLTA--------LENVMLPLRLQEKF------KYAEAEQkaLNLLKRV--------GLER-------- 148
Cdd:cd03241 82 LGIEDDDDLIIRREISrkgrsryfINGQSVTLKLLRELgsllvdIHGQHDH--QNLLNPErqldlldgGLDDveflfstn 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 149 --QAQQTP-KVLSGGEQQRVAIARALI-----REPKIIFaDEPTGNLDGETATEIEQLLFELNRelGTTLVLVTHDPKLA 220
Cdd:cd03241 160 pgEPLKPLaKIASGGELSRLMLALKAIlarkdAVPTLIF-DEIDTGISGEVAQAVGKKLKELSR--SHQVLCITHLPQVA 236
|
....*..
gi 491113568 221 AQCQRHY 227
Cdd:cd03241 237 AMADNHF 243
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
36-216 |
2.98e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 53.76 E-value: 2.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 36 ENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGE--SIAELNEEQRAEVRL-----KHIGFVfqsfql 108
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKpiDIRSPRDAIRAGIMLcpedrKAEGII------ 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 109 lPHLTALENVMLPLR---------LQEKFKYAEAEQ--KALNLLKRvglerQAQQTPKVLSGGEQQRVAIARALIREPKI 177
Cdd:PRK11288 344 -PVHSVADNINISARrhhlragclINNRWEAENADRfiRSLNIKTP-----SREQLIMNLSGGNQQKAILGRWLSEDMKV 417
|
170 180 190
....*....|....*....|....*....|....*....
gi 491113568 178 IFADEPTGNLDGETATEIEQLLFELnRELGTTLVLVTHD 216
Cdd:PRK11288 418 ILLDEPTRGIDVGAKHEIYNVIYEL-AAQGVAVLFVSSD 455
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
38-236 |
6.73e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.82 E-value: 6.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 38 LNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNeeqRAEVRlKHIGFVFQS---------FQL 108
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFG---LMDLR-KVLGIIPQApvlfsgtvrFNL 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 109 LP---HLTAlenvmlplRLQEKFKYAEAEqkalNLLKR--VGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEP 183
Cdd:PLN03130 1334 DPfneHNDA--------DLWESLERAHLK----DVIRRnsLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEA 1401
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491113568 184 TGNLDGETATEIEQLLFELNRelGTTLVLVTHDPKLAAQCQRHYALIDGQLVE 236
Cdd:PLN03130 1402 TAAVDVRTDALIQKTIREEFK--SCTMLIIAHRLNTIIDCDRILVLDAGRVVE 1452
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
132-231 |
8.34e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 52.04 E-value: 8.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 132 EAEQKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETATEIEQLLFELNRElGTTLV 211
Cdd:NF000106 120 DARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVL 198
|
90 100
....*....|....*....|
gi 491113568 212 LVTHDPKLAAQCQRHYALID 231
Cdd:NF000106 199 LTTQYMEEAEQLAHELTVID 218
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
26-242 |
1.13e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.47 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 26 QLAQKQLtiFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKlVVCGESIAELNEE---QRAEVRlKHIGFV 102
Cdd:PTZ00243 669 ELEPKVL--LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGR-VWAERSIAYVPQQawiMNATVR-GNILFF 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 103 FQsfqllphltalENvmlPLRLQEKFKYAEAEQKALNLlkRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADE 182
Cdd:PTZ00243 745 DE-----------ED---AARLADAVRVSQLEADLAQL--GGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDD 808
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491113568 183 PTGNLDGETATEIEQLLFeLNRELGTTLVLVTHDPKLAAQCQRHYALIDGQLV-----EQFAAKP 242
Cdd:PTZ00243 809 PLSALDAHVGERVVEECF-LGALAGKTRVLATHQVHVVPRADYVVALGDGRVEfsgssADFMRTS 872
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
25-216 |
4.29e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.17 E-value: 4.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 25 IQLAQKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGE-SIAELNEEQRAeVRLKHIGFVF 103
Cdd:PRK10636 7 LQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwQLAWVNQETPA-LPQPALEYVI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 104 -------QSFQLLPHLTALENVMLPLRLQEKFKYAEA---EQKALNLLKRVGL-ERQAQQTPKVLSGGEQQRVAIARALI 172
Cdd:PRK10636 86 dgdreyrQLEAQLHDANERNDGHAIATIHGKLDAIDAwtiRSRAASLLHGLGFsNEQLERPVSDFSGGWRMRLNLAQALI 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491113568 173 REPKIIFADEPTGNLDGETATEIEQLLfelnRELGTTLVLVTHD 216
Cdd:PRK10636 166 CRSDLLLLDEPTNHLDLDAVIWLEKWL----KSYQGTLILISHD 205
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
45-215 |
5.05e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.24 E-value: 5.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 45 GEQVAITGRSGSGKSTLLGILA--TLD------QASSGKLVVCGESIAELN-----EEQRAEVRLKHIGFVFQSFQL--- 108
Cdd:PLN03073 203 GRHYGLVGRNGTGKTTFLRYMAmhAIDgipkncQILHVEQEVVGDDTTALQcvlntDIERTQLLEEEAQLVAQQRELefe 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 109 -------LPHLTALENVMLPLRLQEKFKYAE------AEQKALNLLkrVGL----ERQAQQTpKVLSGGEQQRVAIARAL 171
Cdd:PLN03073 283 tetgkgkGANKDGVDKDAVSQRLEEIYKRLElidaytAEARAASIL--AGLsftpEMQVKAT-KTFSGGWRMRIALARAL 359
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491113568 172 IREPKIIFADEPTGNLDGETATEIEQLLFELNRelgtTLVLVTH 215
Cdd:PLN03073 360 FIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK----TFIVVSH 399
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
40-188 |
5.47e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.16 E-value: 5.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 40 FDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAE--LNEEQRaevrlkhigfvfqSFQLLPHLTALEN 117
Cdd:PTZ00243 1331 FRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAygLRELRR-------------QFSMIPQDPVLFD 1397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 118 VMLPLRLQEKFKYAEAE-QKALNLlkrVGL-ERQAQQT----PKVLSG------GEQQRVAIARALI-REPKIIFADEPT 184
Cdd:PTZ00243 1398 GTVRQNVDPFLEASSAEvWAALEL---VGLrERVASESegidSRVLEGgsnysvGQRQLMCMARALLkKGSGFILMDEAT 1474
|
....
gi 491113568 185 GNLD 188
Cdd:PTZ00243 1475 ANID 1478
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
23-188 |
5.63e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 49.02 E-value: 5.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 23 QKIQLAQKQLTIFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLD--QASSGKLVVCGESIAELNEEQRAEvrlKHIG 100
Cdd:PRK09580 5 KDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAG---EGIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 101 FVFQSFQLLPHL-------TALeNVMLPLRLQE---KFKYAEAEQKALNLLKRVG--LERQAQQTpkvLSGGEQQRVAIA 168
Cdd:PRK09580 82 MAFQYPVEIPGVsnqfflqTAL-NAVRSYRGQEpldRFDFQDLMEEKIALLKMPEdlLTRSVNVG---FSGGEKKRNDIL 157
|
170 180
....*....|....*....|
gi 491113568 169 RALIREPKIIFADEPTGNLD 188
Cdd:PRK09580 158 QMAVLEPELCILDESDSGLD 177
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
157-226 |
6.23e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.54 E-value: 6.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 157 LSGGEQQRVAIARALIREPKIIFADEPTGNLDGETATEIEQLLFELNR----------ELGTTL-----VLVTHDPKLAA 221
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQqgvaiivissELPEVLglsdrVLVMHEGKLKG 485
|
....*
gi 491113568 222 QCQRH 226
Cdd:PRK13549 486 DLINH 490
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
49-219 |
6.40e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 49.84 E-value: 6.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 49 AITGRSGSGKSTLLGILATldqASSGKLVVCGESIAELNEEQRAEVRLKhiGFVFQSFQLLPHLTALENVMLP--LRL-- 124
Cdd:PLN03140 910 ALMGVSGAGKTTLMDVLAG---RKTGGYIEGDIRISGFPKKQETFARIS--GYCEQNDIHSPQVTVRESLIYSafLRLpk 984
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 125 ----QEKFKYAE--AEQKALNLLKR--VGLerqaqqtPKV--LSGGEQQRVAIARALIREPKIIFADEPTGNLDGETATe 194
Cdd:PLN03140 985 evskEEKMMFVDevMELVELDNLKDaiVGL-------PGVtgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAA- 1056
|
170 180
....*....|....*....|....*
gi 491113568 195 IEQLLFELNRELGTTLVLVTHDPKL 219
Cdd:PLN03140 1057 IVMRTVRNTVDTGRTVVCTIHQPSI 1081
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
33-239 |
6.65e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.78 E-value: 6.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 33 TIFENLNFDIQEGEQVAITGRSGSGKSTLLGILAtldqassGKLvvcgesiaelnEEQRAEVRL-KHIGFVFQSFQLLPH 111
Cdd:PRK10636 326 IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLA-------GEL-----------APVSGEIGLaKGIKLGYFAQHQLEF 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 112 LTALENvmlPLRLQEKFKYAEAEQKALNLLKRVGLE-RQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDge 190
Cdd:PRK10636 388 LRADES---PLQHLARLAPQELEQKLRDYLGGFGFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD-- 462
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491113568 191 taTEIEQLLFELNRELGTTLVLVTHDPKLAAQCQRHYALIDGQLVEQFA 239
Cdd:PRK10636 463 --LDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFD 509
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
157-216 |
7.01e-07 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 47.95 E-value: 7.01e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 157 LSGGEQQRVAIARALIREPKIIFADEPTGNLDGETATEIEQLLFELNRELGTTLVLVTHD 216
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHD 131
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
34-194 |
7.65e-07 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 48.75 E-value: 7.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 34 IFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELnEEQRAEVRLKHI---GFVFQS---FQ 107
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKL-PLHTLRSRLSIIlqdPILFSGsirFN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 108 LLPHLTALENvmlplRLQEKFKYAEAEqkalNLLKRV--GLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPTG 185
Cdd:cd03288 115 LDPECKCTDD-----RLWEALEIAQLK----NMVKSLpgGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATA 185
|
....*....
gi 491113568 186 NLDgeTATE 194
Cdd:cd03288 186 SID--MATE 192
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
36-215 |
2.63e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.80 E-value: 2.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 36 ENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGEsiaELNEEQRAEVRLKHIGFVFQSFQLLPHLTAL 115
Cdd:PRK10982 15 DNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGK---EIDFKSSKEALENGISMVHQELNLVLQRSVM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 116 ENVMLPlRLQEKFKYAEaEQKALNLLKRVGLERQAQQTPKV----LSGGEQQRVAIARALIREPKIIFADEPTGNLdgeT 191
Cdd:PRK10982 92 DNMWLG-RYPTKGMFVD-QDKMYRDTKAIFDELDIDIDPRAkvatLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL---T 166
|
170 180
....*....|....*....|....*..
gi 491113568 192 ATEIEQlLFELNREL---GTTLVLVTH 215
Cdd:PRK10982 167 EKEVNH-LFTIIRKLkerGCGIVYISH 192
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
45-218 |
2.75e-06 |
|
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: 45.83 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 45 GEQVAITGRSGSGKSTLLGILAT-LDQASSGKLVVCGESIAELNEEQRAEVRLKHigfvfqsfqllphltalenvmlplr 123
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALAReLGPPGGGVIYIDGEDILEEVLDQLLLIIVGG------------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 124 lqekfkyaeaeqkalnllkrvglerqaqqTPKVLSGGEQQRVAIARALIREPKIIFADEPTGNLDGETATEI-----EQL 198
Cdd:smart00382 57 -----------------------------KKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLllleeLRL 107
|
170 180
....*....|....*....|
gi 491113568 199 LFELNRELGTTLVLVTHDPK 218
Cdd:smart00382 108 LLLLKSEKNLTVILTTNDEK 127
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
39-213 |
2.76e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.70 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 39 NFDIQEGEQVAITGRSGSGKSTLlgilatlDQASSGKLV-VCGESIaelNEEQRAeVRLkhigfvfqSFQLLPHLTALE- 116
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSAL-------ARALAGELPlLSGERQ---SQFSHI-TRL--------SFEQLQKLVSDEw 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 117 ---NVMLPLRLQEKFKYAEAE---------QKALNLLKRVGLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADEPT 184
Cdd:PRK10938 84 qrnNTDMLSPGEDDTGRTTAEiiqdevkdpARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPF 163
|
170 180
....*....|....*....|....*....
gi 491113568 185 GNLDGETATEIEQLLFELNRElGTTLVLV 213
Cdd:PRK10938 164 DGLDVASRQQLAELLASLHQS-GITLVLV 191
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
37-219 |
3.42e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 46.48 E-value: 3.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 37 NLNFDIQEGEQVAITGRSGSGKSTLlgILATLDQASSGKLVvcgESIAELneeqrAEVRLKHIGfvfqsfqlLPHLTALE 116
Cdd:cd03270 13 NVDVDIPRNKLVVITGVSGSGKSSL--AFDTIYAEGQRRYV---ESLSAY-----ARQFLGQMD--------KPDVDSIE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 117 NVMLPLRLQEKFK---------------------YAEAEQKA-LNLLKRVGL-----ERQAQqtpkVLSGGEQQRVAIAR 169
Cdd:cd03270 75 GLSPAIAIDQKTTsrnprstvgtvteiydylrllFARVGIRErLGFLVDVGLgyltlSRSAP----TLSGGEAQRIRLAT 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491113568 170 ALIRE-PKIIFA-DEPTGNLDGETATEIEQLLFELnRELGTTLVLVTHDPKL 219
Cdd:cd03270 151 QIGSGlTGVLYVlDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDEDT 201
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
48-216 |
1.41e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 44.62 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 48 VAITGRSGSGKSTLL-GILATLDQASSGKLVVCGESIAELNEEQRAEVRLKHIGFVF---------------------QS 105
Cdd:COG0419 26 NLIVGPNGAGKSTILeAIRYALYGKARSRSKLRSDLINVGSEEASVELEFEHGGKRYrierrqgefaefleakpserkEA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 106 FQLLPHLTALENVMLPLR-LQEKFKYAEAEQKALNLLKRVGLER-QAQQTPKVLSGGEQQRVAIARALirepkIIFADep 183
Cdd:COG0419 106 LKRLLGLEIYEELKERLKeLEEALESALEELAELQKLKQEILAQlSGLDPIETLSGGERLRLALADLL-----SLILD-- 178
|
170 180 190
....*....|....*....|....*....|...
gi 491113568 184 TGNLDGETateIEQLLFELNRelgttLVLVTHD 216
Cdd:COG0419 179 FGSLDEER---LERLLDALEE-----LAIITHV 203
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
23-190 |
7.91e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 42.17 E-value: 7.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 23 QKIQLAQKQLTIFeNLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGESIAELNEeqraevrlKHIGFV 102
Cdd:PRK13541 5 HQLQFNIEQKNLF-DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAK--------PYCTYI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 103 FQSFQLLPHLTALENVMLplrLQEKFKYAEAEQKALNLLKrvgLERQAQQTPKVLSGGEQQRVAIARALIREPKIIFADE 182
Cdd:PRK13541 76 GHNLGLKLEMTVFENLKF---WSEIYNSAETLYAAIHYFK---LHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDE 149
|
....*...
gi 491113568 183 PTGNLDGE 190
Cdd:PRK13541 150 VETNLSKE 157
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
138-215 |
8.08e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 43.46 E-value: 8.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 138 LNLLKRVGLE--RQAQQTPkVLSGGEQQRVAIARALIRE---PKIIFADEPTGNLDGEtatEIEQLLFELNR--ELGTTL 210
Cdd:TIGR00630 810 LQTLCDVGLGyiRLGQPAT-TLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFD---DIKKLLEVLQRlvDKGNTV 885
|
....*
gi 491113568 211 VLVTH 215
Cdd:TIGR00630 886 VVIEH 890
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
125-240 |
1.82e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.08 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 125 QEKFKYAEAEQKALNLlkrvglerqaqQTPKV------LSGGEQQRVAIARALIREPKIIFADEPTGNLDGETATEIEQL 198
Cdd:NF040905 378 NEEIKVAEEYRKKMNI-----------KTPSVfqkvgnLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTI 446
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 491113568 199 LFELNRELGTTLVLVTHDPKLAAQCQRHYALIDGQLVEQFAA 240
Cdd:NF040905 447 INELAAEGKGVIVISSELPELLGMCDRIYVMNEGRITGELPR 488
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
135-215 |
1.99e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 42.32 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 135 QKALNLLKRVGLE--RQAQQTPkVLSGGEQQRVAIARALIREPK----IIFaDEPTGNL---DgetateIEQLLFELNR- 204
Cdd:COG0178 804 ARKLQTLQDVGLGyiKLGQPAT-TLSGGEAQRVKLASELSKRSTgktlYIL-DEPTTGLhfhD------IRKLLEVLHRl 875
|
90
....*....|..
gi 491113568 205 -ELGTTLVLVTH 215
Cdd:COG0178 876 vDKGNTVVVIEH 887
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
35-68 |
2.72e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 37.96 E-value: 2.72e-04
10 20 30
....*....|....*....|....*....|....
gi 491113568 35 FENLNFDIQEGEQVAITGRSGSGKSTLLGILATL 68
Cdd:pfam13555 12 FDGHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTL 45
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
157-249 |
5.27e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 5.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 157 LSGGEQQRVAIARALIREPKII--FADEPTGNLDGETATEIEQLLFELnRELGTTLVLVTHDPKLAAQCQRhyaLIDgql 234
Cdd:PRK00635 477 LSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKL-RDQGNTVLLVEHDEQMISLADR---IID--- 549
|
90
....*....|....*
gi 491113568 235 veqfaAKPTAAITGG 249
Cdd:PRK00635 550 -----IGPGAGIFGG 559
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
138-215 |
7.09e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.44 E-value: 7.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 138 LNLLKRVGLE--RQAQQTPkVLSGGEQQRVAIARALIREPK-----IIfaDEPTGNLDGEtatEIEQLLFELNR--ELGT 208
Cdd:PRK00349 811 LQTLVDVGLGyiKLGQPAT-TLSGGEAQRVKLAKELSKRSTgktlyIL--DEPTTGLHFE---DIRKLLEVLHRlvDKGN 884
|
....*..
gi 491113568 209 TLVLVTH 215
Cdd:PRK00349 885 TVVVIEH 891
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
157-221 |
1.19e-03 |
|
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: 38.49 E-value: 1.19e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 157 LSGGEQQRVAIA-----RALIREPKIIFaDEPTGNLDGETATEIEQLLFELNRElGTTLVLVTHDPKLAA 221
Cdd:cd03227 78 LSGGEKELSALAlilalASLKPRPLYIL-DEIDRGLDPRDGQALAEAILEHLVK-GAQVIVITHLPELAE 145
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
37-68 |
2.89e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 38.52 E-value: 2.89e-03
10 20 30
....*....|....*....|....*....|..
gi 491113568 37 NLNFDIQEGEQVAITGRSGSGKSTLlgILATL 68
Cdd:PRK00349 627 NVDVEIPLGKFTCVTGVSGSGKSTL--INETL 656
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
19-82 |
3.20e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 38.33 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113568 19 QNLTQKIQLAQKQLT----------------IFENLNFDIQEGEQVAITGRSGSGKSTLLGILATLDQASSGKLVVCGES 82
Cdd:PRK13545 8 EHVTKKYKMYNKPFDklkdlffrskdgeyhyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA 87
|
|
| |
