|
Name |
Accession |
Description |
Interval |
E-value |
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
6-243 |
1.07e-95 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 289.61 E-value: 1.07e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 6 TPLVEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDAKKYGI 85
Cdd:COG1129 2 EPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 86 ETIYQTLAVADNVDAAANLYLGRELRTpWGTLDDVAMEAKAREVMGRLNPNFqRFKEPVKALSGGQRQSVAIARAILFDA 165
Cdd:COG1129 82 AIIHQELNLVPNLSVAENIFLGREPRR-GGLIDWRAMRRRARELLARLGLDI-DPDTPVGDLSVAQQQLVEIARALSRDA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489631109 166 RILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTEDVTKDEVLGMII 243
Cdd:COG1129 160 RVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVRLMV 237
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
9-227 |
2.71e-80 |
|
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: 238.87 E-value: 2.71e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDAKKYGIETI 88
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 89 YQtlavadnvdaaanlylgrelrtpwgtlddvameakarevmgrlnpnfqrfkepvkaLSGGQRQSVAIARAILFDARIL 168
Cdd:cd03216 81 YQ--------------------------------------------------------LSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489631109 169 IMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVVGH 227
Cdd:cd03216 105 ILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
6-250 |
4.84e-75 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 236.46 E-value: 4.84e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 6 TPLVEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDAKKYGI 85
Cdd:COG3845 3 PPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 86 ETIYQ--TLavadnvdaaanLYLGRElRTPWGTLDDVAMEAKAREVMGR----LNPNfqrfkEPVKALSGGQRQSVAIAR 159
Cdd:COG3845 83 GMVHQhfMLvpnlt--vaenIVLGLE-PTKGGRLDRKAARARIRELSERygldVDPD-----AKVEDLSVGEQQRVEILK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 160 AILFDARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTEDVTKDEVL 239
Cdd:COG3845 155 ALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEELA 234
|
250
....*....|.
gi 489631109 240 GMIIMGKVPPK 250
Cdd:COG3845 235 ELMVGREVLLR 245
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
6-243 |
9.40e-65 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 209.86 E-value: 9.40e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 6 TPLVEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDAKKYGI 85
Cdd:PRK10762 2 QALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 86 ETIYQTLAVADNVDAAANLYLGRELRTPWGTLDDVAMEAKAREVMGRLNPNFqRFKEPVKALSGGQRQSVAIARAILFDA 165
Cdd:PRK10762 82 GIIHQELNLIPQLTIAENIFLGREFVNRFGRIDWKKMYAEADKLLARLNLRF-SSDKLVGELSIGEQQMVEIAKVLSFES 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489631109 166 RILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTEDVTKDEVLGMII 243
Cdd:PRK10762 161 KVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTEDSLIEMMV 238
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
7-243 |
1.35e-59 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 196.30 E-value: 1.35e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 7 PLVEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDA--GEILINGEPAEINNPRDAKKYG 84
Cdd:PRK13549 4 YLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELQASNIRDTERAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 85 IETIYQTLAVADNVDAAANLYLGRELrTPWGTLDDVAMEAKAREVMGRL----NPNfqrfkEPVKALSGGQRQSVAIARA 160
Cdd:PRK13549 84 IAIIHQELALVKELSVLENIFLGNEI-TPGGIMDYDAMYLRAQKLLAQLkldiNPA-----TPVGNLGLGQQQLVEIAKA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 161 ILFDARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTEDVTKDEVLG 240
Cdd:PRK13549 158 LNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDDIIT 237
|
...
gi 489631109 241 MII 243
Cdd:PRK13549 238 MMV 240
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
6-243 |
1.90e-56 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 188.45 E-value: 1.90e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 6 TPLVEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDAKKYGI 85
Cdd:PRK09700 3 TPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 86 ETIYQTLAVADNVDAAANLYLGREL-RTPWGT--LDDVAMEAKAREVMGRLNPNFQrFKEPVKALSGGQRQSVAIARAIL 162
Cdd:PRK09700 83 GIIYQELSVIDELTVLENLYIGRHLtKKVCGVniIDWREMRVRAAMMLLRVGLKVD-LDEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 163 FDARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTEDVTKDEVLGMI 242
Cdd:PRK09700 162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVRLM 241
|
.
gi 489631109 243 I 243
Cdd:PRK09700 242 V 242
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
9-235 |
2.95e-56 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 179.87 E-value: 2.95e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEiNNPRDAKK------ 82
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA-RDPAEVRRrigyvp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 83 -----YGIETIYQTLAvadnvdaaanlYLGReLRTpwgtLDDVAMEAKAREVMGRLNPNfQRFKEPVKALSGGQRQSVAI 157
Cdd:COG1131 80 qepalYPDLTVRENLR-----------FFAR-LYG----LPRKEARERIDELLELFGLT-DAADRKVGTLSGGMKQRLGL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489631109 158 ARAILFDARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTEDVTK 235
Cdd:COG1131 143 ALALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKA 220
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
10-237 |
2.98e-55 |
|
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: 177.63 E-value: 2.98e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 10 EMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEpaEINN--PRDAKKYGIET 87
Cdd:cd03219 2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGE--DITGlpPHEIARLGIGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 88 IYQTLAVADNVDAAANLYLGRELRTPWGTLDDV------AMEAKAREVMGRLNPNfQRFKEPVKALSGGQRQSVAIARAI 161
Cdd:cd03219 80 TFQIPRLFPELTVLENVMVAAQARTGSGLLLARarreerEARERAEELLERVGLA-DLADRPAGELSYGQQRRLEIARAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489631109 162 LFDARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTEDVTKDE 237
Cdd:cd03219 159 ATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNP 234
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
6-240 |
1.64e-54 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 182.80 E-value: 1.64e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 6 TPLVEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDAKKYGI 85
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 86 ETIYQTLAVADNVDAAANLYLGReLRTPWGTLDDVAMEAKAREVMGRL----NPNfqrfkEPVKALSGGQRQSVAIARAI 161
Cdd:PRK11288 82 AIIYQELHLVPEMTVAENLYLGQ-LPHKGGIVNRRLLNYEAREQLEHLgvdiDPD-----TPLKYLSIGQRQMVEIAKAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 162 LFDARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVVG-HARTEDVTKDEVLG 240
Cdd:PRK11288 156 ARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVAtFDDMAQVDRDQLVQ 235
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
6-237 |
3.05e-54 |
|
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: 175.61 E-value: 3.05e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 6 TPLVEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGE------PAEINnprd 79
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRditglpPHRIA---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 80 akKYGIETIYQTLAVAD-----------NVDAAANLYLGRELRTPWGTLDDVAMEAKAREVMGRLNPNFQRfKEPVKALS 148
Cdd:COG0411 78 --RLGIARTFQNPRLFPeltvlenvlvaAHARLGRGLLAALLRLPRARREEREARERAEELLERVGLADRA-DEPAGNLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 149 GGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDLADRVSVMKNGQVVGH 227
Cdd:COG0411 155 YGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGRVIAE 234
|
250
....*....|
gi 489631109 228 ARTEDVTKDE 237
Cdd:COG0411 235 GTPAEVRADP 244
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-233 |
6.62e-53 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 178.94 E-value: 6.62e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 1 MTEQRTPLVEMKNISISF-----GGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEIN 75
Cdd:COG1123 253 AAAAAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 76 NPRDAKKYG--IETIYQ----------TlavadnvdaaanlyLGRELRTPW---GTLDDVAMEAKAREVMGR--LNPNF- 137
Cdd:COG1123 333 SRRSLRELRrrVQMVFQdpysslnprmT--------------VGDIIAEPLrlhGLLSRAERRERVAELLERvgLPPDLa 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 138 QRFkePvKALSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDLADRV 216
Cdd:COG1123 399 DRY--P-HELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRV 475
|
250
....*....|....*..
gi 489631109 217 SVMKNGQVVGHARTEDV 233
Cdd:COG1123 476 AVMYDGRIVEDGPTEEV 492
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
9-224 |
8.11e-51 |
|
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: 164.11 E-value: 8.11e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAeINNPRDAKK---YGI 85
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI-KKEPEEVKRrigYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 86 ETI--YQTLavadnvdaaanlylgrelrTPWGTLDdvameakarevmgrlnpnfqrfkepvkaLSGGQRQSVAIARAILF 163
Cdd:cd03230 80 EEPslYENL-------------------TVRENLK----------------------------LSGGMKQRLALAQALLH 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489631109 164 DARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQV 224
Cdd:cd03230 113 DPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
9-233 |
1.31e-50 |
|
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: 165.20 E-value: 1.31e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISF-GGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRD-AKKYGI- 85
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElRRKVGLv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 86 ----------ETIYqtlavadnvdaaanlylgrelrtpwgtlDDVA------------MEAKAREVMGRLNpnFQRFKE- 142
Cdd:COG1122 81 fqnpddqlfaPTVE----------------------------EDVAfgpenlglpreeIRERVEEALELVG--LEHLADr 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 143 PVKALSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNG 222
Cdd:COG1122 131 PPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDG 210
|
250
....*....|.
gi 489631109 223 QVVGHARTEDV 233
Cdd:COG1122 211 RIVADGTPREV 221
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
8-243 |
3.03e-49 |
|
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: 169.24 E-value: 3.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 8 LVEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDA--GEILINGEPAEINNPRDAKKYGI 85
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 86 ETIYQTLAVADNVDAAANLYLGRELRTPWGTLDDVAMEAKAREVMGRLNPNFQRFKEPVKALSGGQRQSVAIARAILFDA 165
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489631109 166 RILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTEDVTKDEVLGMII 243
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMV 238
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
10-223 |
6.14e-47 |
|
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: 155.32 E-value: 6.14e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 10 EMKNISISFGG--IHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRD-AKKYGI- 85
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElRRKVGLv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 86 ----------ETIYQTLAvadnvdaaanlyLGRELRTpwgtLDDVAMEAKAREVMGRLNPNFQRfKEPVKALSGGQRQSV 155
Cdd:cd03225 81 fqnpddqffgPTVEEEVA------------FGLENLG----LPEEEIEERVEEALELVGLEGLR-DRSPFTLSGGQKQRV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489631109 156 AIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQ 223
Cdd:cd03225 144 AIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
6-239 |
8.30e-47 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 156.02 E-value: 8.30e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 6 TPLVEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDAkkY-- 83
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIG--Yvp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 84 ---GIE-----TIYQTLAvadnvdaaanlyLGRELRTPWGTLDDVAMEAKAREVMGRLNpnFQRFKE-PVKALSGGQRQS 154
Cdd:COG1121 82 qraEVDwdfpiTVRDVVL------------MGRYGRRGLFRRPSRADREAVDEALERVG--LEDLADrPIGELSGGQQQR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 155 VAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMkNGQVVGHARTEDVT 234
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVL 226
|
....*
gi 489631109 235 KDEVL 239
Cdd:COG1121 227 TPENL 231
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
8-239 |
1.44e-46 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 155.59 E-value: 1.44e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 8 LVEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEP-AEInNPRD-AKKYGI 85
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDlASL-SRRElARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 86 etIYQTLAVADNvdaaanlYLGREL----RTP----WGTLDDvAMEAKAREVMGRLnpNFQRFKE-PVKALSGGQRQSVA 156
Cdd:COG1120 80 --VPQEPPAPFG-------LTVRELvalgRYPhlglFGRPSA-EDREAVEEALERT--GLEHLADrPVDELSGGERQRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 157 IARAILFDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTEDVTK 235
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLT 227
|
....
gi 489631109 236 DEVL 239
Cdd:COG1120 228 PELL 231
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
8-228 |
8.02e-45 |
|
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: 150.35 E-value: 8.02e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 8 LVEMKNISISF----GGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDAKKY 83
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 84 G--IETIYQ----------TLavadnvdaaanlylGRELRTP---WGTLD-DVAMEAKAREVMGRLNPNFQRFKEPVKAL 147
Cdd:cd03257 81 RkeIQMVFQdpmsslnprmTI--------------GEQIAEPlriHGKLSkKEARKEAVLLLLVGVGLPEEVLNRYPHEL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 148 SGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDLADRVSVMKNGQVVG 226
Cdd:cd03257 147 SGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIVE 226
|
..
gi 489631109 227 HA 228
Cdd:cd03257 227 EG 228
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
8-233 |
1.01e-44 |
|
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: 150.78 E-value: 1.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 8 LVEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDAKKYGIet 87
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 88 IYQtlavadnvdaAANLYLGRELR-------TPWGtLDDVAMEAKAREVMGRLN-PNFQRFKepVKALSGGQRQSVAIAR 159
Cdd:COG4555 79 LPD----------ERGLYDRLTVReniryfaELYG-LFDEELKKRIEELIELLGlEEFLDRR--VGELSTGMKKKVALAR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489631109 160 AILFDARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTEDV 233
Cdd:COG4555 146 ALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-242 |
2.61e-44 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 155.98 E-value: 2.61e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 5 RTPLVEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDAKKYG 84
Cdd:PRK15439 8 APPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 85 IETIYQ-TLAVADNVDAAANLYlgrelRTPWGTLDDVAMEAKAREVMGRLNPNFQrfkepVKALSGGQRQSVAIARAILF 163
Cdd:PRK15439 88 IYLVPQePLLFPNLSVKENILF-----GLPKRQASMQKMKQLLAALGCQLDLDSS-----AGSLEVADRQIVEILRGLMR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489631109 164 DARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTEDVTKDEVLGMI 242
Cdd:PRK15439 158 DSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDIIQAI 236
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
8-242 |
8.08e-44 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 154.56 E-value: 8.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 8 LVEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRD--AGEILINGEPAEINNPRDAKKYGI 85
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDGEVCRFKDIRDSEALGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 86 ETIYQTLAVADNVDAAANLYLGRElRTPWGTLDDVAMEAKAREVMGRL----NPNfqrfkEPVKALSGGQRQSVAIARAI 161
Cdd:NF040905 81 VIIHQELALIPYLSIAENIFLGNE-RAKRGVIDWNETNRRARELLAKVgldeSPD-----TLVTDIGVGKQQLVEIAKAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 162 LFDARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVVG--HARTEDVTKDEVL 239
Cdd:NF040905 155 SKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIEtlDCRADEVTEDRII 234
|
....
gi 489631109 240 -GMI 242
Cdd:NF040905 235 rGMV 238
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
9-223 |
8.59e-44 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 146.18 E-value: 8.59e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDakkygieti 88
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDEL--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 89 yqtlavadnvdaaanlylgRELRTPWGTL--DdvameakarevmGRLNPNFQRFKEPVKALSGGQRQSVAIARAILFDAR 166
Cdd:cd03229 72 -------------------PPLRRRIGMVfqD------------FALFPHLTVLENIALGLSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489631109 167 ILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDLADRVSVMKNGQ 223
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
11-243 |
1.03e-43 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 154.12 E-value: 1.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 11 MKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDAKKYGIETIYQ 90
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 91 TLAVADNVDAAANLYLGRELRTPWgTLDDVAMEAKAREVMGRLNPNFQRfKEPVKALSGGQRQSVAIARAILFDARILIM 170
Cdd:PRK10982 81 ELNLVLQRSVMDNMWLGRYPTKGM-FVDQDKMYRDTKAIFDELDIDIDP-RAKVATLSVSQMQMIEIAKAFSYNAKIVIM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489631109 171 DEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTEDVTKDEVLGMII 243
Cdd:PRK10982 159 DEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIAMMV 231
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
10-227 |
2.20e-43 |
|
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: 146.14 E-value: 2.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 10 EMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDA---KKYGIE 86
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGyvpQRRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 87 -----TIYQTLAvadnvdaaanlyLGRELRTPWGTLDDVAMEAKAREVMGRLNPnFQRFKEPVKALSGGQRQSVAIARAI 161
Cdd:cd03235 81 rdfpiSVRDVVL------------MGLYGHKGLFRRLSKADKAKVDEALERVGL-SELADRQIGELSGGQQQRVLLARAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489631109 162 LFDARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVsVMKNGQVVGH 227
Cdd:cd03235 148 VQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRV-LLLNRTVVAS 212
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
10-223 |
5.67e-43 |
|
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: 143.54 E-value: 5.67e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 10 EMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRdakkygietiy 89
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLE----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 90 qtlavadnvdaaanlylgrELRTPWGTLddvameakarevmgrlnpnFQrfkepvkaLSGGQRQSVAIARAILFDARILI 169
Cdd:cd00267 70 -------------------ELRRRIGYV-------------------PQ--------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489631109 170 MDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQ 223
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
8-233 |
1.29e-42 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 145.33 E-value: 1.29e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 8 LVEMKNISISFG----GIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDAKK- 82
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 83 --------YGI----ETIYQTLAVADnvdaaanlylgRELRTPwgtlddvAMEAKAREVMGR--LNPNFqRFKEPvKALS 148
Cdd:COG1124 81 vqmvfqdpYASlhprHTVDRILAEPL-----------RIHGLP-------DREERIAELLEQvgLPPSF-LDRYP-HQLS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 149 GGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDLADRVSVMKNGQVVGH 227
Cdd:COG1124 141 GGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEE 220
|
....*.
gi 489631109 228 ARTEDV 233
Cdd:COG1124 221 LTVADL 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-233 |
3.15e-42 |
|
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: 150.44 E-value: 3.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 6 TPLVEMKNISISF--GGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDA---GEILINGEPAEINNPRDA 80
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 81 KKYgIETIYQtlavaDNVDAAANLYLGRELRTP--WGTLDDVAMEAKAREVMGRLNPNfQRFKEPVKALSGGQRQSVAIA 158
Cdd:COG1123 82 GRR-IGMVFQ-----DPMTQLNPVTVGDQIAEAleNLGLSRAEARARVLELLEAVGLE-RRLDRYPHQLSGGQRQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489631109 159 RAILFDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTEDV 233
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
6-237 |
1.17e-41 |
|
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: 142.43 E-value: 1.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 6 TPLVEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEpaEINN--PRDAKKY 83
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGE--DITGlpPHRIARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 84 GIETIYQtlavadnvdaaanlylGRE----------LRTPWGTLDDVAMEAKAREVMGRLnpnFQRFKE----PVKALSG 149
Cdd:COG0410 79 GIGYVPE----------------GRRifpsltveenLLLGAYARRDRAEVRADLERVYEL---FPRLKErrrqRAGTLSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 150 GQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVVGHAR 229
Cdd:COG0410 140 GEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGT 219
|
....*...
gi 489631109 230 TEDVTKDE 237
Cdd:COG0410 220 AAELLADP 227
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
10-236 |
1.47e-41 |
|
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: 141.80 E-value: 1.47e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 10 EMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDAKKYGIE--- 86
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGyvp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 87 ---------TIYQTLAvadnvdaaanlyLGRELRTPwgtlddvameAKAREVMGRLNPNFQRFKE----PVKALSGGQRQ 153
Cdd:cd03224 82 egrrifpelTVEENLL------------LGAYARRR----------AKRKARLERVYELFPRLKErrkqLAGTLSGGEQQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 154 SVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTEDV 233
Cdd:cd03224 140 MLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
...
gi 489631109 234 TKD 236
Cdd:cd03224 220 LAD 222
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-239 |
3.16e-41 |
|
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: 141.66 E-value: 3.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 4 QRTPLVEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEpaEINNPRDAKKY 83
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQ--DITGLSEKELY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 84 GIE----------------TIYQTLavadnvdaaaNLYLgRELrtpwGTLDDVAMEAKAREVMGRLN-PNFqRFKEPvKA 146
Cdd:COG1127 79 ELRrrigmlfqggalfdslTVFENV----------AFPL-REH----TDLSEAEIRELVLEKLELVGlPGA-ADKMP-SE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 147 LSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDLADRVSVMKNGQVV 225
Cdd:COG1127 142 LSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKII 221
|
250
....*....|....*.
gi 489631109 226 GHARTEDV--TKDEVL 239
Cdd:COG1127 222 AEGTPEELlaSDDPWV 237
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
7-246 |
7.39e-41 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 146.70 E-value: 7.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 7 PLVEMKNISisfgGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDAKKYGI- 85
Cdd:COG1129 255 VVLEVEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRAGIa 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 86 --------------ETIYQ--TLAVadnvdaaanlyLGRelRTPWGTLDDVAMEAKAREVMGRLNPNFQRFKEPVKALSG 149
Cdd:COG1129 331 yvpedrkgeglvldLSIREniTLAS-----------LDR--LSRGGLLDRRRERALAEEYIKRLRIKTPSPEQPVGNLSG 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 150 GQRQSVAIARAILFDARILIMDEPT-----AAlgpqeTAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQV 224
Cdd:COG1129 398 GNQQKVVLAKWLATDPKVLILDEPTrgidvGA-----KAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRI 472
|
250 260
....*....|....*....|..
gi 489631109 225 VGHARTEDVTKDEVLGMIIMGK 246
Cdd:COG1129 473 VGELDREEATEEAIMAAATGGA 494
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
10-225 |
9.91e-41 |
|
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: 139.31 E-value: 9.91e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 10 EMKNISISFG-GIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPaeINNPRDAKKYGI--- 85
Cdd:cd03226 1 RIENISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKP--IKAKERRKSIGYvmq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 86 ETIYQtlavadnvdaaanLY---LGRELRTPWGTLDDVamEAKAREVMGRLNPNFQRFKEPvKALSGGQRQSVAIARAIL 162
Cdd:cd03226 79 DVDYQ-------------LFtdsVREELLLGLKELDAG--NEQAETVLKDLDLYALKERHP-LSLSGGQKQRLAIAAALL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489631109 163 FDARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVV 225
Cdd:cd03226 143 SGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
10-225 |
1.02e-40 |
|
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: 138.34 E-value: 1.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 10 EMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRD-AKKYGieti 88
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKElARKIA---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 89 yqtlavadnvdaaanlYLGRelrtpwgTLDDVAMEAKArevmgrlnpnfqrfKEPVKALSGGQRQSVAIARAILFDARIL 168
Cdd:cd03214 77 ----------------YVPQ-------ALELLGLAHLA--------------DRPFNELSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489631109 169 IMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDLADRVSVMKNGQVV 225
Cdd:cd03214 120 LLDEPTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
9-224 |
5.29e-39 |
|
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: 135.31 E-value: 5.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFGG----IHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEpaEINNPRDAKK-- 82
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGT--DISKLSEKELaa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 83 ---YGIETIYQTLavadnvdaaanlYLGRELrtpwgT-LDDVAM------------EAKAREVMGRLNPNfQRFKEPVKA 146
Cdd:cd03255 79 frrRHIGFVFQSF------------NLLPDL-----TaLENVELplllagvpkkerRERAEELLERVGLG-DRLNHYPSE 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489631109 147 LSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDiHDVFDLADRVSVMKNGQV 224
Cdd:cd03255 141 LSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
9-233 |
6.92e-39 |
|
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: 135.32 E-value: 6.92e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRD----AKKYG 84
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 85 IE----------TIYQTLAvadnvdaaanLYLgRELRTpwgtLDDVAMEAKAREVMGRLNPNFQRFKEPVKaLSGGQRQS 154
Cdd:cd03261 81 MLfqsgalfdslTVFENVA----------FPL-REHTR----LSEEEIREIVLEKLEAVGLRGAEDLYPAE-LSGGMKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 155 VAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTEDV 233
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
9-233 |
1.87e-38 |
|
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: 133.85 E-value: 1.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSG-----AYKRDAGEILINGEpaEINNPRDA--- 80
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGK--DIYDLDVDvle 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 81 --KKYGI---------ETIYQTLAvadnvdaaanlyLGRELRTPWGT--LDDVAMEA--KA---REVMGRLNPnfqrfke 142
Cdd:cd03260 79 lrRRVGMvfqkpnpfpGSIYDNVA------------YGLRLHGIKLKeeLDERVEEAlrKAalwDEVKDRLHA------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 143 pvKALSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKREgIGIFLISHDIHDVFDLADRVSVMKNG 222
Cdd:cd03260 140 --LGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNG 216
|
250
....*....|.
gi 489631109 223 QVVGHARTEDV 233
Cdd:cd03260 217 RLVEFGPTEQI 227
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
7-238 |
4.40e-38 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 133.64 E-value: 4.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 7 PLVEMKNISISF-GGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDAKKY-- 83
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 84 GIETIYQ-----------------TLAVADNVDAAANLYLGRELRTPWGTLDDVAMEAKArevmgrlnpnFQRfkepVKA 146
Cdd:COG3638 81 RIGMIFQqfnlvprlsvltnvlagRLGRTSTWRSLLGLFPPEDRERALEALERVGLADKA----------YQR----ADQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 147 LSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIfLIShdIHDVfDLA----DRVSVMKN 221
Cdd:COG3638 147 LSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREdGITV-VVN--LHQV-DLArryaDRIIGLRD 222
|
250
....*....|....*..
gi 489631109 222 GQVVGHARTEDVTKDEV 238
Cdd:COG3638 223 GRVVFDGPPAELTDAVL 239
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-237 |
9.09e-38 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 133.29 E-value: 9.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 1 MTeQRTPLVEMKNISISF----GGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINN 76
Cdd:COG1116 1 MS-AAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 77 PRdakkYGIetIYQTlavadnvdaaANLYlgrelrtPWGT-LDDVAM------------EAKAREVMGRLNpnFQRFKE- 142
Cdd:COG1116 80 PD----RGV--VFQE----------PALL-------PWLTvLDNVALglelrgvpkaerRERARELLELVG--LAGFEDa 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 143 -PvKALSGGQRQSVAIARAILFDARILIMDEPTAALGPQeTAQV--GELIKQLKREGIGIFLISHDIHD-VFdLADRVSV 218
Cdd:COG1116 135 yP-HQLSGGMRQRVAIARALANDPEVLLMDEPFGALDAL-TRERlqDELLRLWQETGKTVLFVTHDVDEaVF-LADRVVV 211
|
250 260
....*....|....*....|....*...
gi 489631109 219 MKN--GQVVG-------HARTEDVTKDE 237
Cdd:COG1116 212 LSArpGRIVEeidvdlpRPRDRELRTSP 239
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
8-236 |
1.23e-37 |
|
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: 134.41 E-value: 1.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 8 LVEMKNISISF----GGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYK---RDAGEILINGE------PAEI 74
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEdllklsEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 75 N------------------NPRdakkYGIETIyqtlavadnvdaaanlyLGRELRTpWGTLDDVAMEAKAREVMGR--LN 134
Cdd:COG0444 81 RkirgreiqmifqdpmtslNPV----MTVGDQ-----------------IAEPLRI-HGGLSKAEARERAIELLERvgLP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 135 PNFQRFKE-PVkALSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDL 212
Cdd:COG0444 139 DPERRLDRyPH-ELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEI 217
|
250 260
....*....|....*....|....
gi 489631109 213 ADRVSVMKNGQVVGHARTEDVTKD 236
Cdd:COG0444 218 ADRVAVMYAGRIVEEGPVEELFEN 241
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
9-225 |
2.83e-37 |
|
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: 130.41 E-value: 2.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGePAEINNPRDAKKYG--IE 86
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDG-KSYQKNIEALRRIGalIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 87 --TIYQTLAVADNVDAAANLYLGRELRTPwGTLDDVAMEAKArevmgrlnpnfqrfKEPVKALSGGQRQSVAIARAILFD 164
Cdd:cd03268 80 apGFYPNLTARENLRLLARLLGIRKKRID-EVLDVVGLKDSA--------------KKKVKGFSLGMKQRLGIALALLGN 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489631109 165 ARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVV 225
Cdd:cd03268 145 PDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
8-233 |
2.92e-37 |
|
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: 131.16 E-value: 2.92e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 8 LVEMKNISISFGG----IHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILING------EPAEINNP 77
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGtdltllSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 78 RdaKKYGIetIYQTLAVADNVDAAANLYLGRELrtpWGTlDDVAMEAKAREVMgrlnpNFQRFKEPVKA----LSGGQRQ 153
Cdd:cd03258 81 R--RRIGM--IFQHFNLLSSRTVFENVALPLEI---AGV-PKAEIEERVLELL-----ELVGLEDKADAypaqLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 154 SVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTED 232
Cdd:cd03258 148 RVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEE 227
|
.
gi 489631109 233 V 233
Cdd:cd03258 228 V 228
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
9-226 |
7.08e-37 |
|
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: 129.90 E-value: 7.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFGG----IHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPaeINNPRDAKKYg 84
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEP--VTGPGPDRGY- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 85 ietIYQTlavadnvdaaANLYlgrelrtPWGT-LDDVAMEAKAREV-MGRLNPNFQRFKEPV----------KALSGGQR 152
Cdd:cd03293 78 ---VFQQ----------DALL-------PWLTvLDNVALGLELQGVpKAEARERAEELLELVglsgfenaypHQLSGGMR 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489631109 153 QSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDLADRVSVMKN--GQVVG 226
Cdd:cd03293 138 QRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWREtGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVA 214
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
6-229 |
1.26e-36 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 129.39 E-value: 1.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 6 TPLVEMKNISISFG----GIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRD-- 79
Cdd:COG1136 2 SPLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREla 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 80 ---AKKYGIetIYQT----------------LavadnvdaaanLYLGRELRtpwgtlddvAMEAKAREVMGRLN------ 134
Cdd:COG1136 82 rlrRRHIGF--VFQFfnllpeltalenvalpL-----------LLAGVSRK---------ERRERARELLERVGlgdrld 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 135 --PNfqrfkepvkALSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDiHDVFD 211
Cdd:COG1136 140 hrPS---------QLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHD-PELAA 209
|
250
....*....|....*...
gi 489631109 212 LADRVSVMKNGQVVGHAR 229
Cdd:COG1136 210 RADRVIRLRDGRIVSDER 227
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
9-223 |
1.29e-36 |
|
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: 127.50 E-value: 1.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFGG--IHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPaeinnprdakkygie 86
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVD--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 87 tiyqtlavadnvdaaanlylgrelrtpwgtLDDVAMEAKaREVMGRLNPNFQRFKEPVKA--LSGGQRQSVAIARAILFD 164
Cdd:cd03228 66 ------------------------------LRDLDLESL-RKNIAYVPQDPFLFSGTIREniLSGGQRQRIAIARALLRD 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489631109 165 ARILIMDEPTAALGPQETAQVGELIKQLkREGIGIFLISHDIHDVfDLADRVSVMKNGQ 223
Cdd:cd03228 115 PPILILDEATSALDPETEALILEALRAL-AKGKTVIVIAHRLSTI-RDADRIIVLDDGR 171
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
8-239 |
1.31e-36 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 130.24 E-value: 1.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 8 LVEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRD-AKKYGIE 86
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElARRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 87 TIYQTLAVAdnvdaaanlYLGREL----RTPWGTL----DDVAMEAKAR-EVMGRLNPNFQrfkepvkALSGGQRQSVAI 157
Cdd:COG4559 81 PQHSSLAFP---------FTVEEVvalgRAPHGSSaaqdRQIVREALALvGLAHLAGRSYQ-------TLSGGEQQRVQL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 158 ARAIL-------FDARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHdvfdL----ADRVSVMKNGQVVG 226
Cdd:COG4559 145 ARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLN----LaaqyADRILLLHQGRLVA 220
|
250
....*....|...
gi 489631109 227 HARTEDVTKDEVL 239
Cdd:COG4559 221 QGTPEEVLTDELL 233
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
9-225 |
1.38e-36 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 128.85 E-value: 1.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFGGIHAVDDASVDLYPGeVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGepaeinnpRDAKKYGiETI 88
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDG--------QDVLKQP-QKL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 89 YQTLAvadnvdaaanlYLGRELR-----TPWGTLDDVAM-------EAKAR--EVMGRLNPNfQRFKEPVKALSGGQRQS 154
Cdd:cd03264 71 RRRIG-----------YLPQEFGvypnfTVREFLDYIAWlkgipskEVKARvdEVLELVNLG-DRAKKKIGSLSGGMRRR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489631109 155 VAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKREGIgIFLISHDIHDVFDLADRVSVMKNGQVV 225
Cdd:cd03264 139 VGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRI-VILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
9-225 |
1.86e-36 |
|
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: 128.41 E-value: 1.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPaeINNpRDAKKYGIETI 88
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRD--VTG-VPPERRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 89 YQTlavadnvdaaANLYlgrelrtPWGT-LDDVA------------MEAKAREV--MGRLNPNFQRFkepVKALSGGQRQ 153
Cdd:cd03259 78 FQD----------YALF-------PHLTvAENIAfglklrgvpkaeIRARVRELleLVGLEGLLNRY---PHELSGGQQQ 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489631109 154 SVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDLADRVSVMKNGQVV 225
Cdd:cd03259 138 RVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRElGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
10-224 |
2.58e-36 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 128.01 E-value: 2.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 10 EMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDAKKygiETIY 89
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRR---QVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 90 --QTLAvadnvdaaanLYLG--RE-LRTPWGTLDDVAMEAKAREVMGR--LNPNFqrFKEPVKALSGGQRQSVAIARAIL 162
Cdd:COG4619 79 vpQEPA----------LWGGtvRDnLPFPFQLRERKFDRERALELLERlgLPPDI--LDKPVERLSGGERQRLALIRALL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489631109 163 FDARILIMDEPTAALGPQETAQVGELIKQL-KREGIGIFLISHDIHDVFDLADRVSVMKNGQV 224
Cdd:COG4619 147 LQPDVLLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
24-175 |
4.95e-36 |
|
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: 125.45 E-value: 4.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 24 VDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDAKKyGIETIYQTLAVADNVDAAAN 103
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRK-EIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489631109 104 LYLGRELRtpwgTLDDVAMEAKAREVMGRLN-PNF--QRFKEPVKALSGGQRQSVAIARAILFDARILIMDEPTA 175
Cdd:pfam00005 80 LRLGLLLK----GLSKREKDARAEEALEKLGlGDLadRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
9-239 |
5.34e-36 |
|
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: 135.35 E-value: 5.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFGG--IHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDAKK---- 82
Cdd:COG2274 474 IELENVSFRYPGdsPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRqigv 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 83 --------YGieTIYQTLAvadnvdaaanlyLGRelrtPWGTLDDV---AMEAKAREVMGRLnPNfqRFKEPV----KAL 147
Cdd:COG2274 554 vlqdvflfSG--TIRENIT------------LGD----PDATDEEIieaARLAGLHDFIEAL-PM--GYDTVVgeggSNL 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 148 SGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKReGIGIFLISHDIHDVfDLADRVSVMKNGQVVgh 227
Cdd:COG2274 613 SGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLSTI-RLADRIIVLDKGRIV-- 688
|
250
....*....|..
gi 489631109 228 artEDVTKDEVL 239
Cdd:COG2274 689 ---EDGTHEELL 697
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
9-225 |
1.50e-35 |
|
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: 125.86 E-value: 1.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINN-------PRDAK 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAArnrigylPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 82 KYGIETIYQTLavadnvdaaanLYLGRelrtpwgtLDDVAMEAKAREVMGRLNpnfqRF------KEPVKALSGGQRQSV 155
Cdd:cd03269 81 LYPKMKVIDQL-----------VYLAQ--------LKGLKKEEARRRIDEWLE----RLelseyaNKRVEELSKGNQQKV 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 156 AIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVV 225
Cdd:cd03269 138 QFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
5-233 |
6.71e-35 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 127.91 E-value: 6.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 5 RTPLVEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGE-----PAEinnprd 79
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRdvtglPPE------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 80 akKYGIETIYQTlavadnvdaaanlYL-------------GRELRtpwgTLDDVAMEAKAREVMGRLN-PNF-QRFkepV 144
Cdd:COG3842 76 --KRNVGMVFQD-------------YAlfphltvaenvafGLRMR----GVPKAEIRARVAELLELVGlEGLaDRY---P 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 145 KALSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQL-KREGIGIFLISHDIHDVFDLADRVSVMKNGQ 223
Cdd:COG3842 134 HQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLqRELGITFIYVTHDQEEALALADRIAVMNDGR 213
|
250
....*....|
gi 489631109 224 VVGHARTEDV 233
Cdd:COG3842 214 IEQVGTPEEI 223
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
9-225 |
3.15e-34 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 124.08 E-value: 3.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISF--GGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILING----EPAEINNPRdaKK 82
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGldtlDEENLWEIR--KK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 83 YGIetIYQtlavadnvdaaanlylgrelrTP----WGTL--DDVA------------MEAKAREVMGRLNPNFQRFKEPV 144
Cdd:TIGR04520 79 VGM--VFQ---------------------NPdnqfVGATveDDVAfglenlgvpreeMRKRVDEALKLVGMEDFRDREPH 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 145 KaLSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFdLADRVSVMKNGQ 223
Cdd:TIGR04520 136 L-LSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEeGITVISITHDMEEAV-LADRVIVMNKGK 213
|
..
gi 489631109 224 VV 225
Cdd:TIGR04520 214 IV 215
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
12-225 |
5.14e-34 |
|
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: 122.48 E-value: 5.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 12 KNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAeINNPRDAK-KYGI----E 86
Cdd:cd03266 9 KRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV-VKEPAEARrRLGFvsdsT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 87 TIYQTLAVADNVDAAANLYlGRELRTPWGTLDDVAMEAKAREVMGRlnpnfqrfkePVKALSGGQRQSVAIARAILFDAR 166
Cdd:cd03266 88 GLYDRLTARENLEYFAGLY-GLKGDELTARLEELADRLGMEELLDR----------RVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489631109 167 ILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVV 225
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
9-233 |
9.43e-34 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 123.68 E-value: 9.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPaeiNNPRDAKKYG---- 84
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEP---LDPEDRRRIGylpe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 85 ----------IETIyqtlavadnvdaaanLYLGReLRtpwGtLDDVAMEAKAREVMGRLNPNfQRFKEPVKALSGGQRQS 154
Cdd:COG4152 79 erglypkmkvGEQL---------------VYLAR-LK---G-LSKAEAKRRADEWLERLGLG-DRANKKVEELSKGNQQK 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489631109 155 VAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTEDV 233
Cdd:COG4152 138 VQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
4-233 |
1.12e-33 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 124.07 E-value: 1.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 4 QRTPLVEMKNISISF---GGI--------HAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPA 72
Cdd:COG4608 3 MAEPLLEVRDLKKHFpvrGGLfgrtvgvvKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 73 EINNPRDAKKY--GIETIYQ----------TLavadnvdaaanlylGRELRTPW---GTLDDVAMEAKAREVMGR--LNP 135
Cdd:COG4608 83 TGLSGRELRPLrrRMQMVFQdpyaslnprmTV--------------GDIIAEPLrihGLASKAERRERVAELLELvgLRP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 136 NF-QRFkePvKALSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDLA 213
Cdd:COG4608 149 EHaDRY--P-HEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDElGLTYLFISHDLSVVRHIS 225
|
250 260
....*....|....*....|
gi 489631109 214 DRVSVMKNGQVVGHARTEDV 233
Cdd:COG4608 226 DRVAVMYLGKIVEIAPRDEL 245
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
5-232 |
1.27e-33 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 127.57 E-value: 1.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 5 RTPLVEMKNISISF-GGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEP-AEINNPRDAKK 82
Cdd:COG4988 333 GPPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDlSDLDPASWRRQ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 83 -----------YGieTIYQTLAvadnvdaaanlyLGRELRTPWgTLDDVAMEAKAREVMGRLNpnfQRFKEPV----KAL 147
Cdd:COG4988 413 iawvpqnpylfAG--TIRENLR------------LGRPDASDE-ELEAALEAAGLDEFVAALP---DGLDTPLgeggRGL 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 148 SGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKREGIgIFLISHDIHDVfDLADRVSVMKNGQVVGH 227
Cdd:COG4988 475 SGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRT-VILITHRLALL-AQADRILVLDDGRIVEQ 552
|
....*
gi 489631109 228 ARTED 232
Cdd:COG4988 553 GTHEE 557
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
7-224 |
1.82e-33 |
|
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: 119.84 E-value: 1.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 7 PLVEMKNISISfggiHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDAKKYGIe 86
Cdd:cd03215 3 PVLEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGI- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 87 tiyqtlavadnvdaaanLYLGRELRTpwgtlDDVAMEAKARE--VMGRLnpnfqrfkepvkaLSGGQRQSVAIARAILFD 164
Cdd:cd03215 78 -----------------AYVPEDRKR-----EGLVLDLSVAEniALSSL-------------LSGGNQQKVVLARWLARD 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 165 ARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQV 224
Cdd:cd03215 123 PRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
9-233 |
2.01e-33 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 123.65 E-value: 2.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISF----GGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGE------PAEInnpR 78
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVdltalsEREL---R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 79 DAKKyGIETIYQ--TLavadnvdaaanlyLGRelRT-------P---WGTlDDVAMEAKAREVMgrlnpnfqrfkEPV-- 144
Cdd:COG1135 79 AARR-KIGMIFQhfNL-------------LSS--RTvaenvalPleiAGV-PKAEIRKRVAELL-----------ELVgl 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 145 --KA------LSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDLADR 215
Cdd:COG1135 131 sdKAdaypsqLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDR 210
|
250
....*....|....*...
gi 489631109 216 VSVMKNGQVVGHARTEDV 233
Cdd:COG1135 211 VAVLENGRIVEQGPVLDV 228
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
9-225 |
2.64e-33 |
|
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: 120.55 E-value: 2.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAeINNPRDAKKyGIETI 88
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV-VREPREVRR-RIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 89 YQTLAVADNVDAAANLYL-GRELRTPWGTLDDVAMEakAREVMGRLNpnfqrFK-EPVKALSGGQRQSVAIARAILFDAR 166
Cdd:cd03265 79 FQDLSVDDELTGWENLYIhARLYGVPGAERRERIDE--LLDFVGLLE-----AAdRLVKTYSGGMRRRLEIARSLVHRPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 167 ILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDLADRVSVMKNGQVV 225
Cdd:cd03265 152 VLFLDEPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRII 211
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
6-237 |
2.97e-33 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 121.25 E-value: 2.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 6 TPLVEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDAKKYGI 85
Cdd:PRK11300 3 QPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 86 ETIYQTLAVADNVDAAANLYLG--RELRTPW--GTLDDVAMEAKAREVMGRLNPNFQRF------KEPVKALSGGQRQSV 155
Cdd:PRK11300 83 VRTFQHVRLFREMTVIENLLVAqhQQLKTGLfsGLLKTPAFRRAESEALDRAATWLERVgllehaNRQAGNLAYGQQRRL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 156 AIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTEDVT 234
Cdd:PRK11300 163 EIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIR 242
|
...
gi 489631109 235 KDE 237
Cdd:PRK11300 243 NNP 245
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
10-238 |
3.71e-33 |
|
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: 120.32 E-value: 3.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 10 EMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDAKKYGIETIY 89
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 90 QtlavadnvdaaanlylGRELRTPWGTLDDVAMEAKAREVMGRLNPN--FQRFkePV-------KA--LSGGQRQSVAIA 158
Cdd:TIGR03410 82 Q----------------GREIFPRLTVEENLLTGLAALPRRSRKIPDeiYELF--PVlkemlgrRGgdLSGGQQQQLAIA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 159 RAILFDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTEDVTKDE 237
Cdd:TIGR03410 144 RALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEgGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDEDK 223
|
.
gi 489631109 238 V 238
Cdd:TIGR03410 224 V 224
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
6-223 |
4.51e-33 |
|
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: 120.23 E-value: 4.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 6 TPLVEMKNISISF-----GG--IHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEIN--- 75
Cdd:COG4778 2 TTLLEVENLSKTFtlhlqGGkrLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVDlaq 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 76 -NPRD---AKKYGIETIYQTLavadnvdaaanlylgREL-RTPwgTLDDVAM------------EAKAREVMGRLNpnfq 138
Cdd:COG4778 82 aSPREilaLRRRTIGYVSQFL---------------RVIpRVS--ALDVVAEpllergvdreeaRARARELLARLN---- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 139 rFKEPVKAL-----SGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKREG---IGIFlisHDIHDVF 210
Cdd:COG4778 141 -LPERLWDLppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGtaiIGIF---HDEEVRE 216
|
250
....*....|...
gi 489631109 211 DLADRVSVMKNGQ 223
Cdd:COG4778 217 AVADRVVDVTPFS 229
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
7-216 |
5.22e-33 |
|
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: 119.12 E-value: 5.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 7 PLVEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINnprdakkygIE 86
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDA---------RE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 87 TIYQTLavadnvdaaanLYLG------RELrTPWGTLD-------DVAMEAKAREVMGRLnpNFQRFKE-PVKALSGGQR 152
Cdd:COG4133 72 DYRRRL-----------AYLGhadglkPEL-TVRENLRfwaalygLRADREAIDEALEAV--GLAGLADlPVRQLSAGQK 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489631109 153 QSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDihDVFDLADRV 216
Cdd:COG4133 138 RRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQ--PLELAAARV 199
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
6-233 |
9.99e-33 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 124.80 E-value: 9.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 6 TPLVEMKNISISFGG----IHAVDDASVDLYPGEVVALLGHNGAGKS----TLIKILSGAYKRDAGEILINGE------P 71
Cdd:COG4172 4 MPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQdllglsE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 72 AEINNPRDAKkygIETIYQ------------------TLAvadnvdaaanLYLGrelrtpwgtLDDVAMEAKAREVMGRL 133
Cdd:COG4172 84 RELRRIRGNR---IAMIFQepmtslnplhtigkqiaeVLR----------LHRG---------LSGAAARARALELLERV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 134 ---NPnfqrfKEPVKA----LSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHD 205
Cdd:COG4172 142 gipDP-----ERRLDAyphqLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHD 216
|
250 260
....*....|....*....|....*...
gi 489631109 206 IHDVFDLADRVSVMKNGQVVGHARTEDV 233
Cdd:COG4172 217 LGVVRRFADRVAVMRQGEIVEQGPTAEL 244
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
9-225 |
1.01e-32 |
|
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: 119.26 E-value: 1.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAeinNPRDAKKYGIETI 88
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI---TNLPPHKRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 89 YQTLAVADNVDAAANLYLGRELRtpwgTLDDVAMEAKAREVMGRLNPNFQRFKEPvKALSGGQRQSVAIARAILFDARIL 168
Cdd:cd03300 78 FQNYALFPHLTVFENIAFGLRLK----KLPKAEIKERVAEALDLVQLEGYANRKP-SQLSGGQQQRVAIARALVNEPKVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489631109 169 IMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDLADRVSVMKNGQVV 225
Cdd:cd03300 153 LLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQ 210
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
10-238 |
1.92e-32 |
|
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: 118.82 E-value: 1.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 10 EMKNISISFG-GIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEpaEINNPRDAKKYG---- 84
Cdd:cd03256 2 EVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGT--DINKLKGKALRQlrrq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 85 IETIYQTLAVADNVDAAANLYLGRELRTPWG-----------------TLDDVAMEAKArevmgrlnpnFQRfkepVKAL 147
Cdd:cd03256 80 IGMIFQQFNLIERLSVLENVLSGRLGRRSTWrslfglfpkeekqralaALERVGLLDKA----------YQR----ADQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 148 SGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIfLIShdIHDVfDLA----DRVSVMKNG 222
Cdd:cd03256 146 SGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITV-IVS--LHQV-DLAreyaDRIVGLKDG 221
|
250
....*....|....*.
gi 489631109 223 QVVGHARTEDVTKDEV 238
Cdd:cd03256 222 RIVFDGPPAELTDEVL 237
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
5-237 |
2.43e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 119.33 E-value: 2.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 5 RTPLVEMKNISISFGGIH--AVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDA-K 81
Cdd:PRK13632 4 KSVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIrK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 82 KYGIetIYQTLAVAdnvdaaanlYLGRELRtpwgtlDDVA------------MEAKAREVMGRLNPNFQRFKEPVKaLSG 149
Cdd:PRK13632 84 KIGI--IFQNPDNQ---------FIGATVE------DDIAfglenkkvppkkMKDIIDDLAKKVGMEDYLDKEPQN-LSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 150 GQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKREGIG-IFLISHDIHDVFdLADRVSVMKNGQVVGHA 228
Cdd:PRK13632 146 GQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKtLISITHDMDEAI-LADKVIVFSEGKLIAQG 224
|
....*....
gi 489631109 229 RTEDVTKDE 237
Cdd:PRK13632 225 KPKEILNNK 233
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
22-237 |
3.55e-32 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 119.09 E-value: 3.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 22 HAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGE---PAEINNPRDA-KKYGI-----------E 86
Cdd:TIGR04521 19 KALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRditAKKKKKLKDLrKKVGLvfqfpehqlfeE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 87 TIYqtlavadnvdaaanlylgrelrtpwgtlDDVA------------MEAKAREVMGRLNpnfqrFKEPVK-----ALSG 149
Cdd:TIGR04521 99 TVY----------------------------KDIAfgpknlglseeeAEERVKEALELVG-----LDEEYLerspfELSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 150 GQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDLADRVSVMKNGQVVGHA 228
Cdd:TIGR04521 146 GQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEkGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDG 225
|
....*....
gi 489631109 229 RTEDVTKDE 237
Cdd:TIGR04521 226 TPREVFSDV 234
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
9-224 |
5.77e-32 |
|
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: 116.86 E-value: 5.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEpaEINNPRDA-----KKY 83
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGL--KLTDDKKNinelrQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 84 GIetIYQTLAVADNVDAAANLYLGreLRTPWGtLDDVAMEAKAREVMGRLNPNFQRFKEPVKaLSGGQRQSVAIARAILF 163
Cdd:cd03262 79 GM--VFQQFNLFPHLTVLENITLA--PIKVKG-MSKAEAEERALELLEKVGLADKADAYPAQ-LSGGQQQRVAIARALAM 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489631109 164 DARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQV 224
Cdd:cd03262 153 NPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
9-225 |
8.32e-32 |
|
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: 116.45 E-value: 8.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFGGI--HAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEpaEINNPRDAKKYGIE 86
Cdd:cd03263 1 LQIRNLTKTYKKGtkPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGY--SIRTDRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 87 ------------TIYQTLavadnvdaaanLYLGReLRTPWGTLDDVAMEAKAREVmgrlnpNFQRFKE-PVKALSGGQRQ 153
Cdd:cd03263 79 ycpqfdalfdelTVREHL-----------RFYAR-LKGLPKSEIKEEVELLLRVL------GLTDKANkRARTLSGGMKR 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489631109 154 SVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLkREGIGIFLISHDIHDVFDLADRVSVMKNGQVV 225
Cdd:cd03263 141 KLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
9-224 |
9.42e-32 |
|
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: 117.05 E-value: 9.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAeinNPRDAKKYGIETI 88
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA---TDVPVQERNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 89 YQTLAVADNVDAAANLYLGRELRTPWGTLDDVAMEAKAREVMG--RLNPNFQRFKEpvkALSGGQRQSVAIARAILFDAR 166
Cdd:cd03296 80 FQHYALFRHMTVFDNVAFGLRVKPRSERPPEAEIRAKVHELLKlvQLDWLADRYPA---QLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489631109 167 ILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDLADRVSVMKNGQV 224
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
9-225 |
2.29e-31 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 115.38 E-value: 2.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFGG--IHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDAKK-YGi 85
Cdd:cd03245 3 IEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRnIG- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 86 etiyqtlavadnvdaaanlYLGRELRTPWGTL-DDVAM---EAKAREVMG-----------RLNPN-FQR-FKEPVKALS 148
Cdd:cd03245 82 -------------------YVPQDVTLFYGTLrDNITLgapLADDERILRaaelagvtdfvNKHPNgLDLqIGERGRGLS 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489631109 149 GGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKReGIGIFLISHDIhDVFDLADRVSVMKNGQVV 225
Cdd:cd03245 143 GGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG-DKTLIIITHRP-SLLDLVDRIIVMDSGRIV 217
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
9-239 |
6.40e-31 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 120.74 E-value: 6.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFGG--IHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILING------EPAEINN---- 76
Cdd:TIGR03375 464 IEFRNVSFAYPGqeTPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGvdirqiDPADLRRnigy 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 77 -PRDAKK-YGieTIYQTLAvadnvdaaanlyLGRELrtpwgtLDDVAMeAKAREVMG-----RLNPnfQRFKEPV----K 145
Cdd:TIGR03375 544 vPQDPRLfYG--TLRDNIA------------LGAPY------ADDEEI-LRAAELAGvtefvRRHP--DGLDMQIgergR 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 146 ALSGGQRQSVAIARAILFDARILIMDEPTAALgpqETAQVGELIKQLKREGIG--IFLISHDIHdVFDLADRVSVMKNGQ 223
Cdd:TIGR03375 601 SLSGGQRQAVALARALLRDPPILLLDEPTSAM---DNRSEERFKDRLKRWLAGktLVLVTHRTS-LLDLVDRIIVMDNGR 676
|
250
....*....|....*.
gi 489631109 224 VVGharteDVTKDEVL 239
Cdd:TIGR03375 677 IVA-----DGPKDQVL 687
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
8-233 |
9.05e-31 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 114.32 E-value: 9.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 8 LVEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEP-----AEINN------ 76
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDltdskKDINKlrrkvg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 77 ---------------------PRDAKKYGIETIYQtlavadnvdaaanlyLGRELrtpwgtLDDVAMEAKARevmgrlnp 135
Cdd:COG1126 81 mvfqqfnlfphltvlenvtlaPIKVKKMSKAEAEE---------------RAMEL------LERVGLADKAD-------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 136 nfqrfKEPVKaLSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADR 215
Cdd:COG1126 132 -----AYPAQ-LSGGQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADR 205
|
250
....*....|....*...
gi 489631109 216 VSVMKNGQVVGHARTEDV 233
Cdd:COG1126 206 VVFMDGGRIVEEGPPEEF 223
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
9-225 |
1.74e-30 |
|
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: 112.73 E-value: 1.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAeinNPRDAKKYGIETI 88
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV---TDLPPKDRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 89 YQTLAVADNVDAAANLYLGRELRtpwgTLDDVAMEAKAREV--MGRLNPNFQRFkepVKALSGGQRQSVAIARAILFDAR 166
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGLKLR----KVPKDEIDERVREVaeLLQIEHLLDRK---PKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 167 ILIMDEPTAALGPQETAQV-GELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVV 225
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVQMrAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
6-239 |
2.01e-30 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 113.64 E-value: 2.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 6 TPLVEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSG-AYKRDAGEILINGEpaeinnprdakKYG 84
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVRLFGE-----------RRG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 85 IETIyqtlavadnvdaaanlylgRELRT--------------------------------PWGTLDDvAMEAKAREVMGR 132
Cdd:COG1119 70 GEDV-------------------WELRKriglvspalqlrfprdetvldvvlsgffdsigLYREPTD-EQRERARELLEL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 133 LNpnFQRFKE-PVKALSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKREG-IGIFLISHDIHDVF 210
Cdd:COG1119 130 LG--LAHLADrPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIP 207
|
250 260
....*....|....*....|....*....
gi 489631109 211 DLADRVSVMKNGQVVGHARTEDVTKDEVL 239
Cdd:COG1119 208 PGITHVLLLKDGRVVAAGPKEEVLTSENL 236
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
9-239 |
2.10e-30 |
|
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: 113.55 E-value: 2.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFGGIH-AVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNP---RDAKKYG 84
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPvelRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 85 IETIyqtlavadnvdaaaNLYLGRELRTPWGTL------DDVAMEAKAREVMG--RLNPNFQRFKEPvKALSGGQRQSVA 156
Cdd:cd03295 81 IQQI--------------GLFPHMTVEENIALVpkllkwPKEKIRERADELLAlvGLDPAEFADRYP-HELSGGQQQRVG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 157 IARAILFDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDLADRVSVMKNGQVVGHArtedvTK 235
Cdd:cd03295 146 VARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVG-----TP 220
|
....
gi 489631109 236 DEVL 239
Cdd:cd03295 221 DEIL 224
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
26-239 |
2.24e-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: 115.98 E-value: 2.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 26 DASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGE-----PAEINNPRDAKKYGIetIYQTLAVADNVDA 100
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfdsRKGIFLPPEKRRIGY--VFQEARLFPHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 101 AANLYLGRELRTPwgtLDDVAMEAKAREVMGrLNPNFQRfkePVKALSGGQRQSVAIARAILFDARILIMDEPTAALGPQ 180
Cdd:TIGR02142 93 RGNLRYGMKRARP---SERRISFERVIELLG-IGHLLGR---LPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 181 ETAQVGELIKQLKRE-GIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTEDVTKDEVL 239
Cdd:TIGR02142 166 RKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDL 225
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
9-235 |
2.65e-30 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 113.20 E-value: 2.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFGGIHaVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPrdaKKYGIETI 88
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPP---EKRDISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 89 YQTLAVADNVDAAANLYLGRELRTpwgtLDDVAMEAKAREVMGRLNPNFQRFKEPvKALSGGQRQSVAIARAILFDARIL 168
Cdd:cd03299 77 PQNYALFPHMTVYKNIAYGLKKRK----VDKKEIERKVLEIAEMLGIDHLLNRKP-ETLSGGEQQRVAIARALVVNPKIL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489631109 169 IMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTEDVTK 235
Cdd:cd03299 152 LLDEPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFK 219
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
9-227 |
3.86e-30 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 112.80 E-value: 3.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDAKKygieti 88
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKPSEKA------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 89 yqtlavadnvdaaanlylGRELRTPWG------------TLDDVAMEA--------------KAREVMGRLN-PNF-QRF 140
Cdd:COG4161 77 ------------------IRLLRQKVGmvfqqynlwphlTVMENLIEApckvlglskeqareKAMKLLARLRlTDKaDRF 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 141 kePVkALSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMK 220
Cdd:COG4161 139 --PL-HLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYME 215
|
....*..
gi 489631109 221 NGQVVGH 227
Cdd:COG4161 216 KGRIIEQ 222
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
9-229 |
4.19e-30 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 112.07 E-value: 4.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISF-GGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEpaeinNPRDAKKYGIet 87
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQ-----DLSRLKRREI-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 88 iyqtlavadnvdaaanLYLGREL------------RTpwgTLDDVA------------MEAKAREVMGRLNPNFQRFKEP 143
Cdd:COG2884 75 ----------------PYLRRRIgvvfqdfrllpdRT---VYENVAlplrvtgksrkeIRRRVREVLDLVGLSDKAKALP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 144 VkALSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQ 223
Cdd:COG2884 136 H-ELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGR 214
|
....*.
gi 489631109 224 VVGHAR 229
Cdd:COG2884 215 LVRDEA 220
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
7-245 |
9.05e-30 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 116.28 E-value: 9.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 7 PLVEMKNISI-SFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDAKKYGI 85
Cdd:COG3845 256 VVLEVENLSVrDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGV 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 86 E---------------TIYQTLAvadnvdaaanlyLGRELRTP---WGTLDDVAMEAKAREVMGRLNPNFQRFKEPVKAL 147
Cdd:COG3845 336 AyipedrlgrglvpdmSVAENLI------------LGRYRRPPfsrGGFLDRKAIRAFAEELIEEFDVRTPGPDTPARSL 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 148 SGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVVGH 227
Cdd:COG3845 404 SGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGE 483
|
250
....*....|....*...
gi 489631109 228 ARTEDVTKDEvLGMIIMG 245
Cdd:COG3845 484 VPAAEATREE-IGLLMAG 500
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
9-241 |
9.70e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 112.10 E-value: 9.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISF--GGI---HAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEpaEINNPRDAKKY 83
Cdd:COG1101 2 LELKNLSKTFnpGTVnekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGK--DVTKLPEYKRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 84 GietiyqtlavadnvdaaanlYLGRELRTPW-GT------LDDVAMeAKARE-----VMGRLNPNFQRFKE--------- 142
Cdd:COG1101 80 K--------------------YIGRVFQDPMmGTapsmtiEENLAL-AYRRGkrrglRRGLTKKRRELFREllatlglgl 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 143 ------PVKALSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQL-KREGIGIFLISHDIHDVFDLADR 215
Cdd:COG1101 139 enrldtKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHNMEQALDYGNR 218
|
250 260
....*....|....*....|....*....
gi 489631109 216 VSVMKNGQVVGHARTED---VTKDEVLGM 241
Cdd:COG1101 219 LIMMHEGRIILDVSGEEkkkLTVEDLLEL 247
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
9-227 |
2.63e-29 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 110.49 E-value: 2.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDAKKygieti 88
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSDKA------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 89 yqtlavadnvdaaanlylGRELRTPWGT--------------------------LDDVAMEAKAREVMGRL--NPNFQRF 140
Cdd:PRK11124 77 ------------------IRELRRNVGMvfqqynlwphltvqqnlieapcrvlgLSKDQALARAEKLLERLrlKPYADRF 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 141 kePVKaLSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMK 220
Cdd:PRK11124 139 --PLH-LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYME 215
|
....*..
gi 489631109 221 NGQVVGH 227
Cdd:PRK11124 216 NGHIVEQ 222
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
9-225 |
3.82e-29 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 112.47 E-value: 3.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEpaEINNpRDAKKYGIETI 88
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGR--DVTD-LPPKDRNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 89 YQTLAvadnvdaaanLY----------LGRELRTpwgtLDDVAMEAKAREVMGRLN--PNFQRFkepVKALSGGQRQSVA 156
Cdd:COG3839 81 FQSYA----------LYphmtvyeniaFPLKLRK----VPKAEIDRRVREAAELLGleDLLDRK---PKQLSGGQRQRVA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 157 IARAILFDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDLADRVSVMKNGQVV 225
Cdd:COG3839 144 LGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRlGTTTIYVTHDQVEAMTLADRIAVMNDGRIQ 213
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
7-239 |
7.07e-29 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 109.86 E-value: 7.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 7 PLVEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRD-AKKYGI 85
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 86 ETIYQTLAVAdnvdaaanlYLGREL----RTPWGTLDDVAMEAkAREVM---------GRLNPnfqrfkepvkALSGGQR 152
Cdd:PRK13548 81 LPQHSSLSFP---------FTVEEVvamgRAPHGLSRAEDDAL-VAAALaqvdlahlaGRDYP----------QLSGGEQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 153 QSVAIARAIL------FDARILIMDEPTAALGPQETAQVGELIKQL-KREGIGIFLISHDIhdvfDLA----DRVSVMKN 221
Cdd:PRK13548 141 QRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDL----NLAaryaDRIVLLHQ 216
|
250
....*....|....*...
gi 489631109 222 GQVVGHARTEDVTKDEVL 239
Cdd:PRK13548 217 GRLVADGTPAEVLTPETL 234
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
9-238 |
7.07e-29 |
|
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: 109.17 E-value: 7.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEpaEINN-PRDAK-KYGIE 86
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQ--DITKlPMHKRaRLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 87 TIYQTLAVADNVDAAANLYLGRELRTpwgtLDDVAMEAKAREVMGRLNPNFQRfKEPVKALSGGQRQSVAIARAILFDAR 166
Cdd:cd03218 79 YLPQEASIFRKLTVEENILAVLEIRG----LSKKEREEKLEELLEEFHITHLR-KSKASSLSGGERRRVEIARALATNPK 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489631109 167 ILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTEDVTKDEV 238
Cdd:cd03218 154 FLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
6-235 |
9.05e-29 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 109.40 E-value: 9.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 6 TPLVEMKNISISF----------------------GGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAG 63
Cdd:COG1134 2 SSMIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 64 EILINGEPA---EIN---NPRDAkkyGIETIYqtlavadnvdaAANLYLGrelrtpwgtLDDVAMEAKAREV-----MGR 132
Cdd:COG1134 82 RVEVNGRVSallELGagfHPELT---GRENIY-----------LNGRLLG---------LSRKEIDEKFDEIvefaeLGD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 133 lnpnFqrFKEPVKALSGGQRQSVAIARAILFDARILIMDEptaALGpqetaqVG---------ELIKQLKREGIGIFLIS 203
Cdd:COG1134 139 ----F--IDQPVKTYSSGMRARLAFAVATAVDPDILLVDE---VLA------VGdaafqkkclARIRELRESGRTVIFVS 203
|
250 260 270
....*....|....*....|....*....|..
gi 489631109 204 HDIHDVFDLADRVSVMKNGQVVGHARTEDVTK 235
Cdd:COG1134 204 HSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIA 235
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
23-225 |
9.94e-29 |
|
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: 109.66 E-value: 9.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 23 AVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEP-AEINNP--RDAKKYGIETIYQTLAVADNVD 99
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDiAAMSRKelRELRRKKISMVFQSFALLPHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 100 AAANLYLGRELRTpwgtLDDVAMEAKAREVMGRLNPNFQRFKEPvKALSGGQRQSVAIARAILFDARILIMDEPTAALGP 179
Cdd:cd03294 119 VLENVAFGLEVQG----VPRAEREERAAEALELVGLEGWEHKYP-DELSGGMQQRVGLARALAVDPDILLMDEAFSALDP 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489631109 180 QETAQVGELIKQLKRE-GIGIFLISHDIHDVFDLADRVSVMKNGQVV 225
Cdd:cd03294 194 LIRREMQDELLRLQAElQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
24-239 |
1.26e-28 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 113.17 E-value: 1.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 24 VDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDAKKYGIETIYQTlavadnvDAAAN 103
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANGIVYISED-------RKRDG 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 104 LYLG------------RELRTPWGTLDDVAMEAKAREVMGRLNPNFQRFKEPVKALSGGQRQSVAIARAILFDARILIMD 171
Cdd:PRK10762 341 LVLGmsvkenmsltalRYFSRAGGSLKHADEQQAVSDFIRLFNIKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILD 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489631109 172 EPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTEDVTKDEVL 239
Cdd:PRK10762 421 EPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTREQATQEKLM 488
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-237 |
1.53e-28 |
|
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: 113.32 E-value: 1.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 4 QRTPLVEMKNISISF--GGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDAK 81
Cdd:COG4987 329 PGGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 82 KY-GI---------ETIYQTLAvadnvdaaanlyLGRElrtpwgTLDDVAMEAKAREVmgRLNPNFQRFKE----PV--- 144
Cdd:COG4987 409 RRiAVvpqrphlfdTTLRENLR------------LARP------DATDEELWAALERV--GLGDWLAALPDgldtWLgeg 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 145 -KALSGGQRQSVAIARAILFDARILIMDEPTAALGPqETAQvgELIKQLKREGIG--IFLISHDIHDVfDLADRVSVMKN 221
Cdd:COG4987 469 gRRLSGGERRRLALARALLRDAPILLLDEPTEGLDA-ATEQ--ALLADLLEALAGrtVLLITHRLAGL-ERMDRILVLED 544
|
250
....*....|....*.
gi 489631109 222 GQVVGHARTEDVTKDE 237
Cdd:COG4987 545 GRIVEQGTHEELLAQN 560
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-233 |
1.70e-28 |
|
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: 113.24 E-value: 1.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 3 EQRTPLVEMKNISISF-----------GGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYkRDAGEILINGEP 71
Cdd:COG4172 270 PDAPPLLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQD 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 72 AEINNPRDAKK------------YG-------IETIyqtlavadnvdaaanlyLGRELRTPWGTLDDVAMEAKAREVMGR 132
Cdd:COG4172 349 LDGLSRRALRPlrrrmqvvfqdpFGslsprmtVGQI-----------------IAEGLRVHGPGLSAAERRARVAEALEE 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 133 --LNPNFqRFKEPvKALSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDV 209
Cdd:COG4172 412 vgLDPAA-RHRYP-HEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHDLAVV 489
|
250 260
....*....|....*....|....
gi 489631109 210 FDLADRVSVMKNGQVVGHARTEDV 233
Cdd:COG4172 490 RALAHRVMVMKDGKVVEQGPTEQV 513
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-233 |
2.22e-28 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 111.08 E-value: 2.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 6 TPLVEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRdakKYGI 85
Cdd:PRK11607 17 TPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPY---QRPI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 86 ETIYQTLAVADNVDAAANLYLG-RELRTPWGTLDDvameaKAREVMGRLnpNFQRF-KEPVKALSGGQRQSVAIARAILF 163
Cdd:PRK11607 94 NMMFQSYALFPHMTVEQNIAFGlKQDKLPKAEIAS-----RVNEMLGLV--HMQEFaKRKPHQLSGGQRQRVALARSLAK 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489631109 164 DARILIMDEPTAALGPQ--ETAQVgELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTEDV 233
Cdd:PRK11607 167 RPKLLLLDEPMGALDKKlrDRMQL-EVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
23-225 |
7.12e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 107.83 E-value: 7.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 23 AVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILING-----EPAEINNPRdaKKYGI-----------E 86
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdKKVKLSDIR--KKVGLvfqypeyqlfeE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 87 TIYQTLAVADNVdaaanlyLGrelrtpwgtLDDVAMEAKAREVMGRLNPNFQRFKE--PVKaLSGGQRQSVAIARAILFD 164
Cdd:PRK13637 100 TIEKDIAFGPIN-------LG---------LSEEEIENRVKRAMNIVGLDYEDYKDksPFE-LSGGQKRRVAIAGVVAME 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489631109 165 ARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDLADRVSVMKNGQVV 225
Cdd:PRK13637 163 PKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCE 224
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
28-233 |
7.79e-28 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 107.40 E-value: 7.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 28 SVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAeinnprDAKKYGIETIYQTLAVADNVDAAANLYLG 107
Cdd:PRK13638 21 NLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL------DYSKRGLLALRQQVATVFQDPEQQIFYTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 108 RELRTPWGTLD-DVAMEAKAREVMGRLN-PNFQRFK-EPVKALSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQ 184
Cdd:PRK13638 95 IDSDIAFSLRNlGVPEAEITRRVDEALTlVDAQHFRhQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489631109 185 VGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTEDV 233
Cdd:PRK13638 175 MIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEV 223
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
12-233 |
8.56e-28 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 109.08 E-value: 8.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 12 KNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINnpRDAKKYGIE----- 86
Cdd:COG1118 6 RNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTN--LPPRERRVGfvfqh 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 87 -------TIYQTLAvadnvdaaanlyLGRELRTPwgtlDDVAMEAKAREVMGRLN-PNF-QRFkePvKALSGGQRQSVAI 157
Cdd:COG1118 84 yalfphmTVAENIA------------FGLRVRPP----SKAEIRARVEELLELVQlEGLaDRY--P-SQLSGGQRQRVAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 158 ARAILFDARILIMDEPTAALgpqeTAQV-----GELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTED 232
Cdd:COG1118 145 ARALAVEPEVLLLDEPFGAL----DAKVrkelrRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDE 220
|
.
gi 489631109 233 V 233
Cdd:COG1118 221 V 221
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
20-239 |
1.18e-27 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 110.40 E-value: 1.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 20 GIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYK-RDAGEILINGEPAEINNPRDA------------KKYGIE 86
Cdd:PRK13549 274 HIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQQAiaqgiamvpedrKRDGIV 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 87 TIYQ-----TLAVadnvdaaanlyLGRelRTPWGTLDDVAMEAKAREVMGRLNPNFQRFKEPVKALSGGQRQSVAIARAI 161
Cdd:PRK13549 354 PVMGvgkniTLAA-----------LDR--FTGGSRIDDAAELKTILESIQRLKVKTASPELAIARLSGGNQQKAVLAKCL 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489631109 162 LFDARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTEDVTKDEVL 239
Cdd:PRK13549 421 LLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLKGDLINHNLTQEQVM 498
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
8-239 |
1.41e-27 |
|
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: 106.23 E-value: 1.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 8 LVEMKNISISFG-GIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEpaEINNPRDAK----K 82
Cdd:TIGR02315 1 MLEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGT--DITKLRGKKlrklR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 83 YGIETIYQTLAVADNVDAAANLYLGR-----ELRTPWGTLDD----VAMEAKARevMGRLNPNFQRfkepVKALSGGQRQ 153
Cdd:TIGR02315 79 RRIGMIFQHYNLIERLTVLENVLHGRlgykpTWRSLLGRFSEedkeRALSALER--VGLADKAYQR----ADQLSGGQQQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 154 SVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTED 232
Cdd:TIGR02315 153 RVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSE 232
|
....*..
gi 489631109 233 VTkDEVL 239
Cdd:TIGR02315 233 LD-DEVL 238
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
9-239 |
1.81e-27 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 105.39 E-value: 1.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISF-GGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPaeINN-PRDAKKYGIE 86
Cdd:cd03254 3 IEFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGID--IRDiSRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 87 TIYQtlavadnvdaAANLYLG--RE---LRTPWGTLDDVAMEAKA----REVMGRLNPNFQRFKEPVKALSGGQRQSVAI 157
Cdd:cd03254 81 VVLQ----------DTFLFSGtiMEnirLGRPNATDEEVIEAAKEagahDFIMKLPNGYDTVLGENGGNLSQGERQLLAI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 158 ARAILFDARILIMDEPTAALGPQETAQVGELIKQLkREGIGIFLISHDIHDVFDlADRVSVMKNGQVVghartEDVTKDE 237
Cdd:cd03254 151 ARAMLRDPKILILDEATSNIDTETEKLIQEALEKL-MKGRTSIIIAHRLSTIKN-ADKILVLDDGKII-----EEGTHDE 223
|
..
gi 489631109 238 VL 239
Cdd:cd03254 224 LL 225
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
8-232 |
2.55e-27 |
|
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: 110.19 E-value: 2.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 8 LVEMKNISISFGG--IHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDAKKYgI 85
Cdd:TIGR02203 330 DVEFRNVTFRYPGrdRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQ-V 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 86 ETIYQTLAVADNVDAAANLYlGRELRTPWGTLDDVAMEAKAREVMGRLnPNFQRFKEPVKA--LSGGQRQSVAIARAILF 163
Cdd:TIGR02203 409 ALVSQDVVLFNDTIANNIAY-GRTEQADRAEIERALAAAYAQDFVDKL-PLGLDTPIGENGvlLSGGQRQRLAIARALLK 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489631109 164 DARILIMDEPTAALGPQETAQVGELIKQLKREGIGIfLISHDIHDVfDLADRVSVMKNGQVVGHARTED 232
Cdd:TIGR02203 487 DAPILILDEATSALDNESERLVQAALERLMQGRTTL-VIAHRLSTI-EKADRIVVMDDGRIVERGTHNE 553
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
26-233 |
2.75e-27 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 107.88 E-value: 2.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 26 DASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEP-----AEINNPRDAKKYGI----------ETIYQ 90
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlqdsaRGIFLPPHRRRIGYvfqearlfphLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 91 TLavadnvdaaanLYlGRElRTPWG----TLDDVAmeakarEVMGrLNPNFQRFkepVKALSGGQRQSVAIARAILFDAR 166
Cdd:COG4148 97 NL-----------LY-GRK-RAPRAerriSFDEVV------ELLG-IGHLLDRR---PATLSGGERQRVAIGRALLSSPR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489631109 167 ILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTEDV 233
Cdd:COG4148 154 LLLMDEPLAALDLARKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEV 221
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
9-226 |
3.27e-27 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 109.87 E-value: 3.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISF-GGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGepaeinnpRDAKKYGIE- 86
Cdd:COG1132 340 IEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDG--------VDIRDLTLEs 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 87 -----------------TIYQTLAvadnvdaaanlyLGRelrtPWGTLDDV---AMEAKAREVMGRLnPnfQRFKEPV-- 144
Cdd:COG1132 412 lrrqigvvpqdtflfsgTIRENIR------------YGR----PDATDEEVeeaAKAAQAHEFIEAL-P--DGYDTVVge 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 145 --KALSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLkREGIGIFLISHDIHDVFDlADRVSVMKNG 222
Cdd:COG1132 473 rgVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERL-MKGRTTIVIAHRLSTIRN-ADRILVLDDG 550
|
....
gi 489631109 223 QVVG 226
Cdd:COG1132 551 RIVE 554
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
7-225 |
3.51e-27 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 105.87 E-value: 3.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 7 PLVEMKNISISFGGI--HAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDA-KKY 83
Cdd:PRK13635 4 EIIRVEHISFRYPDAatYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVrRQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 84 GIetIYQTLAVAdnvdaaanlYLGRELRtpwgtlDDVA------------MEAKAREVMGRLnpNFQRF--KEPVKaLSG 149
Cdd:PRK13635 84 GM--VFQNPDNQ---------FVGATVQ------DDVAfglenigvpreeMVERVDQALRQV--GMEDFlnREPHR-LSG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489631109 150 GQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDlADRVSVMKNGQVV 225
Cdd:PRK13635 144 GQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQkGITVLSITHDLDEAAQ-ADRVIVMNKGEIL 219
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
12-246 |
5.94e-27 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 104.59 E-value: 5.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 12 KNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDAKKYGIETIYQT 91
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 92 LAVADNVDAAANLYLGRELRtpwgtlDDVAMEA---KAREVMGRLNPNFQRfKEPVKALSGGQRQSVAIARAILFDARIL 168
Cdd:PRK10895 87 ASIFRRLSVYDNLMAVLQIR------DDLSAEQredRANELMEEFHIEHLR-DSMGQSLSGGERRRVEIARALAANPKFI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489631109 169 IMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTEDVTKDEVLGMIIMGK 246
Cdd:PRK10895 160 LLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYLGE 237
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1-255 |
7.26e-27 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 106.33 E-value: 7.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 1 MTEQRTPLVEMKNISISFG-------------GIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILI 67
Cdd:PRK15079 1 VTEGKKVLLEVADLKVHFDikdgkqwfwqppkTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 68 NGEP--AEINNPRDAKKYGIETIYQTLAVADNVDAAANLYLGRELRTPWGTLDDVAMEAKAREVMGR--LNPNF-QRFKE 142
Cdd:PRK15079 81 LGKDllGMKDDEWRAVRSDIQMIFQDPLASLNPRMTIGEIIAEPLRTYHPKLSRQEVKDRVKAMMLKvgLLPNLiNRYPH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 143 pvkALSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDLADRVSVMkn 221
Cdd:PRK15079 161 ---EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVM-- 235
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 489631109 222 gqVVGHArTEDVTKDEVLG-------MIIMGKVPpkaIPGP 255
Cdd:PRK15079 236 --YLGHA-VELGTYDEVYHnplhpytKALMSAVP---IPDP 270
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
21-239 |
8.28e-27 |
|
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: 108.37 E-value: 8.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 21 IHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYK-RDAGEILINGEPAEINNPRDAKKYGIETIYQTlavADNVD 99
Cdd:TIGR02633 273 RKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKPVDIRNPAQAIRAGIAMVPED---RKRHG 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 100 AAANLYLGRELR-------TPWGTLDDVAMEAKAREVMGRLNPNFQRFKEPVKALSGGQRQSVAIARAILFDARILIMDE 172
Cdd:TIGR02633 350 IVPILGVGKNITlsvlksfCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDE 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489631109 173 PTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTEDVTKDEVL 239
Cdd:TIGR02633 430 PTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGDFVNHALTQEQVL 496
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
8-237 |
9.79e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 104.77 E-value: 9.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 8 LVEMKNISISF-GGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNP---RDAKKY 83
Cdd:PRK13639 1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKsllEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 84 GIetIYQTLAVadnvdaaanlylgrELRTPwGTLDDVA-----MEAKAREVMGRLNPNFQRF------KEPVKALSGGQR 152
Cdd:PRK13639 81 GI--VFQNPDD--------------QLFAP-TVEEDVAfgplnLGLSKEEVEKRVKEALKAVgmegfeNKPPHHLSGGQK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 153 QSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTED 232
Cdd:PRK13639 144 KRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKE 223
|
....*
gi 489631109 233 VTKDE 237
Cdd:PRK13639 224 VFSDI 228
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
12-237 |
1.03e-26 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 103.68 E-value: 1.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 12 KNISISFGGIHAVDDASVDlyPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGE------PAEI--------NN- 76
Cdd:COG3840 5 DDLTYRYGDFPLRFDLTIA--AGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQdltalpPAERpvsmlfqeNNl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 77 -PRdakkygiETIYQTLavadnvdaaanlYLGreLRtPWGTLDDvAMEAKAREVMGR--LNPNFQRFKEpvkALSGGQRQ 153
Cdd:COG3840 83 fPH-------LTVAQNI------------GLG--LR-PGLKLTA-EQRAQVEQALERvgLAGLLDRLPG---QLSGGQRQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 154 SVAIARAILFDARILIMDEPTAALGP---QETAQvgeLIKQLKRE-GIGIFLISHDIHDVFDLADRVSVMKNGQVVGHAR 229
Cdd:COG3840 137 RVALARCLVRKRPILLLDEPFSALDPalrQEMLD---LVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAADGP 213
|
....*...
gi 489631109 230 TEDVTKDE 237
Cdd:COG3840 214 TAALLDGE 221
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-224 |
1.07e-26 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 106.57 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 4 QRTPLVEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEpaEINN-PrdAKK 82
Cdd:PRK09452 10 SLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQ--DITHvP--AEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 83 YGIETIYQTLAVADNVDAAANLYLG-RELRTPWGTLDDVAMEAKArevMGRLNPNFQRfkePVKALSGGQRQSVAIARAI 161
Cdd:PRK09452 86 RHVNTVFQSYALFPHMTVFENVAFGlRMQKTPAAEITPRVMEALR---MVQLEEFAQR---KPHQLSGGQQQRVAIARAV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489631109 162 LFDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDLADRVSVMKNGQV 224
Cdd:PRK09452 160 VNKPKVLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRI 223
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
19-225 |
1.30e-26 |
|
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: 103.00 E-value: 1.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 19 GGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPA---EINNPRDAKKYGIETIYqtlava 95
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSsllGLGGGFNPELTGRENIY------ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 96 dnvdaaanlYLGRELRtpwgtLDDVAMEAKAREVMGrlnpnF----QRFKEPVKALSGGQRQSVAIARAILFDARILIMD 171
Cdd:cd03220 107 ---------LNGRLLG-----LSRKEIDEKIDEIIE-----FselgDFIDLPVKTYSSGMKARLAFAIATALEPDILLID 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489631109 172 EPTAA--LGPQETAQvgELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVV 225
Cdd:cd03220 168 EVLAVgdAAFQEKCQ--RRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIR 221
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
12-239 |
2.04e-26 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 103.17 E-value: 2.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 12 KNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDAKKYgIETIYQT 91
Cdd:PRK11231 6 ENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARR-LALLPQH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 92 LAVADNVDAaanlylgREL----RTPWGTL------DDVAMEAKAREVMGRLnpnfQRFKEPVKALSGGQRQSVAIARAI 161
Cdd:PRK11231 85 HLTPEGITV-------RELvaygRSPWLSLwgrlsaEDNARVNQAMEQTRIN----HLADRRLTDLSGGQRQRAFLAMVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489631109 162 LFDARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTEDVTKDEVL 239
Cdd:PRK11231 154 AQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLL 231
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
7-239 |
2.95e-26 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 105.69 E-value: 2.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 7 PLVEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDAKKYgIE 86
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRR-VA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 87 TIYQTLAVADNVDAAANLYLGRELRT----PWGTLDDVAMEakarEVMGRLNPNfQRFKEPVKALSGGQRQSVAIARAIL 162
Cdd:PRK09536 81 SVPQDTSLSFEFDVRQVVEMGRTPHRsrfdTWTETDRAAVE----RAMERTGVA-QFADRPVTSLSGGERQRVLLARALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 163 FDARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIhdvfDLA----DRVSVMKNGQVVGHARTEDVTKDEV 238
Cdd:PRK09536 156 QATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDL----DLAarycDELVLLADGRVRAAGPPADVLTADT 231
|
.
gi 489631109 239 L 239
Cdd:PRK09536 232 L 232
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
6-236 |
3.33e-26 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 102.70 E-value: 3.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 6 TPLVEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILI---NGEPAEINNPRDAKK 82
Cdd:PRK11701 4 QPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRDLYALSEAER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 83 YgietiyqtlavadnvdaaanlylgRELRTPWG-----TLDDVAME-----------------------AKAREVMGRLN 134
Cdd:PRK11701 84 R------------------------RLLRTEWGfvhqhPRDGLRMQvsaggnigerlmavgarhygdirATAGDWLERVE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 135 PNFQRFKEPVKALSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDLA 213
Cdd:PRK11701 140 IDAARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLA 219
|
250 260
....*....|....*....|...
gi 489631109 214 DRVSVMKNGQVVGHARTEDVTKD 236
Cdd:PRK11701 220 HRLLVMKQGRVVESGLTDQVLDD 242
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-233 |
4.00e-26 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 106.33 E-value: 4.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 1 MTEQRTPLVEMKNISISF---GGI--------HAVDDASVDLYPGEVVALLGHNGAGKST----LIKILsgaykRDAGEI 65
Cdd:PRK15134 268 LPEPASPLLDVEQLQVAFpirKGIlkrtvdhnVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEI 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 66 LINGEPAEINNPRDAKKY--GIETIYQTLAVADNVDAAANLYLGRELRTPWGTLDDVAMEAKAREVMGR--LNPNfQRFK 141
Cdd:PRK15134 343 WFDGQPLHNLNRRQLLPVrhRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPTLSAAQREQQVIAVMEEvgLDPE-TRHR 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 142 EPvKALSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLK-REGIGIFLISHDIHDVFDLADRVSVMK 220
Cdd:PRK15134 422 YP-AEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQqKHQLAYLFISHDLHVVRALCHQVIVLR 500
|
250
....*....|...
gi 489631109 221 NGQVVGHARTEDV 233
Cdd:PRK15134 501 QGEVVEQGDCERV 513
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
9-233 |
4.22e-26 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 104.11 E-value: 4.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFGG----IHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGE------PAEInnpR 78
Cdd:PRK11153 2 IELKNISKVFPQggrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQdltalsEKEL---R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 79 DAKKyGIETIYQtlavadnvdaaaNLYLgreL--RTpwgTLDDVAM------EAKArEVMGRLNPNFQRFKEPVKA---- 146
Cdd:PRK11153 79 KARR-QIGMIFQ------------HFNL---LssRT---VFDNVALplelagTPKA-EIKARVTELLELVGLSDKAdryp 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 147 --LSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDLADRVSVMKNGQ 223
Cdd:PRK11153 139 aqLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGR 218
|
250
....*....|
gi 489631109 224 VVGHARTEDV 233
Cdd:PRK11153 219 LVEQGTVSEV 228
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
8-225 |
6.21e-26 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 106.20 E-value: 6.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 8 LVEMKNISISFGGI-HAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEpaeinNPRDAKKYG-- 84
Cdd:PRK13657 334 AVEFDDVSFSYDNSrQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGT-----DIRTVTRASlr 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 85 --IETIYQTlAVADNVDAAANLYLGRELRTPwGTLDDVAMEAKAREVMGRLNPNFQ-RFKEPVKALSGGQRQSVAIARAI 161
Cdd:PRK13657 409 rnIAVVFQD-AGLFNRSIEDNIRVGRPDATD-EEMRAAAERAQAHDFIERKPDGYDtVVGERGRQLSGGERQRLAIARAL 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489631109 162 LFDARILIMDEPTAALGPQETAQVGELIKQLkREGIGIFLISHDIHDVFDlADRVSVMKNGQVV 225
Cdd:PRK13657 487 LKDPPILILDEATSALDVETEAKVKAALDEL-MKGRTTFIIAHRLSTVRN-ADRILVFDNGRVV 548
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
12-237 |
1.08e-25 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 100.87 E-value: 1.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 12 KNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEpaEINN-P--RDAKKyGI--- 85
Cdd:COG1137 7 ENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGE--DITHlPmhKRARL-GIgyl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 86 --E-------TIYQTlavadnvdaaanLYLGRELRtpwgTLDDVAMEAKAREVMGRLNPNFQRfKEPVKALSGGQRQSVA 156
Cdd:COG1137 84 pqEasifrklTVEDN------------ILAVLELR----KLSKKEREERLEELLEEFGITHLR-KSKAYSLSGGERRRVE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 157 IARAILFDARILIMDEPTAALGPQETAQVGELIKQLKREGIGIfLIS-HDIHDVFDLADRVSVMKNGQVVGHARTEDVTK 235
Cdd:COG1137 147 IARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGV-LITdHNVRETLGICDRAYIISEGKVLAEGTPEEILN 225
|
..
gi 489631109 236 DE 237
Cdd:COG1137 226 NP 227
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
9-225 |
1.11e-25 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 99.31 E-value: 1.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFGG--IHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEInnprdakkygie 86
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSD------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 87 tiyqtlavadnvdaaanlyLGRELRTPWGTLDDVA--MEAKAREVMGRlnpnfqRFkepvkalSGGQRQSVAIARAILFD 164
Cdd:cd03247 69 -------------------LEKALSSLISVLNQRPylFDTTLRNNLGR------RF-------SGGERQRLALARILLQD 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489631109 165 ARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFlISHDIHDVfDLADRVSVMKNGQVV 225
Cdd:cd03247 117 APIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIW-ITHHLTGI-EHMDKILFLENGKII 175
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
11-205 |
1.68e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 104.38 E-value: 1.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 11 MKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILING---------EP---------- 71
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglrigylpqEPpldddltvld 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 72 --AEINNPRDAKKYGIETIYQTLAVADNVDAAANlylgrELRTPWGTLDDVAMEAKAREVMGRLNPNFQRFKEPVKALSG 149
Cdd:COG0488 81 tvLDGDAELRALEAELEELEAKLAEPDEDLERLA-----ELQEEFEALGGWEAEARAEEILSGLGFPEEDLDRPVSELSG 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 150 GQRQSVAIARAILFDARILIMDEPT----AalgpqETaqVGELIKQLKREGIGIFLISHD 205
Cdd:COG0488 156 GWRRRVALARALLSEPDLLLLDEPTnhldL-----ES--IEWLEEFLKNYPGTVLVVSHD 208
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
27-239 |
1.75e-25 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 104.22 E-value: 1.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 27 ASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDAKKYGI---------ETIYQTLAVADN 97
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGImlcpedrkaEGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 98 VDAAAnlylgRELRTPWGTLDDVAMEAK-AREVMGRLNPNFQRFKEPVKALSGGQRQSVAIARAILFDARILIMDEPTAA 176
Cdd:PRK11288 352 INISA-----RRHHLRAGCLINNRWEAEnADRFIRSLNIKTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRG 426
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489631109 177 LGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTEDVTKDEVL 239
Cdd:PRK11288 427 IDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGELAREQATERQAL 489
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
6-230 |
2.08e-25 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 104.40 E-value: 2.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 6 TPLVEMKNISISF--GGI--HAVDDASVDLYPGEVVALLGHNGAGKS-TLIKIL----SGAYKRDAGEILINGEP---AE 73
Cdd:PRK15134 3 QPLLAIENLSVAFrqQQTvrTVVNDVSLQIEAGETLALVGESGSGKSvTALSILrllpSPPVVYPSGDIRFHGESllhAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 74 INNPRDAKKYGIETIYQ----------TLAVADNVDaaanLYLGRELRTP------WGTLDDVAMeakaREVMGRLN--P 135
Cdd:PRK15134 83 EQTLRGVRGNKIAMIFQepmvslnplhTLEKQLYEV----LSLHRGMRREaargeiLNCLDRVGI----RQAAKRLTdyP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 136 NfqrfkepvkALSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDLAD 214
Cdd:PRK15134 155 H---------QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLAD 225
|
250
....*....|....*.
gi 489631109 215 RVSVMKNGQVVGHART 230
Cdd:PRK15134 226 RVAVMQNGRCVEQNRA 241
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
7-225 |
3.20e-25 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 99.95 E-value: 3.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 7 PLVEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEpaEINNPRDAK--KYG 84
Cdd:PRK11614 4 VMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGK--DITDWQTAKimREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 85 IETIYQtlavadnvdaaanlylGRELRTPWGTLDDVAM----------EAKAREVMGRLNPNFQRFKEPVKALSGGQRQS 154
Cdd:PRK11614 82 VAIVPE----------------GRRVFSRMTVEENLAMggffaerdqfQERIKWVYELFPRLHERRIQRAGTMSGGEQQM 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489631109 155 VAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVV 225
Cdd:PRK11614 146 LAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
2-232 |
3.62e-25 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 104.26 E-value: 3.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 2 TEQRTPL---VEMKNISISFGGIHA--VDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEP-AEIn 75
Cdd:TIGR03796 468 SEPPRRLsgyVELRNITFGYSPLEPplIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPrEEI- 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 76 nPRDAKKYGIETIYQTLAvadnvdaaanLYLG--RELRTPW-GTLDDVAMEAKAR------EVMGRLNPNFQRFKEPVKA 146
Cdd:TIGR03796 547 -PREVLANSVAMVDQDIF----------LFEGtvRDNLTLWdPTIPDADLVRACKdaaihdVITSRPGGYDAELAEGGAN 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 147 LSGGQRQSVAIARAILFDARILIMDEPTAALGPqETAQVgeLIKQLKREGIGIFLISHDIHDVFDlADRVSVMKNGQVVG 226
Cdd:TIGR03796 616 LSGGQRQRLEIARALVRNPSILILDEATSALDP-ETEKI--IDDNLRRRGCTCIIVAHRLSTIRD-CDEIIVLERGKVVQ 691
|
....*.
gi 489631109 227 HARTED 232
Cdd:TIGR03796 692 RGTHEE 697
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
10-219 |
4.94e-25 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 99.94 E-value: 4.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 10 EMKNISISFGG----IHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPaeINNPrDAKKyGI 85
Cdd:COG4525 5 TVRHVSVRYPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVP--VTGP-GADR-GV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 86 etIYQ--TLAvadnvdaaanlylgrelrtPWGT-LDDVAM------------EAKAREVMGRLN-PNFQRfkEPVKALSG 149
Cdd:COG4525 81 --VFQkdALL-------------------PWLNvLDNVAFglrlrgvpkaerRARAEELLALVGlADFAR--RRIWQLSG 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489631109 150 GQRQSVAIARAILFDARILIMDEPTAALGP--QETAQvgELIKQL-KREGIGIFLISHDIHDVFDLADRVSVM 219
Cdd:COG4525 138 GMRQRVGIARALAADPRFLLMDEPFGALDAltREQMQ--ELLLDVwQRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-233 |
6.71e-25 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 99.34 E-value: 6.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 1 MTEQRT---PLVEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKIL-------SGAykRDAGEILINGE 70
Cdd:COG1117 1 MTAPAStlePKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndliPGA--RVEGEILLDGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 71 paEINNPR-DA----KKYGI---------ETIYQTLavadnvdaaanLYLGR--ELRTPwGTLDDVAMEA--KAR---EV 129
Cdd:COG1117 79 --DIYDPDvDVvelrRRVGMvfqkpnpfpKSIYDNV-----------AYGLRlhGIKSK-SELDEIVEESlrKAAlwdEV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 130 MGRLnpnfqrfKEPVKALSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKREgIGIFLISHDIHDV 209
Cdd:COG1117 145 KDRL-------KKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQA 216
|
250 260
....*....|....*....|....
gi 489631109 210 FDLADRVSVMKNGQVVGHARTEDV 233
Cdd:COG1117 217 ARVSDYTAFFYLGELVEFGPTEQI 240
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
21-225 |
1.04e-24 |
|
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: 98.17 E-value: 1.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 21 IHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDAKKYGI-----ETIYQTLAVA 95
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVvfgqkTQLWWDLPVI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 96 DNVDAAANLYlgrelrtpwgTLDDVAMEAKAREVMGRLnpNFQRF-KEPVKALSGGQRQSVAIARAILFDARILIMDEPT 174
Cdd:cd03267 114 DSFYLLAAIY----------DLPPARFKKRLDELSELL--DLEELlDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489631109 175 AALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDLADRVSVMKNGQVV 225
Cdd:cd03267 182 IGLDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
20-225 |
1.30e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 99.15 E-value: 1.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 20 GIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAeinnprDAKKYGIETIYQTLAVADNVD 99
Cdd:PRK13636 18 GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI------DYSRKGLMKLRESVGMVFQDP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 100 AAANLYLGRELRTPWGTLDdvaMEAKAREVMGRLNPNFQRF------KEPVKALSGGQRQSVAIARAILFDARILIMDEP 173
Cdd:PRK13636 92 DNQLFSASVYQDVSFGAVN---LKLPEDEVRKRVDNALKRTgiehlkDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489631109 174 TAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDLADRVSVMKNGQVV 225
Cdd:PRK13636 169 TAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVI 221
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-225 |
1.34e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 102.07 E-value: 1.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 7 PLVEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILInGEPAEINnprdakkygie 86
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVKIG----------- 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 87 tiyqtlavadnvdaaanlYL---GREL---RTPWGTLDDVA---MEAKAREVMGRLnpNF--QRFKEPVKALSGGQRQSV 155
Cdd:COG0488 382 ------------------YFdqhQEELdpdKTVLDELRDGApggTEQEVRGYLGRF--LFsgDDAFKPVGVLSGGEKARL 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489631109 156 AIARAILFDARILIMDEPTAALGPqETAQVgeLIKQLKR-EGiGIFLISHDIHDVFDLADRVSVMKNGQVV 225
Cdd:COG0488 442 ALAKLLLSPPNVLLLDEPTNHLDI-ETLEA--LEEALDDfPG-TVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
19-213 |
1.52e-24 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 96.72 E-value: 1.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 19 GGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAeinnprDAKKYGIETIYQTLAVADNV 98
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPL------DYSRKGLLERRQRVGLVFQD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 99 DAAANLYLGRELRTPWGTLD----DVAMEAKAREVMGRLNPNFQRfKEPVKALSGGQRQSVAIARAILFDARILIMDEPT 174
Cdd:TIGR01166 77 PDDQLFAADVDQDVAFGPLNlglsEAEVERRVREALTAVGASGLR-ERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPT 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 489631109 175 AALGPQETAQVGELIKQLKREGIGIFLISHDIhdvfDLA 213
Cdd:TIGR01166 156 AGLDPAGREQMLAILRRLRAEGMTVVISTHDV----DLA 190
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
24-227 |
1.59e-24 |
|
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: 96.85 E-value: 1.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 24 VDDASVDLYPGEVVALLGHNGAGKSTLIKILSG--AYKRDAGEILINGEPAEINNPRdaKKYGietiyqtlavadnvdaa 101
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLDKRSFR--KIIG----------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 102 anlYLGRelrtpwgtlDDVAMEA-KAREVMgrlnpnfqRFKEPVKALSGGQRQSVAIARAILFDARILIMDEPTAALGPQ 180
Cdd:cd03213 86 ---YVPQ---------DDILHPTlTVRETL--------MFAAKLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSS 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489631109 181 ETAQVGELIKQLKREGIGIFLIshdIH----DVFDLADRVSVMKNGQVVGH 227
Cdd:cd03213 146 SALQVMSLLRRLADTGRTIICS---IHqpssEIFELFDKLLLLSQGRVIYF 193
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
9-240 |
2.16e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 99.52 E-value: 2.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAeinnPRDAK----KYG 84
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV----PARARlaraRIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 85 IETIYQTLAVADNVDAAANLYlGRELRTpwgtlddvameaKAREVMGRLNP--NFQRFKE----PVKALSGGQRQSVAIA 158
Cdd:PRK13536 118 VVPQFDNLDLEFTVRENLLVF-GRYFGM------------STREIEAVIPSllEFARLESkadaRVSDLSGGMKRRLTLA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 159 RAILFDARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTEDVTkDEV 238
Cdd:PRK13536 185 RALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALI-DEH 263
|
..
gi 489631109 239 LG 240
Cdd:PRK13536 264 IG 265
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
9-239 |
2.21e-24 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 97.85 E-value: 2.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILING-EPAEINNPRDAKKYGIet 87
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGlDVATTPSRELAKRLAI-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 88 iyqtlavadnvdaaanlyLG-----------REL----RTPWG----TLDDVAMEAKAREVMGrLNPNFQRFkepVKALS 148
Cdd:COG4604 80 ------------------LRqenhinsrltvRELvafgRFPYSkgrlTAEDREIIDEAIAYLD-LEDLADRY---LDELS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 149 GGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDLADRVSVMKNGQVVGH 227
Cdd:COG4604 138 GGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLHDINFASCYADHIVAMKDGRVVAQ 217
|
250
....*....|..
gi 489631109 228 ARTEDVTKDEVL 239
Cdd:COG4604 218 GTPEEIITPEVL 229
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-236 |
2.50e-24 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 101.42 E-value: 2.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 3 EQRTPLVEMKN-----ISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGE--ILINGEPAEIN 75
Cdd:TIGR03269 274 EVGEPIIKVRNvskryISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEWVDMT 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 76 NPRD-----AKKY-GI----ETIYQTLAVADNVDAAANLYLGREL--RTPWGTLDDVAM-EAKAREVMGRLnPNfqrfke 142
Cdd:TIGR03269 354 KPGPdgrgrAKRYiGIlhqeYDLYPHRTVLDNLTEAIGLELPDELarMKAVITLKMVGFdEEKAEEILDKY-PD------ 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 143 pvkALSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLI-SHDIHDVFDLADRVSVMKN 221
Cdd:TIGR03269 427 ---ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIvSHDMDFVLDVCDRAALMRD 503
|
250
....*....|....*
gi 489631109 222 GQVVGHARTEDVTKD 236
Cdd:TIGR03269 504 GKIVKIGDPEEIVEE 518
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-219 |
2.71e-24 |
|
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: 101.21 E-value: 2.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 2 TEQRTPLVEMKNISISFGG-IHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEP-AEINnpRD 79
Cdd:TIGR02857 315 TAAPASSLEFSGVSVAYPGrRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPlADAD--AD 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 80 AKKYGIETIYQTlavadnvdaaANLYLGR-----ELRTPWGTLDDVAMEAKAREVMGRLNPNFQRFKEPV----KALSGG 150
Cdd:TIGR02857 393 SWRDQIAWVPQH----------PFLFAGTiaeniRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIgeggAGLSGG 462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489631109 151 QRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLkREGIGIFLISHDIHDVfDLADRVSVM 219
Cdd:TIGR02857 463 QAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRLALA-ALADRIVVL 529
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
9-224 |
3.42e-24 |
|
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: 96.32 E-value: 3.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISF-GGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPaeINNPRDAK----KY 83
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQD--VSDLRGRAipylRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 84 GIETIYQTLAVADNVDAAANLYLGREL----------RTPwGTLDDVAMEAKAREVmgrlnPNfqrfkepvkALSGGQRQ 153
Cdd:cd03292 79 KIGVVFQDFRLLPDRNVYENVAFALEVtgvppreirkRVP-AALELVGLSHKHRAL-----PA---------ELSGGEQQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489631109 154 SVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQV 224
Cdd:cd03292 144 RVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-225 |
8.07e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 97.85 E-value: 8.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 21 IHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILING-EPAEiNNPRDAKKYG--------------- 84
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyVPFK-RRKEFARRIGvvfgqrsqlwwdlpa 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 85 IETiyqtlavadnvdaaanLYLGREL-RTPwgtlddvamEAKAREVMGRLNP--NFQRF-KEPVKALSGGQRQSVAIARA 160
Cdd:COG4586 114 IDS----------------FRLLKAIyRIP---------DAEYKKRLDELVEllDLGELlDTPVRQLSLGQRMRCELAAA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489631109 161 ILFDARILIMDEPTaaLGPQETAQ--VGELIKQLKRE-GIGIFLISHDIHDVFDLADRVSVMKNGQVV 225
Cdd:COG4586 169 LLHRPKILFLDEPT--IGLDVVSKeaIREFLKEYNRErGTTILLTSHDMDDIEALCDRVIVIDHGRII 234
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
6-238 |
1.14e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 97.18 E-value: 1.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 6 TPLVEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDAKKYGI 85
Cdd:PRK13537 5 VAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 86 ETIYQTLAVADNVDAAANLYlGRELRTPwgtlddvamEAKAREVMGRLnPNFQRFKE----PVKALSGGQRQSVAIARAI 161
Cdd:PRK13537 85 VPQFDNLDPDFTVRENLLVF-GRYFGLS---------AAAARALVPPL-LEFAKLENkadaKVGELSGGMKRRLTLARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489631109 162 LFDARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTEDVTKDEV 238
Cdd:PRK13537 154 VNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEI 230
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
24-225 |
1.38e-23 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 95.91 E-value: 1.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 24 VDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDAKKY--GIETIYQTLAVADNVDAA 101
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFrrDIQMVFQDSISAVNPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 102 ANLYLGRELRTpWGTLDDVAMEAKAREV--MGRLNPNFQRfKEPvKALSGGQRQSVAIARAILFDARILIMDEPTAALGP 179
Cdd:PRK10419 108 VREIIREPLRH-LLSLDKAERLARASEMlrAVDLDDSVLD-KRP-PQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489631109 180 QETAQVGELIKQLKRE-GIGIFLISHDIHDVFDLADRVSVMKNGQVV 225
Cdd:PRK10419 185 VLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-233 |
1.42e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 95.75 E-value: 1.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYK-----RDAGEILINGEPAeINNPRDAKKY 83
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDI-FKMDVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 84 GIETIYQTLAVADNVDAAANLYLG----------REL--RTPWgtlddvAMEaKAR---EVMGRLNPnfqrfkePVKALS 148
Cdd:PRK14247 83 RVQMVFQIPNPIPNLSIFENVALGlklnrlvkskKELqeRVRW------ALE-KAQlwdEVKDRLDA-------PAGKLS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 149 GGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKREgIGIFLISHDIHDVFDLADRVSVMKNGQVVGHA 228
Cdd:PRK14247 149 GGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWG 227
|
....*
gi 489631109 229 RTEDV 233
Cdd:PRK14247 228 PTREV 232
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
33-226 |
1.63e-23 |
|
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: 94.67 E-value: 1.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 33 PGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEP-----AEINNPRDAKKYGIetIYQTLAVADNVDAAANLYLG 107
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrKKINLPPQQRKIGL--VFQQYALFPHLNVRENLAFG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 108 reLRtpwgTLDDVAMEAKAREVMGRLNPNfQRFKEPVKALSGGQRQSVAIARAILFDARILIMDEPTAALgpqETAQVGE 187
Cdd:cd03297 100 --LK----RKRNREDRISVDELLDLLGLD-HLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSAL---DRALRLQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489631109 188 LIKQLKRE----GIGIFLISHDIHDVFDLADRVSVMKNGQVVG 226
Cdd:cd03297 170 LLPELKQIkknlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQY 212
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
11-257 |
1.65e-23 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 96.01 E-value: 1.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 11 MKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEinnPRDAKKYGIETIY- 89
Cdd:PRK10575 14 LRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLE---SWSSKAFARKVAYl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 90 -QTLAVADNVDAAANLYLGrelRTPW-GTLDDVAMEAKAR-----EVMGrLNPNFQRFkepVKALSGGQRQSVAIARAIL 162
Cdd:PRK10575 91 pQQLPAAEGMTVRELVAIG---RYPWhGALGRFGAADREKveeaiSLVG-LKPLAHRL---VDSLSGGERQRAWIAMLVA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 163 FDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTEDVTKDEVLGM 241
Cdd:PRK10575 164 QDSRCLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQ 243
|
250
....*....|....*....
gi 489631109 242 II---MGKVPPkaiPGPGA 257
Cdd:PRK10575 244 IYgipMGILPH---PAGAA 259
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
9-225 |
1.90e-23 |
|
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: 94.48 E-value: 1.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFGgiHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDAKkygIETI 88
Cdd:cd03298 1 VRLDKIRFSYG--EQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP---VSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 89 YQTLAVADNVDAAANLYLGRELRTPWGTLDDVAMEAKAREvMGRLNpnfqRFKEPVKALSGGQRQSVAIARAILFDARIL 168
Cdd:cd03298 76 FQENNLFAHLTVEQNVGLGLSPGLKLTAEDRQAIEVALAR-VGLAG----LEKRLPGELSGGERQRVALARVLVRDKPVL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489631109 169 IMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDLADRVSVMKNGQVV 225
Cdd:cd03298 151 LLDEPFAALDPALRAEMLDLVLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
8-224 |
2.43e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 95.57 E-value: 2.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 8 LVEMKNISISFGG---IHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDaKKYG 84
Cdd:PRK13650 4 IIEVKNLTFKYKEdqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWD-IRHK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 85 IETIYQTLAVAdnvdaaanlYLGRELRtpwgtlDDVA--MEAKA---REVMGRLNP-----NFQRFK--EPVKaLSGGQR 152
Cdd:PRK13650 83 IGMVFQNPDNQ---------FVGATVE------DDVAfgLENKGiphEEMKERVNEalelvGMQDFKerEPAR-LSGGQK 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489631109 153 QSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVfDLADRVSVMKNGQV 224
Cdd:PRK13650 147 QRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNGQV 218
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
6-216 |
3.92e-23 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 94.41 E-value: 3.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 6 TPLVEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEIlingepaeinnpRDAKKYGI 85
Cdd:PRK09544 2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------------KRNGKLRI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 86 ETIYQTLavadNVDAAANLYLGRELRTPWGTLDDVAMEAKAREVMGRLnpnfqrFKEPVKALSGGQRQSVAIARAILFDA 165
Cdd:PRK09544 70 GYVPQKL----YLDTTLPLTVNRFLRLRPGTKKEDILPALKRVQAGHL------IDAPMQKLSGGETQRVLLARALLNRP 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489631109 166 RILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDLADRV 216
Cdd:PRK09544 140 QLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEV 191
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
21-233 |
4.68e-23 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 95.80 E-value: 4.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 21 IHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDAK--KYGIETIYQTlavadnv 98
Cdd:PRK11308 28 VKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKllRQKIQIVFQN------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 99 daaanlylgrelrtPWGTL------------------DDVAME--AKAREVMGR--LNPNF-QRFKEpvkALSGGQRQSV 155
Cdd:PRK11308 101 --------------PYGSLnprkkvgqileepllintSLSAAErrEKALAMMAKvgLRPEHyDRYPH---MFSGGQRQRI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489631109 156 AIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTEDV 233
Cdd:PRK11308 164 AIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQI 242
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
9-225 |
8.46e-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: 8.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISF---GGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRD-AKKYG 84
Cdd:cd03249 1 IEFKNVSFRYpsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWlRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 85 I---E------TIYQTLAvadnvdaaanlyLGRELRTPwGTLDDVAMEAKAREVMGRLnPNfqRFKEPVKA----LSGGQ 151
Cdd:cd03249 81 LvsqEpvlfdgTIAENIR------------YGKPDATD-EEVEEAAKKANIHDFIMSL-PD--GYDTLVGErgsqLSGGQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489631109 152 RQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLkREGIGIFLISHDIHDVFDlADRVSVMKNGQVV 225
Cdd:cd03249 145 KQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRA-MKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVV 216
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
10-224 |
9.19e-23 |
|
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: 91.51 E-value: 9.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 10 EMKNISISFGGIHA--VDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGepaeinnpRDAKKYGIET 87
Cdd:cd03246 2 EVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDG--------ADISQWDPNE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 88 IYQTLAvadnvdaaanlYLGRELRTPWGTLDDvameakarevmgrlnpnfqrfkepvKALSGGQRQSVAIARAILFDARI 167
Cdd:cd03246 74 LGDHVG-----------YLPQDDELFSGSIAE-------------------------NILSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489631109 168 LIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIhDVFDLADRVSVMKNGQV 224
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
3-237 |
1.49e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 93.28 E-value: 1.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 3 EQRTPLVEMKNISISFGGIHA--VDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDA 80
Cdd:PRK13648 2 EDKNSIIVFKNVSFQYQSDASftLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 81 KKYgIETIYQTLAVAdnvdaaanlYLGRELRTpwgtldDVA------------MEAKAREVMGRLNPNFQRFKEPvKALS 148
Cdd:PRK13648 82 RKH-IGIVFQNPDNQ---------FVGSIVKY------DVAfglenhavpydeMHRRVSEALKQVDMLERADYEP-NALS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 149 GGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDlADRVSVMKNGQVVGH 227
Cdd:PRK13648 145 GGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKGTVYKE 223
|
250
....*....|
gi 489631109 228 ARTEDVTKDE 237
Cdd:PRK13648 224 GTPTEIFDHA 233
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
17-216 |
1.78e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 91.14 E-value: 1.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 17 SFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGE------PAEINNPRDAKKygieTIYQ 90
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGarvayvPQRSEVPDSLPL----TVRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 91 TLAvadnvdaaanlyLGR-ELRTPWGTL--DDVAMEAKAREVMGrlnpnFQRF-KEPVKALSGGQRQSVAIARAILFDAR 166
Cdd:NF040873 77 LVA------------MGRwARRGLWRRLtrDDRAAVDDALERVG-----LADLaGRQLGELSGGQRQRALLAQGLAQEAD 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489631109 167 ILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDlADRV 216
Cdd:NF040873 140 LLLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRR-ADPC 188
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
8-239 |
2.01e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 93.33 E-value: 2.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 8 LVEMKNISISF-GGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDAKKY-GI 85
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFvGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 86 ------ETIYQTLAVADNVDAAANLylgrelrtpwgTLDDVAMEAKAREVMGRLNPNFQRFKEPvKALSGGQRQSVAIAR 159
Cdd:PRK13652 83 vfqnpdDQIFSPTVEQDIAFGPINL-----------GLDEETVAHRVSSALHMLGLEELRDRVP-HHLSGGEKKRVAIAG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 160 AILFDARILIMDEPTAALGPQETAQVGELIKQL-KREGIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTEDV-TKDE 237
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLpETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIfLQPD 230
|
..
gi 489631109 238 VL 239
Cdd:PRK13652 231 LL 232
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
8-252 |
2.73e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 92.74 E-value: 2.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 8 LVEMKNISISF-GGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILING----EPAEINNPRdaKK 82
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtgDFSKLQGIR--KL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 83 YGIetIYQTLAVAdnvdaaanlYLGRELRTPWG------TLDDVAMEAKAREVMGRLNPNFQRFKEPvKALSGGQRQSVA 156
Cdd:PRK13644 79 VGI--VFQNPETQ---------FVGRTVEEDLAfgpenlCLPPIEIRKRVDRALAEIGLEKYRHRSP-KTLSGGQGQCVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 157 IARAILFDARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDlADRVSVMKNGQVVGHARTEDVTKD 236
Cdd:PRK13644 147 LAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVLSD 225
|
250
....*....|....*.
gi 489631109 237 evLGMIIMGKVPPKAI 252
Cdd:PRK13644 226 --VSLQTLGLTPPSLI 239
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
9-233 |
3.31e-22 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 92.07 E-value: 3.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFGGIhAVDDASVDLYPGEVVALLGHNGAGKS----TLIKILSGAYKRDAGEILINGEPAE----------- 73
Cdd:PRK10418 5 IELRNIALQAAQP-LVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVApcalrgrkiat 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 74 -INNPRDA-------KKYGIETIYQtlavadnvdaaanlyLGRE--LRTPWGTLDDVAMEAKARevMGRLNPnFQrfkep 143
Cdd:PRK10418 84 iMQNPRSAfnplhtmHTHARETCLA---------------LGKPadDATLTAALEAVGLENAAR--VLKLYP-FE----- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 144 vkaLSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDLADRVSVMKNG 222
Cdd:PRK10418 141 ---MSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHG 217
|
250
....*....|.
gi 489631109 223 QVVGHARTEDV 233
Cdd:PRK10418 218 RIVEQGDVETL 228
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
9-232 |
3.47e-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: 91.52 E-value: 3.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFGG--IHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILING---EPAEINNPRdaKKY 83
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvRDYTLASLR--RQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 84 GI---------ETIYQTLAvadnvdaaanlyLGRelrtPWGTLDDV---AMEAKAREVMGRLNPNFQRF--KEPVKaLSG 149
Cdd:cd03251 79 GLvsqdvflfnDTVAENIA------------YGR----PGATREEVeeaARAANAHEFIMELPEGYDTVigERGVK-LSG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 150 GQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKrEGIGIFLISHDIHDVFDlADRVSVMKNGQVVGHAR 229
Cdd:cd03251 142 GQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLM-KNRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGT 219
|
...
gi 489631109 230 TED 232
Cdd:cd03251 220 HEE 222
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
8-239 |
4.55e-22 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 91.31 E-value: 4.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 8 LVEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGepAEINNPRdAKKYGIE- 86
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG--LKVNDPK-VDERLIRq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 87 ---TIYQtlavadnvdaaaNLYLGRELRtpwgTLDDVAM-------------EAKAREVMGRLNPNfQRFKEPVKALSGG 150
Cdd:PRK09493 78 eagMVFQ------------QFYLFPHLT----ALENVMFgplrvrgaskeeaEKQARELLAKVGLA-ERAHHYPSELSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 151 QRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVvgharT 230
Cdd:PRK09493 141 QQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRI-----A 215
|
....*....
gi 489631109 231 EDVTKDEVL 239
Cdd:PRK09493 216 EDGDPQVLI 224
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
9-238 |
8.91e-22 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 93.88 E-value: 8.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFG-GIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDAKKYgIET 87
Cdd:PRK10522 323 LELRNVTFAYQdNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKL-FSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 88 IYqtlavadnvdaaANLYLGRELRTPWGTLDDVA----------MEAKAREVMGRLNpNFQrfkepvkaLSGGQRQSVAI 157
Cdd:PRK10522 402 VF------------TDFHLFDQLLGPEGKPANPAlvekwlerlkMAHKLELEDGRIS-NLK--------LSKGQKKRLAL 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 158 ARAILFDARILIMDEPTAALGPQ---ETAQvgELIKQLKREGIGIFLISHDIHdVFDLADRVSVMKNGQV---VGHARtE 231
Cdd:PRK10522 461 LLALAEERDILLLDEWAADQDPHfrrEFYQ--VLLPLLQEMGKTIFAISHDDH-YFIHADRLLEMRNGQLselTGEER-D 536
|
....*..
gi 489631109 232 DVTKDEV 238
Cdd:PRK10522 537 AASRDAV 543
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
9-224 |
9.64e-22 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 92.45 E-value: 9.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDaKKYGIetI 88
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD-RKVGF--V 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 89 YQTLAVADNVDAAANLYLG-----RELRtpwgtLDDVAMEAKAREV--MGRLNPNFQRFkePVKaLSGGQRQSVAIARAI 161
Cdd:PRK10851 80 FQHYALFRHMTVFDNIAFGltvlpRRER-----PNAAAIKAKVTQLleMVQLAHLADRY--PAQ-LSGGQKQRVALARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489631109 162 LFDARILIMDEPTAALGPQETAQVGELIKQLKRE--GIGIFlISHDIHDVFDLADRVSVMKNGQV 224
Cdd:PRK10851 152 AVEPQILLLDEPFGALDAQVRKELRRWLRQLHEElkFTSVF-VTHDQEEAMEVADRVVVMSQGNI 215
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
8-225 |
9.68e-22 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 94.02 E-value: 9.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 8 LVEMKNISISF---GGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEP-AEINNPRDAKKY 83
Cdd:TIGR00958 478 LIEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPlVQYDHHYLHRQV 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 84 GIetIYQTLAVADNVDAAANLYLGRelRTPWGTLDDVAMEAKARE-VMGRLNPNFQRFKEPVKALSGGQRQSVAIARAIL 162
Cdd:TIGR00958 558 AL--VGQEPVLFSGSVRENIAYGLT--DTPDEEIMAAAKAANAHDfIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALV 633
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489631109 163 FDARILIMDEPTAALGPQETAQVGELikqLKREGIGIFLISHDIHDVfDLADRVSVMKNGQVV 225
Cdd:TIGR00958 634 RKPRVLILDEATSALDAECEQLLQES---RSRASRTVLLIAHRLSTV-ERADQILVLKKGSVV 692
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-224 |
1.34e-21 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 90.51 E-value: 1.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 4 QRTPLVeMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPaeINNPRDakky 83
Cdd:PRK11247 9 QGTPLL-LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAP--LAEARE---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 84 GIETIYQTlavadnvdaaanlylGRELrtPWGT-LDDVAM------EAKAREVMGRLNPNfQRFKEPVKALSGGQRQSVA 156
Cdd:PRK11247 82 DTRLMFQD---------------ARLL--PWKKvIDNVGLglkgqwRDAALQALAAVGLA-DRANEWPAALSGGQKQRVA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489631109 157 IARAILFDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDLADRVSVMKNGQV 224
Cdd:PRK11247 144 LARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQhGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
29-225 |
1.35e-21 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 89.91 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 29 VDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINN------PRD---AKKYGIEtIYQTLAVADNVD 99
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKGWrhigyvPQRhefAWDFPIS-VAHTVMSGRTGH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 100 AAanlYLGRELRTPWGTLDDVAMEAKAREVMGRlnpnfqrfkePVKALSGGQRQSVAIARAILFDARILIMDEPTAALGP 179
Cdd:TIGR03771 80 IG---WLRRPCVADFAAVRDALRRVGLTELADR----------PVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDM 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489631109 180 QETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVsVMKNGQVV 225
Cdd:TIGR03771 147 PTQELLTELFIELAGAGTAILMTTHDLAQAMATCDRV-VLLNGRVI 191
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
24-236 |
1.42e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 91.04 E-value: 1.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 24 VDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDA-----KKYGIETIYQTLAVADNV 98
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNlkklrKKVSLVFQFPEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 99 DAAANLYLGRELrtpwGTLDDVAMEaKAREVMGRLNPNFQRFKEPVKALSGGQRQSVAIARAILFDARILIMDEPTAALG 178
Cdd:PRK13641 103 VLKDVEFGPKNF----GFSEDEAKE-KALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489631109 179 PQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTEDVTKD 236
Cdd:PRK13641 178 PEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSD 235
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
8-213 |
1.68e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 90.14 E-value: 1.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 8 LVEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPaeINNPrdakkyGIE- 86
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKP--VEGP------GAEr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 87 -TIYQtlavadnvdaaanlylgRELRTPW-GTLDDVAM------------EAKAREVMGR--LNPNFQRFkepVKALSGG 150
Cdd:PRK11248 73 gVVFQ-----------------NEGLLPWrNVQDNVAFglqlagvekmqrLEIAHQMLKKvgLEGAEKRY---IWQLSGG 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489631109 151 QRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDLA 213
Cdd:PRK11248 133 QRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQEtGKQVLLITHDIEEAVFMA 196
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
26-241 |
2.02e-21 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 92.81 E-value: 2.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 26 DASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEpaEINN--PRDAKKYGIetIYqtlavADNVDAAAN 103
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGK--EINAlsTAQRLARGL--VY-----LPEDRQSSG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 104 LYLGRELRtpW-------GTLDDVAMEAKAREVMGR----LNPNFQRFKEPVKALSGGQRQSVAIARAILFDARILIMDE 172
Cdd:PRK15439 352 LYLDAPLA--WnvcalthNRRGFWIKPARENAVLERyrraLNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDE 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489631109 173 PTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTEDVTKDEVLGM 241
Cdd:PRK15439 430 PTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAINVDTIMRL 498
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
28-216 |
2.17e-21 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 88.71 E-value: 2.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 28 SVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPaeINNPRDAkkygietIYQTLavadnvdaaanLYLG 107
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEP--IRRQRDE-------YHQDL-----------LYLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 108 ------RELrTPWGTL-----------DDVAMEAKARevMGrlnpnFQRFKE-PVKALSGGQRQSVAIARAILFDARILI 169
Cdd:PRK13538 81 hqpgikTEL-TALENLrfyqrlhgpgdDEALWEALAQ--VG-----LAGFEDvPVRQLSAGQQRRVALARLWLTRAPLWI 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489631109 170 MDEPTAALGPQETAQVGELIKQ-LKREGIGIfLISHdiHDVFDLADRV 216
Cdd:PRK13538 153 LDEPFTAIDKQGVARLEALLAQhAEQGGMVI-LTTH--QDLPVASDKV 197
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-225 |
2.24e-21 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 93.00 E-value: 2.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 2 TEQRT-----PLVEMKNISISF---GGI--------HAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEI 65
Cdd:PRK10261 302 IEQDTvvdgePILQVRNLVTRFplrSGLlnrvtrevHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEI 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 66 LINGEpaEINNPRDAK----KYGIETIYQTLAVADNVDAAANLYLGRELRTPwGTLDDVAMEAKAREVMGR--LNPNfQR 139
Cdd:PRK10261 382 IFNGQ--RIDTLSPGKlqalRRDIQFIFQDPYASLDPRQTVGDSIMEPLRVH-GLLPGKAAAARVAWLLERvgLLPE-HA 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 140 FKEPvKALSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDLADRVSV 218
Cdd:PRK10261 458 WRYP-HEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAV 536
|
....*..
gi 489631109 219 MKNGQVV 225
Cdd:PRK10261 537 MYLGQIV 543
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
39-225 |
3.42e-21 |
|
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: 90.63 E-value: 3.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 39 LLGHNGAGKSTLIKILSGAYKRDAGEILINGEpaEINNpRDAKKYGIETIYQTLAVADNVDAAANLYLGRELRTpwgtLD 118
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGE--DVTN-VPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRK----VP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 119 DVAMEAKAREVMGRLNPNFQRFKEPVKaLSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKRE-GI 197
Cdd:TIGR01187 74 RAEIKPRVLEALRLVQLEEFADRKPHQ-LSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQlGI 152
|
170 180
....*....|....*....|....*...
gi 489631109 198 GIFLISHDIHDVFDLADRVSVMKNGQVV 225
Cdd:TIGR01187 153 TFVFVTHDQEEAMTMSDRIAIMRKGKIA 180
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
23-236 |
5.69e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 89.42 E-value: 5.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 23 AVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEpaEINNprDAKKYGIETIYQTLavadnvdaaa 102
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDT--LITS--TSKNKDIKQIRKKV---------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 103 nlylGRELRTPWG------TLDDVAM------------EAKAREVMGRLNPNFQRFKEPVKALSGGQRQSVAIARAILFD 164
Cdd:PRK13649 88 ----GLVFQFPESqlfeetVLKDVAFgpqnfgvsqeeaEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAME 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489631109 165 ARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTEDVTKD 236
Cdd:PRK13649 164 PKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
28-242 |
5.90e-21 |
|
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: 91.73 E-value: 5.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 28 SVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGepAEINN-PRDAkkygietiyqtlavadnvdaaanlyL 106
Cdd:COG4618 352 SFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDG--ADLSQwDREE-------------------------L 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 107 GR---------EL----------RTPWGTLDDV---AMEAKAREVMGRLNpnfQRFKEPV----KALSGGQRQSVAIARA 160
Cdd:COG4618 405 GRhigylpqdvELfdgtiaeniaRFGDADPEKVvaaAKLAGVHEMILRLP---DGYDTRIgeggARLSGGQRQRIGLARA 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 161 ILFDARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHdVFDLADRVSVMKNGQVVGHArtedvTKDEVLG 240
Cdd:COG4618 482 LYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPS-LLAAVDKLLVLRDGRVQAFG-----PRDEVLA 555
|
..
gi 489631109 241 MI 242
Cdd:COG4618 556 RL 557
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-233 |
7.23e-21 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 89.78 E-value: 7.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 1 MTEQRTPLVEMKNISISF----GGIHAVDDASVDLYPGEVVALLGHNGAGKS----TLIKIL------SGAYKRDAGEIL 66
Cdd:PRK09473 5 AQQQADALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLaangriGGSATFNGREIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 67 iNGEPAEINNPRdAKKygIETIYQT--------LAVADNVDAAANLYLGRELRTPWG----TLDDVAM-EAKARevMGRL 133
Cdd:PRK09473 85 -NLPEKELNKLR-AEQ--ISMIFQDpmtslnpyMRVGEQLMEVLMLHKGMSKAEAFEesvrMLDAVKMpEARKR--MKMY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 134 NPNFqrfkepvkalSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDL 212
Cdd:PRK09473 159 PHEF----------SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGI 228
|
250 260
....*....|....*....|.
gi 489631109 213 ADRVSVMKNGQVVGHARTEDV 233
Cdd:PRK09473 229 CDKVLVMYAGRTMEYGNARDV 249
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
23-239 |
8.16e-21 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 90.94 E-value: 8.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 23 AVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDAKKYGIET---------IYQTLA 93
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHGFALvteerrstgIYAYLD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 94 VADNVDAAANlylgRELRTPWGTLDDVAMEAKAREVMGRLNPNFQRFKEPVKALSGGQRQSVAIARAILFDARILIMDEP 173
Cdd:PRK10982 343 IGFNSLISNI----RNYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEP 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489631109 174 TAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTEDVTKDEVL 239
Cdd:PRK10982 419 TRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAGIVDTKTTTQNEIL 484
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
9-225 |
8.36e-21 |
|
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: 88.06 E-value: 8.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFG-GIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEP-AEINNPRDAKKYGI- 85
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDiREVTLDSLRRAIGVv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 86 --------ETIYQTLAvadnvdaaanlylgrelrtpWGTLD--DVAMEAKARevMGRLNPNFQRFKEPVKA--------L 147
Cdd:cd03253 81 pqdtvlfnDTIGYNIR--------------------YGRPDatDEEVIEAAK--AAQIHDKIMRFPDGYDTivgerglkL 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489631109 148 SGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFlISHDIHDVFDlADRVSVMKNGQVV 225
Cdd:cd03253 139 SGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIV-IAHRLSTIVN-ADKIIVLKDGRIV 214
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
9-237 |
1.05e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 88.99 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFGG-----IHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEIN-NPRDAKK 82
Cdd:PRK13651 3 IKVKNIVKIFNKklpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 83 YGIETIYQtlavadnVDAAANLYLGRELRTPWGTL--------------DDVAM----------EAKAR-----EVMGrL 133
Cdd:PRK13651 83 VLEKLVIQ-------KTRFKKIKKIKEIRRRVGVVfqfaeyqlfeqtieKDIIFgpvsmgvskeEAKKRaakyiELVG-L 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 134 NPNFQRfKEPVkALSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLA 213
Cdd:PRK13651 155 DESYLQ-RSPF-ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWT 232
|
250 260
....*....|....*....|....
gi 489631109 214 DRVSVMKNGQVVGHARTEDVTKDE 237
Cdd:PRK13651 233 KRTIFFKDGKIIKDGDTYDILSDN 256
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
28-242 |
1.16e-20 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 87.59 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 28 SVDLYPGEVVALLGHNGAGKSTLIKILSGAYkRDAGEILINGEPAEINNPRDAKKY-----------GIETIYQTLAvad 96
Cdd:COG4138 16 SAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHraylsqqqsppFAMPVFQYLA--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 97 nvdaaanLYLGRELRTPwgtLDDVAMEAKAREVmgRLNPNFQRfkePVKALSGGQRQSVAIARAIL-------FDARILI 169
Cdd:COG4138 92 -------LHQPAGASSE---AVEQLLAQLAEAL--GLEDKLSR---PLTQLSGGEWQRVRLAAVLLqvwptinPEGQLLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489631109 170 MDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTEDVTKDEVLGMI 242
Cdd:COG4138 157 LDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEV 229
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-216 |
1.18e-20 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 87.46 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 1 MTEqRTPLVEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDA 80
Cdd:PRK10247 1 MQE-NSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 81 KK-----------YGiETIYQTLAVadnvdaaanlylgrelrtPWGTLDDVAMEAKAREVMGRLNPNFQRFKEPVKALSG 149
Cdd:PRK10247 80 RQqvsycaqtptlFG-DTVYDNLIF------------------PWQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSG 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489631109 150 GQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDiHDVFDLADRV 216
Cdd:PRK10247 141 GEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREqNIAVLWVTHD-KDEINHADKV 207
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
24-233 |
1.19e-20 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 88.35 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 24 VDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYK--------RDAGEILINGEP-AEINNPRDAKKYGIetIYQTLAV 94
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgaRVTGDVTLNGEPlAAIDAPRLARLRAV--LPQAAQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 95 ADNVDAAANLYLGR--------ELRTPWGTLDDVAME-AKAREVMGRlnpnfqrfkePVKALSGGQRQSVAIARAI---- 161
Cdd:PRK13547 95 AFAFSAREIVLLGRypharragALTHRDGEIAWQALAlAGATALVGR----------DVTTLSGGELARVQFARVLaqlw 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489631109 162 -----LFDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTEDV 233
Cdd:PRK13547 165 pphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
28-240 |
1.29e-20 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 87.68 E-value: 1.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 28 SVDLYPGEVVALLGHNGAGKSTLIKILSG--AYKrdaGEILINGEPAEINNPRDAKKY-----------GIETIYQTLAv 94
Cdd:PRK03695 16 SAEVRAGEILHLVGPNGAGKSTLLARMAGllPGS---GSIQFAGQPLEAWSAAELARHraylsqqqtppFAMPVFQYLT- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 95 adnvdaaanLYL--GRELRTPWGTLDDVAMEAKAREVMGRlnpnfqrfkePVKALSGGQRQSVAIARAIL-------FDA 165
Cdd:PRK03695 92 ---------LHQpdKTRTEAVASALNEVAEALGLDDKLGR----------SVNQLSGGEWQRVRLAAVVLqvwpdinPAG 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489631109 166 RILIMDEPTAALgpqETAQVG---ELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTEDVTKDEVLG 240
Cdd:PRK03695 153 QLLLLDEPMNSL---DVAQQAaldRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLA 227
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
26-225 |
2.54e-20 |
|
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: 86.56 E-value: 2.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 26 DASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDA---GEILINGEPAEINNPRDAKKYGIE--------TIYQTLav 94
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKPDQFQKCVAYVRQddillpglTVRETL-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 95 adnvdaaanlYLGRELRTPWGTLDDVAMEAKAREVMGRLNpnFQRFKEP-VKALSGGQRQSVAIARAILFDARILIMDEP 173
Cdd:cd03234 103 ----------TYTAILRLPRKSSDAIRKKRVEDVLLRDLA--LTRIGGNlVKGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489631109 174 TAALGPQETAQVGELIKQLKREGIGIfLIShdIH----DVFDLADRVSVMKNGQVV 225
Cdd:cd03234 171 TSGLDSFTALNLVSTLSQLARRNRIV-ILT--IHqprsDLFRLFDRILLLSSGEIV 223
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2-239 |
2.90e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 89.46 E-value: 2.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 2 TEQRTPLVEMKNISISFGGihAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDAK 81
Cdd:PRK09700 259 NLAHETVFEVRNVTSRDRK--KVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAV 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 82 KYGIETI---------YQTLAVADNVDAAANLYLGReLRTPWGTLDDVAMEAKAREVMGRLNPNFQRFKEPVKALSGGQR 152
Cdd:PRK09700 337 KKGMAYItesrrdngfFPNFSIAQNMAISRSLKDGG-YKGAMGLFHEVDEQRTAENQRELLALKCHSVNQNITELSGGNQ 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 153 QSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVVGH-ARTE 231
Cdd:PRK09700 416 QKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQIlTNRD 495
|
....*...
gi 489631109 232 DVTKDEVL 239
Cdd:PRK09700 496 DMSEEEIM 503
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
9-240 |
3.10e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 87.10 E-value: 3.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISF-GGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDA-KKYGIe 86
Cdd:PRK13647 5 IEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVrSKVGL- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 87 tIYQTLAVADNVDaaanlylgrelrTPWgtlDDVA-----MEAKAREVMGRLNP-----NFQRFKE-PVKALSGGQRQSV 155
Cdd:PRK13647 84 -VFQDPDDQVFSS------------TVW---DDVAfgpvnMGLDKDEVERRVEEalkavRMWDFRDkPPYHLSYGQKKRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 156 AIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTEDVTK 235
Cdd:PRK13647 148 AIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTD 227
|
....*
gi 489631109 236 DEVLG 240
Cdd:PRK13647 228 EDIVE 232
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
6-225 |
3.11e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 89.78 E-value: 3.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 6 TPLVEMKNISISF----GGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEP-AEINNPRDA 80
Cdd:PRK10535 2 TALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDvATLDADALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 81 K----KYGIetIYQ-----TLAVADNVDAAANLYLGRELRtpwgtlddvAMEAKAREVMGRLNPNfQRFKEPVKALSGGQ 151
Cdd:PRK10535 82 QlrreHFGF--IFQryhllSHLTAAQNVEVPAVYAGLERK---------QRLLRAQELLQRLGLE-DRVEYQPSQLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489631109 152 RQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHdVFDLADRVSVMKNGQVV 225
Cdd:PRK10535 150 QQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQ-VAAQAERVIEIRDGEIV 222
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
21-224 |
3.27e-20 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 86.99 E-value: 3.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 21 IHAVDdasVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAG-----EILINGEPAEINNPRDAKKYGIET--IYQTLA 93
Cdd:PRK09984 20 LHAVD---LNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSagshiELLGRTVQREGRLARDIRKSRANTgyIFQQFN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 94 VADNVDAAANLYLGRELRTP-WGTL--------DDVAMEAKARevMGRLNPNFQRfkepVKALSGGQRQSVAIARAILFD 164
Cdd:PRK09984 97 LVNRLSVLENVLIGALGSTPfWRTCfswftreqKQRALQALTR--VGMVHFAHQR----VSTLSGGQQQRVAIARALMQQ 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489631109 165 ARILIMDEPTAALGPQETAQVGELIKQLKR-EGIGIFLISHDIHDVFDLADRVSVMKNGQV 224
Cdd:PRK09984 171 AKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
9-225 |
4.40e-20 |
|
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: 85.62 E-value: 4.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISF--GGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGepaeinnpRDAKKYGIE 86
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDG--------VDISKIGLH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 87 TIYQTLAVADNVDAaanLYLG--RELRTP---------WGTLDDVAMEAKAREVMGRLNpnfQRFKEPVKALSGGQRQSV 155
Cdd:cd03244 75 DLRSRISIIPQDPV---LFSGtiRSNLDPfgeysdeelWQALERVGLKEFVESLPGGLD---TVVEEGGENLSVGQRQLL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 156 AIARAILFDARILIMDEPTAALGPQETAQVGELIKQlKREGIGIFLISHDIHDVFDlADRVSVMKNGQVV 225
Cdd:cd03244 149 CLARALLRKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHRLDTIID-SDRILVLDKGRVV 216
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
23-225 |
9.16e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 85.99 E-value: 9.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 23 AVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINgepaEINNPRDAKKYGIETIYQTLAVADNVDAAA 102
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVD----DITITHKTKDKYIRPVRKRIGMVFQFPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 103 NLYLGRELRTPWG------TLDDVAMEAK--------AREVMgRLNPnFQrfkepvkaLSGGQRQSVAIARAILFDARIL 168
Cdd:PRK13646 98 LFEDTVEREIIFGpknfkmNLDEVKNYAHrllmdlgfSRDVM-SQSP-FQ--------MSGGQMRKIAIVSILAMNPDII 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489631109 169 IMDEPTAALGPQETAQVGELIKQLK-REGIGIFLISHDIHDVFDLADRVSVMKNGQVV 225
Cdd:PRK13646 168 VLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIV 225
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-231 |
1.20e-19 |
|
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: 84.79 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 1 MTEQRTPLVEMKNISISFGG----IHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEpaEINN 76
Cdd:COG4181 1 MSSSSAPIIELRGLTKTVGTgageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQ--DLFA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 77 -PRDA------KKYGIetIYQ------TLavadnvdaaanlylgrelrtpwgT-LDDVAM----------EAKAREVMGR 132
Cdd:COG4181 79 lDEDArarlraRHVGF--VFQsfqllpTL-----------------------TaLENVMLplelagrrdaRARARALLER 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 133 --LNpnfQRFKEPVKALSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHdv 209
Cdd:COG4181 134 vgLG---HRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRErGTTLVLVTHDPA-- 208
|
250 260
....*....|....*....|....*
gi 489631109 210 fdLA---DRVSVMKNGQVVGHARTE 231
Cdd:COG4181 209 --LAarcDRVLRLRAGRLVEDTAAT 231
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
30-225 |
3.01e-19 |
|
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: 86.78 E-value: 3.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 30 DLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNpRDAKKYGIETIYQtlavadnvdaaaNLYLGRE 109
Cdd:COG4615 354 TIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADN-REAYRQLFSAVFS------------DFHLFDR 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 110 LrtpWGtLDDVAMEAKAREVMGRLNpnfqrFKEPVK---------ALSGGQRQSVAIARAILFDARILIMDEPTAALGPQ 180
Cdd:COG4615 421 L---LG-LDGEADPARARELLERLE-----LDHKVSvedgrfsttDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPE 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489631109 181 ------EtaqvgELIKQLKREGIGIFLISHDIHdVFDLADRVSVMKNGQVV 225
Cdd:COG4615 492 frrvfyT-----ELLPELKARGKTVIAISHDDR-YFDLADRVLKMDYGKLV 536
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
34-224 |
3.78e-19 |
|
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: 82.99 E-value: 3.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 34 GEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPrdaKKYGIETIYQTLAVADNVDAAANLYLGRELRTP 113
Cdd:TIGR01277 24 GEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAP---YQRPVSMLFQENNLFAHLTVRQNIGLGLHPGLK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 114 WGTLDDVAMEAKAREV-----MGRLnPNfqrfkepvkALSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGEL 188
Cdd:TIGR01277 101 LNAEQQEKVVDAAQQVgiadyLDRL-PE---------QLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLAL 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 489631109 189 IKQLKRE-GIGIFLISHDIHDVFDLADRVSVMKNGQV 224
Cdd:TIGR01277 171 VKQLCSErQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
10-204 |
1.07e-18 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 81.25 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 10 EMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAeinnPRDAKKYGIETIY 89
Cdd:TIGR01189 2 AARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPL----AEQRDEPHENILY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 90 --------QTLAVADNVDAAANLyLGRELRTPWGTLDDVAMEAKArevmgrlnpnfqrfKEPVKALSGGQRQSVAIARAI 161
Cdd:TIGR01189 78 lghlpglkPELSALENLHFWAAI-HGGAQRTIEDALAAVGLTGFE--------------DLPAAQLSAGQQRRLALARLW 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489631109 162 LFDARILIMDEPTAALGPQETAQVGELIKQ-LKREGIgIFLISH 204
Cdd:TIGR01189 143 LSRRPLWILDEPTTALDKAGVALLAGLLRAhLARGGI-VLLTTH 185
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
9-230 |
1.25e-18 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 82.49 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDAKKYGIETI 88
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQKGLIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 89 YQTLAVadnvdaaanLYLGRELRTPWGTLDDV-------------AMEAKAREVMGRLNPNFQRFKEPvKALSGGQRQSV 155
Cdd:PRK11264 84 RQHVGF---------VFQNFNLFPHRTVLENIiegpvivkgepkeEATARARELLAKVGLAGKETSYP-RRLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489631109 156 AIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVV--GHART 230
Cdd:PRK11264 154 AIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVeqGPAKA 230
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
23-239 |
1.27e-18 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 84.31 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 23 AVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILING-EPAEINNP--RDAKKYGIETIYQTLAVADNVD 99
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvDIAKISDAelREVRRKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 100 AAANLYLGRELrtpwGTLDDVAMEAKAREVMGRLNPNFQRFKEPvKALSGGQRQSVAIARAILFDARILIMDEPTAALGP 179
Cdd:PRK10070 123 VLDNTAFGMEL----AGINAEERREKALDALRQVGLENYAHSYP-DELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489631109 180 Q-ETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVVghartEDVTKDEVL 239
Cdd:PRK10070 198 LiRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV-----QVGTPDEIL 253
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
24-235 |
1.36e-18 |
|
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: 84.71 E-value: 1.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 24 VDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGepAEINNpRDAKKYGiETIYqtlavadnvdaaan 103
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDG--ADLKQ-WDRETFG-KHIG-------------- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 104 lYLGRELRTPWGTL--------DDV--------AMEAKAREVMGRLNPNFQRFKEPVKA-LSGGQRQSVAIARAILFDAR 166
Cdd:TIGR01842 396 -YLPQDVELFPGTVaeniarfgENAdpekiieaAKLAGVHELILRLPDGYDTVIGPGGAtLSGGQRQRIALARALYGDPK 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489631109 167 ILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIhDVFDLADRVSVMKNGQVVGHARTEDVTK 235
Cdd:TIGR01842 475 LVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRP-SLLGCVDKILVLQDGRIARFGERDEVLA 542
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
23-236 |
1.36e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 82.76 E-value: 1.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 23 AVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILInGEpAEINNPRDAK-------KYGI---------- 85
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GE-RVITAGKKNKklkplrkKVGIvfqfpehqlf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 86 -ETIYQTLAVADNVdaaanlylgrelrtpWGTLDDVAmEAKAREVMGR--LNPNFqRFKEPVkALSGGQRQSVAIARAIL 162
Cdd:PRK13634 100 eETVEKDICFGPMN---------------FGVSEEDA-KQKAREMIELvgLPEEL-LARSPF-ELSGGQMRRVAIAGVLA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489631109 163 FDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTEDVTKD 236
Cdd:PRK13634 162 MEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEkGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFAD 236
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
7-205 |
1.47e-18 |
|
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: 84.72 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 7 PLVEMKNISISFGGIHAV-DDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINN--------- 76
Cdd:TIGR02868 333 PTLELRDLSAGYPGAPPVlDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDqdevrrrvs 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 77 --PRDAKKYGiETIYQTLAvadnvdaaanlyLGRELRTP---WGTLDDVAMEAKAREVMGRLNpnfQRFKEPVKALSGGQ 151
Cdd:TIGR02868 413 vcAQDAHLFD-TTVRENLR------------LARPDATDeelWAALERVGLADWLRALPDGLD---TVLGEGGARLSGGE 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489631109 152 RQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKrEGIGIFLISHD 205
Cdd:TIGR02868 477 RQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAAL-SGRTVVLITHH 529
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-261 |
1.56e-18 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 83.62 E-value: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 1 MTEQRtpLVEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGE---PAEINNp 77
Cdd:PRK11432 1 MTQKN--FVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEdvtHRSIQQ- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 78 RDakkygIETIYQTLAvadnvdaaanLYlgrelrtPWGTLDD-----VAMEAKAREVMGrlnpnfQRFKEP--------- 143
Cdd:PRK11432 78 RD-----ICMVFQSYA----------LF-------PHMSLGEnvgygLKMLGVPKEERK------QRVKEAlelvdlagf 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 144 ----VKALSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQL-KREGIGIFLISHDIHDVFDLADRVSV 218
Cdd:PRK11432 130 edryVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELqQQFNITSLYVTHDQSEAFAVSDTVIV 209
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 489631109 219 MKNGQvvghartedvtkdevlgmiIMGKVPPKAI-PGPGAMQMA 261
Cdd:PRK11432 210 MNKGK-------------------IMQIGSPQELyRQPASRFMA 234
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
9-239 |
2.11e-18 |
|
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: 81.38 E-value: 2.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFG--GIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPrdakkygie 86
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADP--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 87 tiyQTLAVADNVDAAANLYLGRELR---------TPWGTLDDVAMEAKAREVMGRLNPNF-QRFKEPVKALSGGQRQSVA 156
Cdd:cd03252 72 ---AWLRRQVGVVLQENVLFNRSIRdnialadpgMSMERVIEAAKLAGAHDFISELPEGYdTIVGEQGAGLSGGQRQRIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 157 IARAILFDARILIMDEPTAALGPQETAQVgelIKQLKR--EGIGIFLISHDIHDVFDlADRVSVMKNGQVVghartEDVT 234
Cdd:cd03252 149 IARALIHNPRILIFDEATSALDYESEHAI---MRNMHDicAGRTVIIIAHRLSTVKN-ADRIIVMEKGRIV-----EQGS 219
|
....*
gi 489631109 235 KDEVL 239
Cdd:cd03252 220 HDELL 224
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
9-223 |
2.62e-18 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 79.03 E-value: 2.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGepaeinnprdakkyGIETI 88
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS--------------TVKIG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 89 YqtlavadnvdaaanlylgrelrtpwgtlddvameakarevmgrlnpnfqrfkepVKALSGGQRQSVAIARAILFDARIL 168
Cdd:cd03221 67 Y------------------------------------------------------FEQLSGGEKMRLALAKLLLENPNLL 92
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489631109 169 IMDEPTAALGPqETAQVgeLIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQ 223
Cdd:cd03221 93 LLDEPTNHLDL-ESIEA--LEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
31-231 |
3.45e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 83.56 E-value: 3.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 31 LYPGEVVALLGHNGAGKSTLIKILSGAYKRD---AGEILINGEPAEINNPRDAKKYgietIYQTLAVADNVDAAANLYLG 107
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMRAISAY----VQQDDLFIPTLTVREHLMFQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 108 RELRTPWGTLDDVAMEAkAREV---MGRLNPNFQRFKEP--VKALSGGQRQSVAIARAILFDARILIMDEPTAALGPQET 182
Cdd:TIGR00955 124 AHLRMPRRVTKKEKRER-VDEVlqaLGLRKCANTRIGVPgrVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMA 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489631109 183 AQVGELIKQLKREGIGIFLIshdIH----DVFDLADRVSVMKNGQVVGHARTE 231
Cdd:TIGR00955 203 YSVVQVLKGLAQKGKTIICT---IHqpssELFELFDKIILMAEGRVAYLGSPD 252
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
8-224 |
3.66e-18 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 80.59 E-value: 3.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 8 LVEMKNISISF---GGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAeinnPRDAKKYg 84
Cdd:cd03248 11 IVKFQNVTFAYptrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPI----SQYEHKY- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 85 ietiyqtLAVADNVDAAANLYLGRELR---------TPWGTLDDVAMEAKAREVMGRLNPNFQ-RFKEPVKALSGGQRQS 154
Cdd:cd03248 86 -------LHSKVSLVGQEPVLFARSLQdniayglqsCSFECVKEAAQKAHAHSFISELASGYDtEVGEKGSQLSGGQKQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 155 VAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKREGIgIFLISHDIHDVfDLADRVSVMKNGQV 224
Cdd:cd03248 159 VAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRT-VLVIAHRLSTV-ERADQILVLDGGRI 226
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
8-233 |
4.18e-18 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 81.37 E-value: 4.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 8 LVEMKNISISF---------GGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPR 78
Cdd:PRK15112 4 LLEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 79 dAKKYGIETIYQTLAVADNVDAAANLYLGRELRTpwgtldDVAMEAKARE--------VMGRLNPNFQRFKEpvkALSGG 150
Cdd:PRK15112 84 -YRSQRIRMIFQDPSTSLNPRQRISQILDFPLRL------NTDLEPEQREkqiietlrQVGLLPDHASYYPH---MLAPG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 151 QRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLK-REGIGIFLISHDIHDVFDLADRVSVMKNGQVVGHAR 229
Cdd:PRK15112 154 QKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQeKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGS 233
|
....
gi 489631109 230 TEDV 233
Cdd:PRK15112 234 TADV 237
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
7-224 |
4.33e-18 |
|
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: 83.52 E-value: 4.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 7 PLVEMKNISISF--GGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDAKKYG 84
Cdd:TIGR01257 927 PGVCVKNLVKIFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLG 1006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 85 IETIYQTLAVADNVDAAANLYLGRELRTpWgtlDDVAMEAKArevMGRLNPNFQRFKEPVKALSGGQRQSVAIARAILFD 164
Cdd:TIGR01257 1007 MCPQHNILFHHLTVAEHILFYAQLKGRS-W---EEAQLEMEA---MLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGD 1079
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 165 ARILIMDEPTAALGPQETAQVGELIKQLkREGIGIFLISHDIHDVFDLADRVSVMKNGQV 224
Cdd:TIGR01257 1080 AKVVVLDEPTSGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
7-233 |
4.93e-18 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 81.77 E-value: 4.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 7 PLVEMKNISISF----GGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDageILINGEPAEINN------ 76
Cdd:PRK15093 2 PLLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDN---WRVTADRMRFDDidllrl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 77 -PRDAKK---YGIETIYQ----------TLAVADNVDAAANLYLGREL-RTPWgtlddvaMEAKAREVMGRLNpnFQRFK 141
Cdd:PRK15093 79 sPRERRKlvgHNVSMIFQepqscldpseRVGRQLMQNIPGWTYKGRWWqRFGW-------RKRRAIELLHRVG--IKDHK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 142 EPVKA----LSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQL-KREGIGIFLISHDIHDVFDLADRV 216
Cdd:PRK15093 150 DAMRSfpyeLTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKI 229
|
250
....*....|....*..
gi 489631109 217 SVMKNGQVVGHARTEDV 233
Cdd:PRK15093 230 NVLYCGQTVETAPSKEL 246
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-233 |
5.63e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 80.59 E-value: 5.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 1 MTEqrtPLVEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRD-----AGEILINGepAEIN 75
Cdd:PRK14239 1 MTE---PILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNG--HNIY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 76 NPR----DAKKYgIETIYQTLAVADNVDAAANLYlGRELRtpwGTLD----DVAMEAKAR------EVMGRLNpnfqrfk 141
Cdd:PRK14239 76 SPRtdtvDLRKE-IGMVFQQPNPFPMSIYENVVY-GLRLK---GIKDkqvlDEAVEKSLKgasiwdEVKDRLH------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 142 EPVKALSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKREgIGIFLISHDIHDVFDLADRVSVMKN 221
Cdd:PRK14239 144 DSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLD 222
|
250
....*....|..
gi 489631109 222 GQVVGHARTEDV 233
Cdd:PRK14239 223 GDLIEYNDTKQM 234
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-230 |
5.70e-18 |
|
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: 82.91 E-value: 5.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 2 TEQRTPLVEMKNISISFGGIHAVDDASvDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEIL----INGEPAEINNP 77
Cdd:COG1245 335 EKEEETLVEYPDLTKSYGGFSLEVEGG-EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDedlkISYKPQYISPD 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 78 RDakkygiETIYQTLAVAdnvdaaanlyLGRELRTPWGTLddvameakarEVMGRLN--PNFQRfkePVKALSGGQRQSV 155
Cdd:COG1245 414 YD------GTVEEFLRSA----------NTDDFGSSYYKT----------EIIKPLGleKLLDK---NVKDLSGGELQRV 464
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489631109 156 AIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDLADRVSVMKnGQ--VVGHART 230
Cdd:COG1245 465 AIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENrGKTAMVVDHDIYLIDYISDRLMVFE-GEpgVHGHASG 541
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
3-218 |
5.98e-18 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 82.93 E-value: 5.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 3 EQRTPLVEMKNISISFGGIHAVDDASvDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINgepaeinnPRDAKK 82
Cdd:PRK13409 335 SERETLVEYPDLTKKLGDFSLEVEGG-EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE--------LKISYK 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 83 --YgIETIYQtlavadnvdaaanlylgrelrtpwGTLDDVAMEAKAR--------EVMGRLNPNfQRFKEPVKALSGGQR 152
Cdd:PRK13409 406 pqY-IKPDYD------------------------GTVEDLLRSITDDlgssyyksEIIKPLQLE-RLLDKNVKDLSGGEL 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489631109 153 QSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDI--HDVfdLADRVSV 218
Cdd:PRK13409 460 QRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEErEATALVVDHDIymIDY--ISDRLMV 526
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-225 |
7.38e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 82.57 E-value: 7.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 3 EQRTPLVEMKNISISF--GGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPaeINN-PRD 79
Cdd:PRK11160 333 AADQVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQP--IADySEA 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 80 AKKYGIETIYQ-------TLavadnvdaaanlylgRE-LRTPWGTLDDVAMEAKAREV-MGRLNPNFQRFK----EPVKA 146
Cdd:PRK11160 411 ALRQAISVVSQrvhlfsaTL---------------RDnLLLAAPNASDEALIEVLQQVgLEKLLEDDKGLNawlgEGGRQ 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489631109 147 LSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFlISHDIHDVfDLADRVSVMKNGQVV 225
Cdd:PRK11160 476 LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLM-ITHRLTGL-EQFDRICVMDNGQII 552
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
9-229 |
7.59e-18 |
|
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: 79.38 E-value: 7.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFGG--IHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEpaeinnprDAKKYGIE 86
Cdd:cd03369 7 IEVENLSVRYAPdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGI--------DISTIPLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 87 TIYQTLAVADNVDAaanLYLGrELRT---PWGTLDDVameakarEVMGRLnpnfqRFKEPVKALSGGQRQSVAIARAILF 163
Cdd:cd03369 79 DLRSSLTIIPQDPT---LFSG-TIRSnldPFDEYSDE-------EIYGAL-----RVSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489631109 164 DARILIMDEPTAALGPQETAQVGELIKQLkREGIGIFLISHDIHDVFDLaDRVSVMKNGQVVGHAR 229
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREE-FTNSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDH 206
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
6-224 |
8.32e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 79.86 E-value: 8.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 6 TPLVEMKNISISF--GGIHA--VDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEP---------A 72
Cdd:PRK11629 3 KILLQCDNLCKRYqeGSVQTdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPmsklssaakA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 73 EINNprdaKKYGIetIYQTlavadnvdaaanlylgRELRTPWGTLDDVAM------------EAKAREVMGRLNPNfQRF 140
Cdd:PRK11629 83 ELRN----QKLGF--IYQF----------------HHLLPDFTALENVAMplligkkkpaeiNSRALEMLAAVGLE-HRA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 141 KEPVKALSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQL-KREGIGIFLISHDIHdvfdLADRVS-- 217
Cdd:PRK11629 140 NHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQ----LAKRMSrq 215
|
....*...
gi 489631109 218 -VMKNGQV 224
Cdd:PRK11629 216 lEMRDGRL 223
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
9-239 |
8.80e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 80.61 E-value: 8.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISF--GGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAY-KRDAGEILINGEPAEIN-----NPRDa 80
Cdd:PRK13640 6 VEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlPDDNPNSKITVDGITLTaktvwDIRE- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 81 kKYGIetIYQTLAVAdnvdaaanlYLGRELRtpwgtlDDVAMEAKAREV---------------MGRLNpnFQRfKEPvK 145
Cdd:PRK13640 85 -KVGI--VFQNPDNQ---------FVGATVG------DDVAFGLENRAVprpemikivrdvladVGMLD--YID-SEP-A 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 146 ALSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVfDLADRVSVMKNGQV 224
Cdd:PRK13640 143 NLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEA-NMADQVLVLDDGKL 221
|
250
....*....|....*
gi 489631109 225 VGHARTEDVTKDEVL 239
Cdd:PRK13640 222 LAQGSPVEIFSKVEM 236
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
33-225 |
1.08e-17 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 79.24 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 33 PGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPrdaKKYGIETIYQ--------TLAVADNVDAAANL 104
Cdd:PRK10771 24 RGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPP---SRRPVSMLFQennlfshlTVAQNIGLGLNPGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 105 YLGRELRtpwGTLDDVAMEAKAREVMGRLnPNfqrfkepvkALSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQ 184
Cdd:PRK10771 101 KLNAAQR---EKLHAIARQMGIEDLLARL-PG---------QLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489631109 185 VGELIKQLKRE-GIGIFLISHDIHDVFDLADRVSVMKNGQVV 225
Cdd:PRK10771 168 MLTLVSQVCQErQLTLLMVSHSLEDAARIAPRSLVVADGRIA 209
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-240 |
1.92e-17 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 79.07 E-value: 1.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 1 MTEQRTPLVEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEI------ 74
Cdd:COG4598 1 MTDTAPPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLkpdrdg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 75 -NNPRDAKKygietiyqtlavadnvdaaanlyLGReLRTP----------WG---TLDDVaMEA--------------KA 126
Cdd:COG4598 81 eLVPADRRQ-----------------------LQR-IRTRlgmvfqsfnlWShmtVLENV-IEApvhvlgrpkaeaieRA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 127 REVMGRLNPNFQRFKEPVKaLSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDI 206
Cdd:COG4598 136 EALLAKVGLADKRDAYPAH-LSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEM 214
|
250 260 270
....*....|....*....|....*....|....
gi 489631109 207 HDVFDLADRVSVMKNGQVvgharTEDVTKDEVLG 240
Cdd:COG4598 215 GFARDVSSHVVFLHQGRI-----EEQGPPAEVFG 243
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-233 |
2.02e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 79.31 E-value: 2.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 7 PLVEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDaGEILINGEPAEINNPRDAKKYGIE 86
Cdd:PRK14258 6 PAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGRVEFFNQNIYERRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 87 TIYQTLAVADNVDAAANLYL------GREL--RTPWGTLDDVAMEA-KAREVMGRLNpnfQRFKEPVKALSGGQRQSVAI 157
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMSVydnvayGVKIvgWRPKLEIDDIVESAlKDADLWDEIK---HKIHKSALDLSGGQQQRLCI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 158 ARAILFDARILIMDEPTAALGPQETAQVGELIKQLK-REGIGIFLISHDIHDVFDLADRVSVMKN-----GQVVGHARTE 231
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTK 241
|
..
gi 489631109 232 DV 233
Cdd:PRK14258 242 KI 243
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
10-225 |
2.03e-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: 77.95 E-value: 2.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 10 EMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSG--AYKRDAGEILINGEpaEINN--PRDAKKYGI 85
Cdd:cd03217 2 EIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGE--DITDlpPEERARLGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 86 ETIYQtlavadnvdaaanlylgrelRTPwgtlddvameakarEVMGRLNPNFQRFKEpvKALSGGQRQSVAIARAILFDA 165
Cdd:cd03217 80 FLAFQ--------------------YPP--------------EIPGVKNADFLRYVN--EGFSGGEKKRNEILQLLLLEP 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489631109 166 RILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHdIHDVFDL--ADRVSVMKNGQVV 225
Cdd:cd03217 124 DLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITH-YQRLLDYikPDRVHVLYDGRIV 184
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
9-225 |
4.47e-17 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 80.15 E-value: 4.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFGGIHAV-DDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRdAKKYGIET 87
Cdd:PRK10790 341 IDIDNVSFAYRDDNLVlQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHS-VLRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 88 IYQTlAVADNVDAAANLYLGRELRTP--WGTLDDVAMEAKAREVMGRLNpnfQRFKEPVKALSGGQRQSVAIARAILFDA 165
Cdd:PRK10790 420 VQQD-PVVLADTFLANVTLGRDISEEqvWQALETVQLAELARSLPDGLY---TPLGEQGNNLSVGQKQLLALARVLVQTP 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 166 RILIMDEPTAALGpQETAQVGELIKQLKREGIGIFLISHDIHDVFDlADRVSVMKNGQVV 225
Cdd:PRK10790 496 QILILDEATANID-SGTEQAIQQALAAVREHTTLVVIAHRLSTIVE-ADTILVLHRGQAV 553
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
7-235 |
5.29e-17 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 79.18 E-value: 5.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 7 PLVEMKNISISF----GGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRD----AGEILINGepaeIN--- 75
Cdd:COG4170 2 PLLDIRNLTIEIdtpqGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtADRFRWNG----IDllk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 76 -NPRDAKKY---GIETIYQtlavadnvdaaanlylgrELRT---PWGTLDDVAMEA-KAREVMGRLnpnFQRF---KEPV 144
Cdd:COG4170 78 lSPRERRKIigrEIAMIFQ------------------EPSScldPSAKIGDQLIEAiPSWTFKGKW---WQRFkwrKKRA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 145 KAL--------------------SGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQL-KREGIGIFLIS 203
Cdd:COG4170 137 IELlhrvgikdhkdimnsyphelTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLnQLQGTSILLIS 216
|
250 260 270
....*....|....*....|....*....|..
gi 489631109 204 HDIHDVFDLADRVSVMKNGQVVGHARTEDVTK 235
Cdd:COG4170 217 HDLESISQWADTITVLYCGQTVESGPTEQILK 248
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
23-225 |
5.45e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 78.21 E-value: 5.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 23 AVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILING-EPAEINNPRDAKKYGietiyqtlavadnvdaa 101
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGlDTSDEENLWDIRNKA----------------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 102 anlylGRELRTPWGTL------DDVA-----MEAKAREVMGRLNPNFQRF------KEPVKALSGGQRQSVAIARAILFD 164
Cdd:PRK13633 88 -----GMVFQNPDNQIvativeEDVAfgpenLGIPPEEIRERVDESLKKVgmyeyrRHAPHLLSGGQKQRVAIAGILAMR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489631109 165 ARILIMDEPTAALGPQETAQVGELIKQL-KREGIGIFLISHDIHDVFDlADRVSVMKNGQVV 225
Cdd:PRK13633 163 PECIIFDEPTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEAVE-ADRIIVMDSGKVV 223
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-218 |
6.97e-17 |
|
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: 77.45 E-value: 6.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 30 DLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGE-----PAEInnprDAKKYGieTIYQTLAVADNVDAAANL 104
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDtvsykPQYI----KADYEG--TVRDLLSSITKDFYTHPY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 105 YlgrelRTpwgtldDVAMEAKAREVMGRLNPNfqrfkepvkaLSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQ 184
Cdd:cd03237 95 F-----KT------EIAKPLQIEQILDREVPE----------LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLM 153
|
170 180 190
....*....|....*....|....*....|....*
gi 489631109 185 VGELIKQL-KREGIGIFLISHDIHDVFDLADRVSV 218
Cdd:cd03237 154 ASKVIRRFaENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
24-222 |
8.00e-17 |
|
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: 77.12 E-value: 8.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 24 VDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEpaEINNPRDAKKygieTIYQTLAVADNVDAAAN 103
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGK--QITEPGPDRM----VVFQNYSLLPWLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 104 LYLGRELRTPwgTLDDVAMEAKAREVMGRLNPNFQRFKEPVKaLSGGQRQSVAIARAILFDARILIMDEPTAALGPQETA 183
Cdd:TIGR01184 75 IALAVDRVLP--DLSKSERRAIVEEHIALVGLTEAADKRPGQ-LSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489631109 184 QVGELIKQLKRE-GIGIFLISHDIHDVFDLADRVSVMKNG 222
Cdd:TIGR01184 152 NLQEELMQIWEEhRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
9-224 |
2.24e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 77.76 E-value: 2.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEpaEINNPRDAKKyGIETI 88
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK--RMNDVPPAER-GVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 89 YQTLAVADNVDAAANLYLGRELrtpwgtlddvaMEAKAREVMGRLNPN---------FQRfkEPvKALSGGQRQSVAIAR 159
Cdd:PRK11000 81 FQSYALYPHLSVAENMSFGLKL-----------AGAKKEEINQRVNQVaevlqlahlLDR--KP-KALSGGQRQRVAIGR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489631109 160 AILFDARILIMDEP----TAALGPQETAQVGELIKQLKREGIgifLISHDIHDVFDLADRVSVMKNGQV 224
Cdd:PRK11000 147 TLVAEPSVFLLDEPlsnlDAALRVQMRIEISRLHKRLGRTMI---YVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
147-237 |
3.31e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 76.81 E-value: 3.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 147 LSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVVG 226
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILK 256
|
90
....*....|.
gi 489631109 227 HARTEDVTKDE 237
Cdd:PRK13631 257 TGTPYEIFTDQ 267
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
23-236 |
3.32e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 76.31 E-value: 3.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 23 AVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILI-------NGEPAEINNPRdaKKYGIETIYQTLAVA 95
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivvssTSKQKEIKPVR--KKVGVVFQFPESQLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 96 DNVDAAANLYLGRELRTPWGTLDDVAmeAKAREVMGrLNPNFQRfKEPVKaLSGGQRQSVAIARAILFDARILIMDEPTA 175
Cdd:PRK13643 99 EETVLKDVAFGPQNFGIPKEKAEKIA--AEKLEMVG-LADEFWE-KSPFE-LSGGQMRRVAIAGILAMEPEVLVLDEPTA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489631109 176 ALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTEDVTKD 236
Cdd:PRK13643 174 GLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-233 |
4.23e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 75.90 E-value: 4.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 7 PLVEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILS------GAYkRDAGEILINGEpaEINNPRDA 80
Cdd:PRK14271 20 PAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNrmndkvSGY-RYSGDVLLGGR--SIFNYRDV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 81 KKYG--IETIYQTLAVADNVDAAANLYLGRELR-TPWGTLDDVAmEAKAREVmGRLNPNFQRFKEPVKALSGGQRQSVAI 157
Cdd:PRK14271 97 LEFRrrVGMLFQRPNPFPMSIMDNVLAGVRAHKlVPRKEFRGVA-QARLTEV-GLWDAVKDRLSDSPFRLSGGQQQLLCL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489631109 158 ARAILFDARILIMDEPTAALGPQETAQVGELIKQLKrEGIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTEDV 233
Cdd:PRK14271 175 ARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLA-DRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
8-231 |
4.79e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 75.59 E-value: 4.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 8 LVEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKilsgAYKR--DageiLINGEPAEinnprDAKKYGI 85
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILR----CFNRlnD----LIPGFRVE-----GKVTFHG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 86 ETIYQTLAVADNVDAAANLYLGRELRTPWGTLDDVAMEAKAREVMGRLNPNFQR--------------FKEPVKALSGGQ 151
Cdd:PRK14243 77 KNLYAPDVDPVEVRRRIGMVFQKPNPFPKSIYDNIAYGARINGYKGDMDELVERslrqaalwdevkdkLKQSGLSLSGGQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 152 RQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKREgIGIFLISHDIHDvfdlADRVSVM------------ 219
Cdd:PRK14243 157 QQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQ----AARVSDMtaffnveltegg 231
|
250
....*....|...
gi 489631109 220 -KNGQVVGHARTE 231
Cdd:PRK14243 232 gRYGYLVEFDRTE 244
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
28-199 |
5.12e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 74.14 E-value: 5.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 28 SVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDAkkygietiyqtlavadnvdaaaNLYLG 107
Cdd:PRK13539 22 SFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEA----------------------CHYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 108 -----------RELRTPW----GTLDDVAMEAKARevMGrLNPNFQRfkePVKALSGGQRQSVAIARAILFDARILIMDE 172
Cdd:PRK13539 80 hrnamkpaltvAENLEFWaaflGGEELDIAAALEA--VG-LAPLAHL---PFGYLSAGQKRRVALARLLVSNRPIWILDE 153
|
170 180
....*....|....*....|....*...
gi 489631109 173 PTAALGPQETAQVGELIK-QLKREGIGI 199
Cdd:PRK13539 154 PTAALDAAAVALFAELIRaHLAQGGIVI 181
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
18-231 |
7.87e-16 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 74.14 E-value: 7.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 18 FGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILING-EPAEINN---PRDAKKYGI-------- 85
Cdd:PRK10908 12 LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhDITRLKNrevPFLRRQIGMifqdhhll 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 86 --ETIYQTLAVADNVDAAANLYLGRELRtpwGTLDDVAMEAKARevmgrlnpNFqrfkePVKaLSGGQRQSVAIARAILF 163
Cdd:PRK10908 92 mdRTVYDNVAIPLIIAGASGDDIRRRVS---AALDKVGLLDKAK--------NF-----PIQ-LSGGEQQRVGIARAVVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489631109 164 DARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTE 231
Cdd:PRK10908 155 KPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGGVGGE 222
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
12-209 |
8.94e-16 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 73.67 E-value: 8.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 12 KNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDA---GEILINGEpaEINN-PRDAKKYGIet 87
Cdd:COG4136 5 ENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFsasGEVLLNGR--RLTAlPAEQRRIGI-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 88 IYQTlavadnvdaaANLY----------------LGRELRtpwgtlDDVAMEAKAREVMGRLnpnFQRFkepVKALSGGQ 151
Cdd:COG4136 81 LFQD----------DLLFphlsvgenlafalpptIGRAQR------RARVEQALEEAGLAGF---ADRD---PATLSGGQ 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489631109 152 RQSVAIARAILFDARILIMDEPTAALGPQETAQVGELI-KQLKREGIGIFLISHDIHDV 209
Cdd:COG4136 139 RARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFVfEQIRQRGIPALLVTHDEEDA 197
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
31-225 |
1.54e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 75.65 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 31 LYPGEVVALLGHNGAGKSTLIKILSG--AYKrdaGEILING-EPAEINnprdakkygIETIYQTLAvadnvdaaanlYLG 107
Cdd:PRK11174 373 LPAGQRIALVGPSGAGKTSLLNALLGflPYQ---GSLKINGiELRELD---------PESWRKHLS-----------WVG 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 108 RELRTPWGTL-DDVAM---------------EAKAREVMGRLNPNFQR-FKEPVKALSGGQRQSVAIARAILFDARILIM 170
Cdd:PRK11174 430 QNPQLPHGTLrDNVLLgnpdasdeqlqqaleNAWVSEFLPLLPQGLDTpIGDQAAGLSVGQAQRLALARALLQPCQLLLL 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489631109 171 DEPTAALGPQETAQVGELIKQLKREGIGIfLISHDIHDVFDLaDRVSVMKNGQVV 225
Cdd:PRK11174 510 DEPTASLDAHSEQLVMQALNAASRRQTTL-MVTHQLEDLAQW-DQIWVMQDGQIV 562
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
9-238 |
2.69e-15 |
|
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: 74.84 E-value: 2.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSG--AYKRDAGEILIN----------------GE 70
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYHvalcekcgyverpskvGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 71 P------------AEINNPRDAKKYGIETIYQTLAVADNVDAAANLYLGRELRTpwgtLDDVAMEAK-----AREVMGRL 133
Cdd:TIGR03269 81 PcpvcggtlepeeVDFWNLSDKLRRRIRKRIAIMLQRTFALYGDDTVLDNVLEA----LEEIGYEGKeavgrAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 134 NPNfQRFKEPVKALSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGE-LIKQLKREGIGIFLISHDIHDVFDL 212
Cdd:TIGR03269 157 QLS-HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNaLEEAVKASGISMVLTSHWPEVIEDL 235
|
250 260
....*....|....*....|....*.
gi 489631109 213 ADRVSVMKNGQVVghartEDVTKDEV 238
Cdd:TIGR03269 236 SDKAIWLENGEIK-----EEGTPDEV 256
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
23-250 |
4.95e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 73.12 E-value: 4.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 23 AVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGE--PAEINNPRDAKKYGIET-------IYQTLA 93
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYaiPANLKKIKEVKRLRKEIglvfqfpEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 94 VADNVDAA-ANLYLGRELRTPWGTLDDVAMEAKAREVMGRLNPnFQrfkepvkaLSGGQRQSVAIARAILFDARILIMDE 172
Cdd:PRK13645 106 ETIEKDIAfGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRSP-FE--------LSGGQKRRVALAGIIAMDGNTLVLDE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 173 PTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDLADRVSVMKNGQVVGHART-EDVTKDEVLGMIIMGkvPPK 250
Cdd:PRK13645 177 PTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPfEIFSNQELLTKIEID--PPK 254
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
9-225 |
5.20e-15 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 74.28 E-value: 5.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFGG--IHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGepaeiNNPRDAK----K 82
Cdd:PRK11176 342 IEFRNVTFTYPGkeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDG-----HDLRDYTlaslR 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 83 YGIETIYQTLAVADNVDAAANLYLgrelRTPWGTLDDVAMEAKAREVMGRLNPNFQRFK----EPVKALSGGQRQSVAIA 158
Cdd:PRK11176 417 NQVALVSQNVHLFNDTIANNIAYA----RTEQYSREQIEEAARMAYAMDFINKMDNGLDtvigENGVLLSGGQRQRIAIA 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489631109 159 RAILFDARILIMDEPTAALGPQETAQVGELIKQLKREGIGIfLISHDIHDVfDLADRVSVMKNGQVV 225
Cdd:PRK11176 493 RALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSL-VIAHRLSTI-EKADEILVVEDGEIV 557
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
3-237 |
5.45e-15 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 72.49 E-value: 5.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 3 EQRTPLVEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGE--PAEINNPRDA 80
Cdd:PRK11831 2 QSVANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGEniPAMSRSRLYT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 81 KKYGIETIYQT--LAVADNVDAAANLYLGRELRTPWGTLDDVAM---EAKAREVMGRLNPNfqrfkepvkALSGGQRQSV 155
Cdd:PRK11831 82 VRKRMSMLFQSgaLFTDMNVFDNVAYPLREHTQLPAPLLHSTVMmklEAVGLRGAAKLMPS---------ELSGGMARRA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 156 AIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTEDVT 234
Cdd:PRK11831 153 ALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQ 232
|
...
gi 489631109 235 KDE 237
Cdd:PRK11831 233 ANP 235
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
8-228 |
5.91e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 72.82 E-value: 5.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 8 LVEMKNISISF---GGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDAKKyG 84
Cdd:PRK13642 4 ILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRR-K 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 85 IETIYQTLAVAdnvdaaanlYLGRELRtpwgtlDDVA--MEAKA--REVMGR------LNPNFQRFK--EPVKaLSGGQR 152
Cdd:PRK13642 83 IGMVFQNPDNQ---------FVGATVE------DDVAfgMENQGipREEMIKrvdealLAVNMLDFKtrEPAR-LSGGQK 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489631109 153 QSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLK-REGIGIFLISHDIHDVFDlADRVSVMKNGQVVGHA 228
Cdd:PRK13642 147 QRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKeKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEA 222
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-233 |
6.60e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 72.18 E-value: 6.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILS-----GAYKRDAGEILINGE---PAEINNPRDA 80
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNrllelNEEARVEGEVRLFGRniySPDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 81 KKYGIetIYQTLAVADNVDAAANLYLGRELR---TPWGTLDDV---AMEAKA--REVMGRLNpnfqrfkEPVKALSGGQR 152
Cdd:PRK14267 85 REVGM--VFQYPNPFPHLTIYDNVAIGVKLNglvKSKKELDERvewALKKAAlwDEVKDRLN-------DYPSNLSGGQR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 153 QSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKREgIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTED 232
Cdd:PRK14267 156 QRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRK 234
|
.
gi 489631109 233 V 233
Cdd:PRK14267 235 V 235
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
26-233 |
7.05e-15 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 72.98 E-value: 7.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 26 DASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGE-----PAEINNPRDAKKYGietiyqtlavadnvda 100
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfdaEKGICLPPEKRRIG---------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 101 aanlYLGRELR-----TPWGTL------DDVAMEAKAREVMGrLNPNFQRFkePVkALSGGQRQSVAIARAILFDARILI 169
Cdd:PRK11144 80 ----YVFQDARlfphyKVRGNLrygmakSMVAQFDKIVALLG-IEPLLDRY--PG-SLSGGEKQRVAIGRALLTAPELLL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489631109 170 MDEPTAALG-PQETaqvgELI---KQLKRE-GIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTEDV 233
Cdd:PRK11144 152 MDEPLASLDlPRKR----ELLpylERLAREiNIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
11-233 |
7.82e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 73.74 E-value: 7.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 11 MKNISISF----GGIHAVDDASVDLYPGEVVALLGHNGAGKS----TLIKIL--SGAYKRDAGEILI--NGEPAEINNPR 78
Cdd:PRK10261 15 VENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGLVQCDKMLLRrrSRQVIELSEQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 79 DAKKYGIE-----TIYQTLAVADNVDAAANLYLGRELRTPWGTLDDVAM-EAKAREVMGRLNPNFQRFKEPVKALSGGQR 152
Cdd:PRK10261 95 AAQMRHVRgadmaMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMvEAKRMLDQVRIPEAQTILSRYPHQLSGGMR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 153 QSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTE 231
Cdd:PRK10261 175 QRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVE 254
|
..
gi 489631109 232 DV 233
Cdd:PRK10261 255 QI 256
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-224 |
8.16e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 71.92 E-value: 8.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 1 MTEQRTPLVEMKNisiSFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEpaEINNPRD- 79
Cdd:PRK10619 1 MSENKLNVIDLHK---RYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQ--TINLVRDk 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 80 ------AKKYGIETIYQ--TLAVADNVDAAANLYLGRELRTPWGTLDDVAMEAKAREVMgRLNP----NFQRFKEPVKaL 147
Cdd:PRK10619 76 dgqlkvADKNQLRLLRTrlTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVK-YLAKvgidERAQGKYPVH-L 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489631109 148 SGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQV 224
Cdd:PRK10619 154 SGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-222 |
1.02e-14 |
|
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: 73.89 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 5 RTPLVEMKNISISFGGIH--AVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINnprdakk 82
Cdd:TIGR01257 1934 KTDILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTN------- 2006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 83 ygIETIYQTLAVADNVDAAANLYLGRELRTPWGTLDDVAmeakAREVMGRLNPNFQRFKEPVKA------LSGGQRQSVA 156
Cdd:TIGR01257 2007 --ISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVP----AEEIEKVANWSIQSLGLSLYAdrlagtYSGGNKRKLS 2080
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489631109 157 IARAILFDARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNG 222
Cdd:TIGR01257 2081 TAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
10-217 |
1.32e-14 |
|
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: 70.21 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 10 EMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPrdakkygieTIY 89
Cdd:cd03231 2 EADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRD---------SIA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 90 QTLAVADNVDAAANLYLGRELRTPWGTL--DDVAMEAKAREVMGRLNpnfqrfKEPVKALSGGQRQSVAIARAILFDARI 167
Cdd:cd03231 73 RGLLYLGHAPGIKTTLSVLENLRFWHADhsDEQVEEALARVGLNGFE------DRPVAQLSAGQQRRVALARLLLSGRPL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489631109 168 LIMDEPTAALGPQETAQVGELIKQ-LKREGIGIFLISHDIHDVFDLADRVS 217
Cdd:cd03231 147 WILDEPTTALDKAGVARFAEAMAGhCARGGMVVLTTHQDLGLSEAGARELD 197
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
147-235 |
1.43e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 72.08 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 147 LSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQL-KREGIGIFLISHDIHDVFDLADRVSVMKNGQVV 225
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKIIVMYAGQVV 233
|
90
....*....|
gi 489631109 226 GHARTEDVTK 235
Cdd:PRK11022 234 ETGKAHDIFR 243
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
20-231 |
1.65e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.45 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 20 GIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEinnpRDAKKYGIETIYQT--LAVADN 97
Cdd:PRK15056 19 GHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKNLVAYVPQSeeVDWSFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 98 VDAAANLYLGRELRTPWGTLDDVAMEAKAREVMGRLNPNFQRFKEpVKALSGGQRQSVAIARAILFDARILIMDEPTAAL 177
Cdd:PRK15056 95 VLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQ-IGELSGGQKKRVFLARAIAQQGQVILLDEPFTGV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489631109 178 GPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADrVSVMKNGQVVGHARTE 231
Cdd:PRK15056 174 DVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTE 226
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
9-174 |
2.01e-14 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 72.28 E-value: 2.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILInGEP---AEINNPRDAKKyGI 85
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETvklAYVDQSRDALD-PN 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 86 ETIYQTLAvadnvdaaanlylgrelrtpwGTLDDVAM---EAKAREVMGRLNpnfqrFK-----EPVKALSGGQRQSVAI 157
Cdd:TIGR03719 401 KTVWEEIS---------------------GGLDIIKLgkrEIPSRAYVGRFN-----FKgsdqqKKVGQLSGGERNRVHL 454
|
170
....*....|....*..
gi 489631109 158 ARAILFDARILIMDEPT 174
Cdd:TIGR03719 455 AKTLKSGGNVLLLDEPT 471
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1-242 |
2.19e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 70.79 E-value: 2.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 1 MTEQRTPLvEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRD- 79
Cdd:PRK10253 1 MTESVARL-RGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 80 AKKYGIetIYQTLAVADNVDAAANLYLGR----ELRTPWGTLDDVAMeAKAREVMGRLNPNFQRfkepVKALSGGQRQSV 155
Cdd:PRK10253 80 ARRIGL--LAQNATTPGDITVQELVARGRyphqPLFTRWRKEDEEAV-TKAMQATGITHLADQS----VDTLSGGQRQRA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 156 AIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTEDVT 234
Cdd:PRK10253 153 WIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV 232
|
....*...
gi 489631109 235 KDEVLGMI 242
Cdd:PRK10253 233 TAELIERI 240
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
26-247 |
2.46e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 70.46 E-value: 2.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 26 DASVDLYPGEVVALLGHNGAGKSTLIKILS-------GAYKRDAGEILINGEPAEINNPRDAKKYGIE----------TI 88
Cdd:PRK14246 28 DITIKIPNNSIFGIMGPSGSGKSTLLKVLNrlieiydSKIKVDGKVLYFGKDIFQIDAIKLRKEVGMVfqqpnpfphlSI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 89 YQTLAVADNVDAAANlylGRELRTpwgtlddvAMEAKAREVmGRLNPNFQRFKEPVKALSGGQRQSVAIARAILFDARIL 168
Cdd:PRK14246 108 YDNIAYPLKSHGIKE---KREIKK--------IVEECLRKV-GLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 169 IMDEPTAALGPQETAQVGELIKQLKREgIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTEDV---TKDEVLGMIIMG 245
Cdd:PRK14246 176 LMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIftsPKNELTEKYVIG 254
|
..
gi 489631109 246 KV 247
Cdd:PRK14246 255 RI 256
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
9-223 |
2.58e-14 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 69.42 E-value: 2.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFG-----GIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAeinnprdakky 83
Cdd:cd03250 1 ISVEDASFTWDsgeqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIA----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 84 gietiY--QTlavadnvdaaanlylgrelrtPW---GTLddvameakaRE--VMGRlnP-NFQRFKEPVKA--------- 146
Cdd:cd03250 70 -----YvsQE---------------------PWiqnGTI---------REniLFGK--PfDEERYEKVIKAcalepdlei 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 147 ---------------LSGGQRQSVAIARAILFDARILIMDEPTAALgpqeTAQVG-----ELIKQLKREGIGIFLISHDI 206
Cdd:cd03250 113 lpdgdlteigekginLSGGQKQRISLARAVYSDADIYLLDDPLSAV----DAHVGrhifeNCILGLLLNNKTRILVTHQL 188
|
250
....*....|....*..
gi 489631109 207 HdVFDLADRVSVMKNGQ 223
Cdd:cd03250 189 Q-LLPHADQIVVLDNGR 204
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
33-219 |
2.83e-14 |
|
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: 72.12 E-value: 2.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 33 PGEVVALLGHNGAGKSTLIKILSGAYKRDAGEIlinGEPAEINnprDAKKY--GIEtIYQTLAVadnvdaaanLYLGrEL 110
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDY---DEEPSWD---EVLKRfrGTE-LQDYFKK---------LANG-EI 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 111 R-----------------TPWGTLDDVAMEAKAREVMGRLN--PNFQRfkePVKALSGGQRQSVAIARAILFDARILIMD 171
Cdd:COG1245 161 KvahkpqyvdlipkvfkgTVRELLEKVDERGKLDELAEKLGleNILDR---DISELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489631109 172 EPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHdVFD-LADRVSVM 219
Cdd:COG1245 238 EPSSYLDIYQRLNVARLIRELAEEGKYVLVVEHDLA-ILDyLADYVHIL 285
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
8-205 |
4.81e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 71.52 E-value: 4.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 8 LVEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPA----EINNPRDAKky 83
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIvarlQQDPPRNVE-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 84 giETIYQTLAVADNVdaaanlyLGRELRTPWGTLDDVAME---------AKAREVM---------GRLNPNFQRFK---- 141
Cdd:PRK11147 81 --GTVYDFVAEGIEE-------QAEYLKRYHDISHLVETDpseknlnelAKLQEQLdhhnlwqleNRINEVLAQLGldpd 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489631109 142 EPVKALSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKreGIGIFlISHD 205
Cdd:PRK11147 152 AALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQ--GSIIF-ISHD 212
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
25-225 |
5.47e-14 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 71.00 E-value: 5.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 25 DDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEpaeinNPRDAKK------YGI---------ETIY 89
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQ-----DIRDVTQaslraaIGIvpqdtvlfnDTIA 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 90 QTLAvadnvdaaanlYlGRelrtPWGTLDDVAMEAKAREVMG---RLnPnfQRFKEPV-----KaLSGGQRQSVAIARAI 161
Cdd:COG5265 450 YNIA-----------Y-GR----PDASEEEVEAAARAAQIHDfieSL-P--DGYDTRVgerglK-LSGGEKQRVAIARTL 509
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489631109 162 LFDARILIMDEPTAALgpqETAQVGELIKQLKREGIG--IFLISHDIHDVFDlADRVSVMKNGQVV 225
Cdd:COG5265 510 LKNPPILIFDEATSAL---DSRTERAIQAALREVARGrtTLVIAHRLSTIVD-ADEILVLEAGRIV 571
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
22-204 |
7.35e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 68.83 E-value: 7.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 22 HAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNprdaKKYGIETIYqtlavadnvdaa 101
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGR----EASLIDAIG------------ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 102 anlylgrelrtPWGTLDDvAMEAKARevMGrLNPNFQrFKEPVKALSGGQRQSVAIARAILFDARILIMDEPTAALGPQe 181
Cdd:COG2401 108 -----------RKGDFKD-AVELLNA--VG-LSDAVL-WLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ- 170
|
170 180
....*....|....*....|....*
gi 489631109 182 TAQVGELI--KQLKREGIGIFLISH 204
Cdd:COG2401 171 TAKRVARNlqKLARRAGITLVVATH 195
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
10-225 |
8.86e-14 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 68.94 E-value: 8.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 10 EMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSG--AYKRDAGEILINGE----------------- 70
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSILLDGEdilelspderaragifl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 71 ----PAEInnPrdakkyGIETIYQtlavadnvdaaanlylgreLRT-----PWGTLDDVAMEAKAREVMGRL--NPNF-Q 138
Cdd:COG0396 82 afqyPVEI--P------GVSVSNF-------------------LRTalnarRGEELSAREFLKLLKEKMKELglDEDFlD 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 139 RfkePVKA-LSGGQRQSVAIARAILFDARILIMDEPTA-----ALGPqetaqVGELIKQLKREGIGIFLISH------DI 206
Cdd:COG0396 135 R---YVNEgFSGGEKKRNEILQMLLLEPKLAILDETDSgldidALRI-----VAEGVNKLRSPDRGILIITHyqrildYI 206
|
250
....*....|....*....
gi 489631109 207 HdvfdlADRVSVMKNGQVV 225
Cdd:COG0396 207 K-----PDFVHVLVDGRIV 220
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
10-205 |
1.07e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 70.36 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 10 EMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEIlingepaeinnprdakKYG--IET 87
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI----------------HCGtkLEV 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 88 IY--QTlavadnvdaaanlylgRELRTPWGTLDD--------VAMEAKAREVMGRLNpNF----QRFKEPVKALSGGQRQ 153
Cdd:PRK11147 385 AYfdQH----------------RAELDPEKTVMDnlaegkqeVMVNGRPRHVLGYLQ-DFlfhpKRAMTPVKALSGGERN 447
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489631109 154 SVAIARAILFDARILIMDEPTAALGpQETAqvgELIKQLKREGIG-IFLISHD 205
Cdd:PRK11147 448 RLLLARLFLKPSNLLILDEPTNDLD-VETL---ELLEELLDSYQGtVLLVSHD 496
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
24-242 |
1.13e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 70.20 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 24 VDDASVDLYPGEVVALLGHNGAGKSTLIKILSG-AYKRD-AGEILINGEPAEINNPRDA------------KKYG---IE 86
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGrSYGRNiSGTVFKDGKEVDVSTVSDAidaglayvtedrKGYGlnlID 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 87 TIYQTLAVADnvdaaanlyLGRELRtpWGTLDDVAMEAKAREVMGRLN---PNFQrfkEPVKALSGGQRQSVAIARAILF 163
Cdd:NF040905 356 DIKRNITLAN---------LGKVSR--RGVIDENEEIKVAEEYRKKMNiktPSVF---QKVGNLSGGNQQKVVLSKWLFT 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 164 DARILIMDEPTAALgpqetaQVG------ELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTEDVTKDE 237
Cdd:NF040905 422 DPDVLILDEPTRGI------DVGakyeiyTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRITGELPREEASQER 495
|
....*
gi 489631109 238 VLGMI 242
Cdd:NF040905 496 IMRLI 500
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
25-225 |
3.40e-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: 3.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 25 DDASVDLYPGEVVALLGHNGAGKSTLIKILSGayKRDA----GEILINGEPAEINNPRdakkygiETIY--Qtlavadnv 98
Cdd:cd03232 24 NNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAgvitGEILINGRPLDKNFQR-------STGYveQ-------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 99 daaanlylgrelrtpwgtLDDVAMEAKAREVMgrlnpnfqRFKEPVKALSGGQRQSVAIARAILFDARILIMDEPTAALG 178
Cdd:cd03232 87 ------------------QDVHSPNLTVREAL--------RFSALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489631109 179 PQETAQVGELIKQLKREGIGIfLIShdIH----DVFDLADRVSVMK-NGQVV 225
Cdd:cd03232 141 SQAAYNIVRFLKKLADSGQAI-LCT--IHqpsaSIFEKFDRLLLLKrGGKTV 189
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
9-225 |
1.59e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 66.84 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINgEPAEINN-PRDAKKYGIET 87
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWS-ENANIGYyAQDHAYDFEND 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 88 IyqTLAvadnvdaaanlylgrELRTPWGTLDDvaMEAKAREVMGRLNPNFQRFKEPVKALSGGQRQSVAIARAILFDARI 167
Cdd:PRK15064 399 L--TLF---------------DWMSQWRQEGD--DEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNV 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489631109 168 LIMDEPTAALGPqetaqvgELIKQL-----KREGIGIFlISHDIHDVFDLADRVSVMKNGQVV 225
Cdd:PRK15064 460 LVMDEPTNHMDM-------ESIESLnmaleKYEGTLIF-VSHDREFVSSLATRIIEITPDGVV 514
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
33-205 |
1.73e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 64.80 E-value: 1.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 33 PGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRD-----AKKYGIetIYQTLAVADNVDAAANLYLG 107
Cdd:PRK10584 35 RGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEAraklrAKHVGF--VFQSFMLIPTLNALENVELP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 108 RELRTPwgtlDDVAMEAKAREVMGRLNPNfQRFKEPVKALSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGE 187
Cdd:PRK10584 113 ALLRGE----SSRQSRNGAKALLEQLGLG-KRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIAD 187
|
170
....*....|....*....
gi 489631109 188 LIKQLKRE-GIGIFLISHD 205
Cdd:PRK10584 188 LLFSLNREhGTTLILVTHD 206
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
24-216 |
2.08e-12 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 66.37 E-value: 2.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 24 VDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILIngepaeinnPRDAKkygietiyqtlavadnvdaaaN 103
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR---------PAGAR---------------------V 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 104 LYLGRELRTPWGTLDDV--------AM-EAKAREVMGRLN-PNF-QRFKEPV---KALSGGQRQSVAIARAILFDARILI 169
Cdd:COG4178 429 LFLPQRPYLPLGTLREAllypataeAFsDAELREALEAVGlGHLaERLDEEAdwdQVLSLGEQQRLAFARLLLHKPDWLF 508
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489631109 170 MDEPTAALGPqETAQvgELIKQLKRE--GIGIFLISHDiHDVFDLADRV 216
Cdd:COG4178 509 LDEATSALDE-ENEA--ALYQLLREElpGTTVISVGHR-STLAAFHDRV 553
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
22-236 |
2.12e-12 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 65.22 E-value: 2.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 22 HAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPA--EINNPRDAKKYGIETIyqtlavadnvd 99
Cdd:PRK13546 38 FALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSviAISAGLSGQLTGIENI----------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 100 aaanlylgrELRTpwgtlddVAMEAKAREVMgRLNPNFQRFKE-------PVKALSGGQRQSVAIARAILFDARILIMDE 172
Cdd:PRK13546 107 ---------EFKM-------LCMGFKRKEIK-AMTPKIIEFSElgefiyqPVKKYSSGMRAKLGFSINITVNPDILVIDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489631109 173 pTAALGPQETAQVG-ELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTEDVTKD 236
Cdd:PRK13546 170 -ALSVGDQTFAQKClDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
9-174 |
3.23e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 65.91 E-value: 3.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILInGEPAEI---NNPRDA---KK 82
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVKLayvDQSRDAldpNK 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 83 ygieTIYQTLAvadnvdaaanlylgrelrtpwGTLDDVAM---EAKAREVMGRLNpnfqrFK-----EPVKALSGGQRQS 154
Cdd:PRK11819 404 ----TVWEEIS---------------------GGLDIIKVgnrEIPSRAYVGRFN-----FKggdqqKKVGVLSGGERNR 453
|
170 180
....*....|....*....|
gi 489631109 155 VAIARAILFDARILIMDEPT 174
Cdd:PRK11819 454 LHLAKTLKQGGNVLLLDEPT 473
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
33-219 |
3.90e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.60 E-value: 3.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 33 PGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEInnprdAKKY-GIE--TIYQTLAVADNVDAAANLYL--- 106
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPSWDEV-----LKRFrGTElqNYFKKLYNGEIKVVHKPQYVdli 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 107 -------GREL------RtpwGTLDDVAMEAKAREVMGRlnpnfqrfkePVKALSGGQRQSVAIARAILFDARILIMDEP 173
Cdd:PRK13409 173 pkvfkgkVRELlkkvdeR---GKLDEVVERLGLENILDR----------DISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489631109 174 TAALGPQETAQVGELIKQLKrEGIGIFLISHDIHdVFD-LADRVSVM 219
Cdd:PRK13409 240 TSYLDIRQRLNVARLIRELA-EGKYVLVVEHDLA-VLDyLADNVHIA 284
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
31-237 |
4.83e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 65.77 E-value: 4.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 31 LYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGepaeinnpRDAKKYGIETIYQTLavaDNVDAAANLYLG--R 108
Cdd:PLN03232 1259 VSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDD--------CDVAKFGLTDLRRVL---SIIPQSPVLFSGtvR 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 109 ELRTPWGTLDDV----AME-AKAREVMGRlNP---NFQRFkEPVKALSGGQRQSVAIARAILFDARILIMDEPTAALgpq 180
Cdd:PLN03232 1328 FNIDPFSEHNDAdlweALErAHIKDVIDR-NPfglDAEVS-EGGENFSVGQRQLLSLARALLRRSKILVLDEATASV--- 1402
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 181 eTAQVGELIKQLKRE---GIGIFLISHDIHDVFDlADRVSVMKNGQVVGHARTEDVTKDE 237
Cdd:PLN03232 1403 -DVRTDSLIQRTIREefkSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRD 1460
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
6-225 |
8.93e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 63.12 E-value: 8.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 6 TPLVEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSG--AYKRDAGEILINGEPAEINNPRDAKKY 83
Cdd:CHL00131 5 KPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERAHL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 84 GI-------------------ETIYQTLAVADNVDAAANLYLgRELRTPwgTLDDVAMEAK--AREVmgrlNPNFqrfke 142
Cdd:CHL00131 85 GIflafqypieipgvsnadflRLAYNSKRKFQGLPELDPLEF-LEIINE--KLKLVGMDPSflSRNV----NEGF----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 143 pvkalSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHdIHDVFD--LADRVSVMK 220
Cdd:CHL00131 153 -----SGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH-YQRLLDyiKPDYVHVMQ 226
|
....*
gi 489631109 221 NGQVV 225
Cdd:CHL00131 227 NGKII 231
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
6-224 |
2.13e-11 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 63.65 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 6 TPLVEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILIngepaeinnprdAKkyGI 85
Cdd:PRK10636 310 NPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL------------AK--GI 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 86 ETIYqtlavadnvDAAANLYLGRELRTPWGTLDDVA---MEAKAREVMGRLNPNFQRFKEPVKALSGGQRQSVAIARAIL 162
Cdd:PRK10636 376 KLGY---------FAQHQLEFLRADESPLQHLARLApqeLEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVW 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489631109 163 FDARILIMDEPTAALGPQETAQVGELIkqLKREGiGIFLISHDIHDVFDLADRVSVMKNGQV 224
Cdd:PRK10636 447 QRPNLLLLDEPTNHLDLDMRQALTEAL--IDFEG-ALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
19-224 |
2.32e-11 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 62.94 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 19 GGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILING------EPAEinnpRDakkygIETIYQTL 92
Cdd:PRK11650 15 GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGrvvnelEPAD----RD-----IAMVFQNY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 93 AvadnvdaaanLY--------LGRELR---TPWGTLDD-VAMEAKAREvmgrLNPNFQRfkEPvKALSGGQRQSVAIARA 160
Cdd:PRK11650 86 A----------LYphmsvrenMAYGLKirgMPKAEIEErVAEAARILE----LEPLLDR--KP-RELSGGQRQRVAMGRA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489631109 161 ILFDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHDIHDVFDLADRVSVMKNGQV 224
Cdd:PRK11650 149 IVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRlKTTSLYVTHDQVEAMTLADRVVVMNGGVA 213
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
24-204 |
2.87e-11 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 60.25 E-value: 2.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 24 VDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILIngepaeinnPRDAKkygietiyqtlavadnvdaaaN 103
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------PEGED---------------------L 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 104 LYLGRELRTPWGTLddvameakaREVMGRlnpnfqrfkeP-VKALSGGQRQSVAIARAILFDARILIMDEPTAALGPQET 182
Cdd:cd03223 67 LFLPQRPYLPLGTL---------REQLIY----------PwDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESE 127
|
170 180
....*....|....*....|..
gi 489631109 183 AQvgeLIKQLKREGIGIFLISH 204
Cdd:cd03223 128 DR---LYQLLKELGITVISVGH 146
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
24-216 |
3.01e-11 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 63.27 E-value: 3.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 24 VDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEIL---------INGEPAEINNPrdAKKYGIETIYQTLAV 94
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTfpgnwqlawVNQETPALPQP--ALEYVIDGDREYRQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 95 ADNVDAAANLYLGRELRTPWGTLDDV---AMEAKAREVMGRLNPNFQRFKEPVKALSGGQRQSVAIARAILFDARILIMD 171
Cdd:PRK10636 95 EAQLHDANERNDGHAIATIHGKLDAIdawTIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLD 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489631109 172 EPTAALgpqETAQVGELIKQLKREGIGIFLISHDiHDVFD-LADRV 216
Cdd:PRK10636 175 EPTNHL---DLDAVIWLEKWLKSYQGTLILISHD-RDFLDpIVDKI 216
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
33-225 |
5.79e-11 |
|
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: 60.35 E-value: 5.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 33 PGEVVALLGHNGAGKSTLIKILSGA---YKRDAGEILINGEPAEINnprdAKKYGIETIYQtlavadnvdaaanlylgre 109
Cdd:cd03233 32 PGEMVLVLGRPGSGCSTLLKALANRtegNVSVEGDIHYNGIPYKEF----AEKYPGEIIYV------------------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 110 lrtpwgTLDDVAM-EAKAREVM---GRLNPNfqrfkEPVKALSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQV 185
Cdd:cd03233 89 ------SEEDVHFpTLTVRETLdfaLRCKGN-----EFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489631109 186 GELIKQLKRE--GIGIFLISHDIHDVFDLADRVSVMKNGQVV 225
Cdd:cd03233 158 LKCIRTMADVlkTTTFVSLYQASDEIYDLFDKVLVLYEGRQI 199
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
33-204 |
6.27e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 60.25 E-value: 6.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 33 PGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNPRDAKKY--GIETIYQTLAVADNVDAAANLYLGREL 110
Cdd:PRK13543 36 AGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYlgHLPGLKADLSTLENLHFLCGLHGRRAK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 111 RTPWGTLDDVAMEAKAREVmgrlnpnfqrfkepVKALSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIK 190
Cdd:PRK13543 116 QMPGSALAIVGLAGYEDTL--------------VRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMIS 181
|
170
....*....|....
gi 489631109 191 QLKREGIGIFLISH 204
Cdd:PRK13543 182 AHLRGGGAALVTTH 195
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
33-225 |
9.59e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 61.66 E-value: 9.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 33 PGEVVALLGHNGAGKSTLIKILS----GAYKRDAGEILING-EPAEInnprdAKKYGIETIY--QTLAVADNVDAAANLY 105
Cdd:TIGR00956 86 PGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGiTPEEI-----KKHYRGDVVYnaETDVHFPHLTVGETLD 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 106 LGRELRTPWGTLDDVAMEAKAREVMG--------RLNPNFQRFKEPVKALSGGQRQSVAIARAILFDARILIMDEPTAAL 177
Cdd:TIGR00956 161 FAARCKTPQNRPDGVSREEYAKHIADvymatyglSHTRNTKVGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGL 240
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489631109 178 gpqETAQVGELIKQLKREG--------IGIFLISHDIHDVFdlaDRVSVMKNGQVV 225
Cdd:TIGR00956 241 ---DSATALEFIRALKTSAnildttplVAIYQCSQDAYELF---DKVIVLYEGYQI 290
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
23-225 |
1.07e-10 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 61.27 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 23 AVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPaeINNPR-DAKKYGIETIYQTlAVADNVDAA 101
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIP--LTKLQlDSWRSRLAVVSQT-PFLFSDTVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 102 ANLYLGRELRTPwGTLDDVAMEAKAREVMGRLNPNFQ-RFKEPVKALSGGQRQSVAIARAILFDARILIMDEPTAALGPQ 180
Cdd:PRK10789 407 NNIALGRPDATQ-QEIEHVARLASVHDDILRLPQGYDtEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGR 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489631109 181 ETAQVGELIKQLkREGIGIFLISHDIHDVFDlADRVSVMKNGQVV 225
Cdd:PRK10789 486 TEHQILHNLRQW-GEGRTVIISAHRLSALTE-ASEILVMQHGHIA 528
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-219 |
1.07e-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: 60.07 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 33 PGEVVALLGHNGAGKSTLIKILSGAYKRDAG---------EILINGEPAEINN-----PRDAKKYGIETIYQTLAVADNV 98
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGkfddppdwdEILDEFRGSELQNyftklLEGDVKVIVKPQYVDLIPKAVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 99 DAAANLYLGRELRtpwGTLDDVAMEAKAREVMGRlnpnfqrfkePVKALSGGQRQSVAIARAILFDARILIMDEPTAALG 178
Cdd:cd03236 105 GKVGELLKKKDER---GKLDELVDQLELRHVLDR----------NIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489631109 179 PQETAQVGELIKQLKREGIGIFLISHDIhDVFD-LADRVSVM 219
Cdd:cd03236 172 IKQRLNAARLIRELAEDDNYVLVVEHDL-AVLDyLSDYIHCL 212
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
28-237 |
1.17e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 61.68 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 28 SVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGepaeinnpRDAKKYGIETIYQTLAVADNVDAaanLYLG 107
Cdd:PLN03130 1259 SFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDG--------CDISKFGLMDLRKVLGIIPQAPV---LFSG 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 108 --RELRTPWGTLDDV----AME-AKAREVMgRLNP------------NFqrfkepvkalSGGQRQSVAIARAILFDARIL 168
Cdd:PLN03130 1328 tvRFNLDPFNEHNDAdlweSLErAHLKDVI-RRNSlgldaevseageNF----------SVGQRQLLSLARALLRRSKIL 1396
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489631109 169 IMDEPTAALGPQETAqvgeLIKQLKRE---GIGIFLISHDIHDVFDlADRVSVMKNGQVVGHARTEDVTKDE 237
Cdd:PLN03130 1397 VLDEATAAVDVRTDA----LIQKTIREefkSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLSNE 1463
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-194 |
5.93e-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: 5.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 19 GGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDaGEILING---EPAEINNPRdaKKYGI--ETIYQTLA 93
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGvswNSVTLQTWR--KAFGVipQKVFIFSG 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 94 VADNVDAAANLYLGRELrtpWGTLDDVAMEAKAREVMGRLNpnFQrFKEPVKALSGGQRQSVAIARAILFDARILIMDEP 173
Cdd:TIGR01271 1307 TFRKNLDPYEQWSDEEI---WKVAEEVGLKSVIEQFPDKLD--FV-LVDGGYVLSNGHKQLMCLARSILSKAKILLLDEP 1380
|
170 180
....*....|....*....|.
gi 489631109 174 TAALGPQeTAQVgeLIKQLKR 194
Cdd:TIGR01271 1381 SAHLDPV-TLQI--IRKTLKQ 1398
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
24-204 |
4.57e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 54.96 E-value: 4.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 24 VDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEpaEINNPRDAkkygietiYQTLAVADNVDAAAN 103
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQ--SIKKDLCT--------YQKQLCFVGHRSGIN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 104 LYLgrELRTpwGTLDDVAMEAKAREV--MGRLNPNFQRFKEPVKALSGGQRQSVAIARAILFDARILIMDEPTAALGPQE 181
Cdd:PRK13540 87 PYL--TLRE--NCLYDIHFSPGAVGIteLCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS 162
|
170 180
....*....|....*....|...
gi 489631109 182 TAQVGELIKQLKREGIGIFLISH 204
Cdd:PRK13540 163 LLTIITKIQEHRAKGGAVLLTSH 185
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
33-223 |
8.86e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 55.66 E-value: 8.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 33 PGEVVALLGHNGAGKSTLIKILSGAYKRD--AGEILING-EPAEINNPR------DAKKYGIETIYQTLAVADNVDAAAN 103
Cdd:PLN03211 93 PGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNrKPTKQILKRtgfvtqDDILYPHLTVRETLVFCSLLRLPKS 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 104 LYLGRELRTPWGTLDDVAMEAKAREVMGRlnpNFqrfkepVKALSGGQRQSVAIARAILFDARILIMDEPTAALGPQETA 183
Cdd:PLN03211 173 LTKQEKILVAESVISELGLTKCENTIIGN---SF------IRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAY 243
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489631109 184 QVGELIKQLKREGIGIFLISHDIHD-VFDLADRVSVMKNGQ 223
Cdd:PLN03211 244 RLVLTLGSLAQKGKTIVTSMHQPSSrVYQMFDSVLVLSEGR 284
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
9-224 |
1.42e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 55.34 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISF--GGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGepaeINnprdAKKYGIE 86
Cdd:TIGR00957 1285 VEFRNYCLRYreDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG----LN----IAKIGLH 1356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 87 TIYQTLAVADNVDAaanLYLGrELRT---PWGTLDD----VAMEAKAREVMGRLNPNFQRFK--EPVKALSGGQRQSVAI 157
Cdd:TIGR00957 1357 DLRFKITIIPQDPV---LFSG-SLRMnldPFSQYSDeevwWALELAHLKTFVSALPDKLDHEcaEGGENLSVGQRQLVCL 1432
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489631109 158 ARAILFDARILIMDEPTAALGpQETAQVGELIKQLKREGIGIFLISHDIHDVFDLAdRVSVMKNGQV 224
Cdd:TIGR00957 1433 ARALLRKTKILVLDEATAAVD-LETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEV 1497
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
9-233 |
1.53e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 54.74 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAG--KSTLIKILSGAykrDAGEILINGEPAEINNPRDAKKYGIE 86
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GP---DAGRRPWRF*TWCANRRALRRTIG*H 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 87 TIYQTLAVADNVDAAANLYLGRELrtpwgTLDDVAMEAKAREVMGRLNPNFQRFKEPVKaLSGGQRQSVAIARAILFDAR 166
Cdd:NF000106 91 RPVR*GRRESFSGRENLYMIGR*L-----DLSRKDARARADELLERFSLTEAAGRAAAK-YSGGMRRRLDLAASMIGRPA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489631109 167 ILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTEDV 233
Cdd:NF000106 165 VLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
9-224 |
1.72e-08 |
|
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: 54.09 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISF--GGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDaGEILINGEP-AEINNPRDAKKYGI 85
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSwNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 86 etIYQTLAvadnvdaaanLYLG--RELRTPWGTLDD-----VAMEAKAREVM----GRLNpnFQrFKEPVKALSGGQRQS 154
Cdd:cd03289 82 --IPQKVF----------IFSGtfRKNLDPYGKWSDeeiwkVAEEVGLKSVIeqfpGQLD--FV-LVDGGCVLSHGHKQL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489631109 155 VAIARAILFDARILIMDEPTAALGPQeTAQVgeLIKQLKR--EGIGIFLISHDIHDVFDlADRVSVMKNGQV 224
Cdd:cd03289 147 MCLARSVLSKAKILLLDEPSAHLDPI-TYQV--IRKTLKQafADCTVILSEHRIEAMLE-CQRFLVIEENKV 214
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
145-239 |
2.09e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 54.65 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 145 KALSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLK-REGIGIFLISHDIHDVfDLADRVSVMKNGQ 223
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdKADKTIITIAHRIASI-KRSDKIVVFNNPD 1435
|
90
....*....|....*.
gi 489631109 224 VVGHARTEDVTKDEVL 239
Cdd:PTZ00265 1436 RTGSFVQAHGTHEELL 1451
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
33-215 |
2.17e-08 |
|
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: 51.99 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 33 PGEVVALLGHNGAGKSTLIKILSGAYKRD-AGEILINGEPAEINNPRDAKKYGIetiyqtlavadnvdaaanlylgrelr 111
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPgGGVIYIDGEDILEEVLDQLLLIIV-------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 112 tpwgtlddvameakarevmgrlnpnfqrfKEPVKALSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQV------ 185
Cdd:smart00382 55 -----------------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLllleel 105
|
170 180 190
....*....|....*....|....*....|
gi 489631109 186 GELIKQLKREGIGIFLISHDIHDVFDLADR 215
Cdd:smart00382 106 RLLLLLKSEKNLTVILTTNDEKDLGPALLR 135
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
22-233 |
2.81e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 54.13 E-value: 2.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 22 HAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPA--EINNPRDAKKYGIETIyqtlavadnvd 99
Cdd:PRK13545 38 YALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAAliAISSGLNGQLTGIENI----------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 100 aaanlylgrELRTpwgtlddvAMEAKAREVMGRLNPNFQRFKE-------PVKALSGGQRQSVAIARAILFDARILIMDE 172
Cdd:PRK13545 107 ---------ELKG--------LMMGLTKEKIKEIIPEIIEFADigkfiyqPVKTYSSGMKSRLGFAISVHINPDILVIDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489631109 173 pTAALGPQE-TAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNGQVVGHARTEDV 233
Cdd:PRK13545 170 -ALSVGDQTfTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEV 230
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
9-236 |
4.88e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.49 E-value: 4.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFGGIHAVD---DASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILING---------------- 69
Cdd:PTZ00265 383 IQFKNVRFHYDTRKDVEiykDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlkdinlkwwrski 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 70 -----EPAEINNP-RDAKKYGI------ETIYQTLAVADNVDAAANLYLGRELRTPWGTLDDVAMEAKAREVMgRLNPNF 137
Cdd:PTZ00265 463 gvvsqDPLLFSNSiKNNIKYSLyslkdlEALSNYYNEDGNDSQENKNKRNSCRAKCAGDLNDMSNTTDSNELI-EMRKNY 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 138 QRFKE-------------------PVK----------ALSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGEL 188
Cdd:PTZ00265 542 QTIKDsevvdvskkvlihdfvsalPDKyetlvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 489631109 189 IKQLK-REGIGIFLISHDI------HDVFDLADRvsvMKNGQVVGHARTEDVTKD 236
Cdd:PTZ00265 622 INNLKgNENRITIIIAHRLstiryaNTIFVLSNR---ERGSTVDVDIIGEDPTKD 673
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
30-218 |
7.07e-08 |
|
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: 51.03 E-value: 7.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 30 DLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEIlingepaeinnprdakkygietiyqtlavadnvdaaanlylgre 109
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDND-------------------------------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 110 lrtpwgTLDDVAMEAKAREVmgrlnpnfqrfkepvkALSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELI 189
Cdd:cd03222 57 ------EWDGITPVYKPQYI----------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAI 114
|
170 180 190
....*....|....*....|....*....|
gi 489631109 190 KQLKREGI-GIFLISHDIHDVFDLADRVSV 218
Cdd:cd03222 115 RRLSEEGKkTALVVEHDLAVLDYLSDRIHV 144
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
11-174 |
8.75e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 52.63 E-value: 8.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 11 MKNISISFggihavddasvdlYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILIN---------GEPaEINNPRDAK 81
Cdd:TIGR03719 21 LKDISLSF-------------FPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQpgikvgylpQEP-QLDPTKTVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 82 KYGIETIYQTLAVADNVDAAANLY---------LGREL---------RTPWgTLD---DVAMEAKarevmgRLNPNFQrf 140
Cdd:TIGR03719 87 ENVEEGVAEIKDALDRFNEISAKYaepdadfdkLAAEQaelqeiidaADAW-DLDsqlEIAMDAL------RCPPWDA-- 157
|
170 180 190
....*....|....*....|....*....|....
gi 489631109 141 kePVKALSGGQRQSVAIARAILFDARILIMDEPT 174
Cdd:TIGR03719 158 --DVTKLSGGERRRVALCRLLLSKPDMLLLDEPT 189
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
7-224 |
2.28e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 51.28 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 7 PLVEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEINNpRDAKK---- 82
Cdd:NF033858 265 PAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGD-IATRRrvgy 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 83 -------YGIETIYQTLavadnvdaaanlylgrEL-----RTPwgtlddvAMEAKAR--EVMgrlnpnfQRFK-EPVK-- 145
Cdd:NF033858 344 msqafslYGELTVRQNL----------------ELharlfHLP-------AAEIAARvaEML-------ERFDlADVAda 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 146 ---ALSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKRE-GIGIFLISHdihdvF----DLADRVS 217
Cdd:NF033858 394 lpdSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREdGVTIFISTH-----FmneaERCDRIS 468
|
....*..
gi 489631109 218 VMKNGQV 224
Cdd:NF033858 469 LMHAGRV 475
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
130-216 |
3.31e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 50.98 E-value: 3.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 130 MGRLNPNfqrfkEPVKALSGGQRQSVAIAR---AILFDArILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDi 206
Cdd:PRK00635 465 LPYLTPE-----RALATLSGGEQERTALAKhlgAELIGI-TYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD- 537
|
90
....*....|
gi 489631109 207 HDVFDLADRV 216
Cdd:PRK00635 538 EQMISLADRI 547
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
37-224 |
4.10e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.63 E-value: 4.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 37 VALLGHNGAGKSTLIKILSGAYKRDAGEILingepaeinnpRDAKkYGIETIYQTLAVADNVDAAANLYLGRELRTpwgt 116
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTVF-----------RSAK-VRMAVFSQHHVDGLDLSSNPLLYMMRCFPG---- 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 117 lddvAMEAKAREVMGRLNPNFQRFKEPVKALSGGQRQSVAIARAILFDARILIMDEPTAALgpqETAQVGELIKQLKREG 196
Cdd:PLN03073 602 ----VPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHL---DLDAVEALIQGLVLFQ 674
|
170 180
....*....|....*....|....*...
gi 489631109 197 IGIFLISHDIHDVFDLADRVSVMKNGQV 224
Cdd:PLN03073 675 GGVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
9-177 |
5.10e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.24 E-value: 5.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIK---------------------------------ILS 55
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRymamhaidgipkncqilhveqevvgddttalqcVLN 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 56 GAYKRD---AGEILINGEPAEINNPRDAKKYGIETIyQTLAVADNVDAAANLYLGRELrtpwgtLDDVAMEAKAREVMGR 132
Cdd:PLN03073 258 TDIERTqllEEEAQLVAQQRELEFETETGKGKGANK-DGVDKDAVSQRLEEIYKRLEL------IDAYTAEARAASILAG 330
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489631109 133 LN--PNFQRFKepVKALSGGQRQSVAIARAILFDARILIMDEPTAAL 177
Cdd:PLN03073 331 LSftPEMQVKA--TKTFSGGWRMRIALARALFIEPDLLLLDEPTNHL 375
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
6-196 |
1.81e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.47 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 6 TPLVEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSG----AY---------KRDAGEILIngepa 72
Cdd:PRK10938 258 EPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqGYsndltlfgrRRGSGETIW----- 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 73 einnprDAKK------------YGIET---------------IYQTLAVadnvdaaanlylgrelrtpwgtlddvAMEAK 125
Cdd:PRK10938 333 ------DIKKhigyvssslhldYRVSTsvrnvilsgffdsigIYQAVSD--------------------------RQQKL 380
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489631109 126 AREVMGRLNPNFQRFKEPVKALSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKREG 196
Cdd:PRK10938 381 AQQWLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEG 451
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
9-65 |
1.87e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 48.58 E-value: 1.87e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 489631109 9 VEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEI 65
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRV 58
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
143-238 |
2.63e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.09 E-value: 2.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 143 PVKALSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHDVFDLADRVSVMKNG 222
Cdd:PRK10938 132 RFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADC 211
|
90
....*....|....*.
gi 489631109 223 QVVGHARTEDVTKDEV 238
Cdd:PRK10938 212 TLAETGEREEILQQAL 227
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
33-225 |
1.14e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 46.26 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 33 PGEVVALLGHNGAGKSTLIKILSGaykR------DAGEILINGEPAEINNPRDakkygIETIYQTLAVADNVDAAANLYL 106
Cdd:TIGR00956 788 PGTLTALMGASGAGKTTLLNVLAE---RvttgviTGGDRLVNGRPLDSSFQRS-----IGYVQQQDLHLPTSTVRESLRF 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 107 GRELRTPwgtlDDVAMEAKAR---EVMGRLnpNFQRFKEPVKALSGG-----QRQSVAIARAILFDARILI-MDEPTAAL 177
Cdd:TIGR00956 860 SAYLRQP----KSVSKSEKMEyveEVIKLL--EMESYADAVVGVPGEglnveQRKRLTIGVELVAKPKLLLfLDEPTSGL 933
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489631109 178 GPQETAQVGELIKQLKREGIGIFLIshdIH----DVFDLADRVSVM-KNGQVV 225
Cdd:TIGR00956 934 DSQTAWSICKLMRKLADHGQAILCT---IHqpsaILFEEFDRLLLLqKGGQTV 983
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
26-225 |
1.29e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 46.31 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 26 DASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILingepAEinnprdakkYGIETIYQTLAVADNVDAAANLY 105
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-----AE---------RSIAYVPQQAWIMNATVRGNILF 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 106 LGRElRTpwGTLDDVA----MEAKAREVMGRLNpnfQRFKEPVKALSGGQRQSVAIARAILFDARILIMDEPTAALgpqe 181
Cdd:PTZ00243 744 FDEE-DA--ARLADAVrvsqLEADLAQLGGGLE---TEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSAL---- 813
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489631109 182 TAQVGELIKQ---LKR-EGIGIFLISHDIHdVFDLADRVSVMKNGQVV 225
Cdd:PTZ00243 814 DAHVGERVVEecfLGAlAGKTRVLATHQVH-VVPRADYVVALGDGRVE 860
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
34-224 |
1.91e-05 |
|
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: 45.71 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 34 GEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGEPAEInnPRDAkkygietiyqtlaVADNVDAAANLYLGRELRTP 113
Cdd:TIGR00957 664 GALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYV--PQQA-------------WIQNDSLRENILFGKALNEK 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 114 WGTlddVAMEAKAREVMGRLNPNFQRFKEPVKA--LSGGQRQSVAIARAILFDARILIMDEPTAALgpqeTAQVGELI-- 189
Cdd:TIGR00957 729 YYQ---QVLEACALLPDLEILPSGDRTEIGEKGvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAV----DAHVGKHIfe 801
|
170 180 190
....*....|....*....|....*....|....*....
gi 489631109 190 KQLKREGI----GIFLISHDIhDVFDLADRVSVMKNGQV 224
Cdd:TIGR00957 802 HVIGPEGVlknkTRILVTHGI-SYLPQVDVIIVMSGGKI 839
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
6-244 |
2.82e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 45.35 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 6 TPLVEMKNISISFGGIHA---VDDASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKR-DAGEILINGEPAEInnPRdak 81
Cdd:PLN03232 612 APAISIKNGYFSWDSKTSkptLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHaETSSVVIRGSVAYV--PQ--- 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 82 kygIETIYQTlavadnvDAAANLYLGRELRTP--WGTLDDVAMEAKAREVMGRlnpNFQRFKEPVKALSGGQRQSVAIAR 159
Cdd:PLN03232 687 ---VSWIFNA-------TVRENILFGSDFESEryWRAIDVTALQHDLDLLPGR---DLTEIGERGVNISGGQKQRVSMAR 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 160 AILFDARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHdVFDLADRVSVMKNGQVVGHARTEDVTKDEVL 239
Cdd:PLN03232 754 AVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLH-FLPLMDRIILVSEGMIKEEGTFAELSKSGSL 832
|
....*
gi 489631109 240 GMIIM 244
Cdd:PLN03232 833 FKKLM 837
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
26-204 |
3.10e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 43.71 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 26 DASVDLYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGepAEINNprdakkygIETIYQTlavadnvdaaanlY 105
Cdd:PRK13541 18 DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKN--CNINN--------IAKPYCT-------------Y 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 106 LGREL--RTPWGTLDDVAMEAKAREVMGRLNPNFQRFK------EPVKALSGGQRQSVAIARAILFDARILIMDEPTAAL 177
Cdd:PRK13541 75 IGHNLglKLEMTVFENLKFWSEIYNSAETLYAAIHYFKlhdlldEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNL 154
|
170 180
....*....|....*....|....*..
gi 489631109 178 GPQETAQVGELIKQLKREGIGIFLISH 204
Cdd:PRK13541 155 SKENRDLLNNLIVMKANSGGIVLLSSH 181
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
12-174 |
3.66e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 44.72 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 12 KNISISFggihavddasvdlYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGE-ILING--------EP----------- 71
Cdd:PRK11819 24 KDISLSF-------------FPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEaRPAPGikvgylpqEPqldpektvren 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 72 -----AEINNPRD-----AKKYG---------------IETIYQTLAVadnvdaaanlylgrelrtpWgTLD---DVAME 123
Cdd:PRK11819 91 veegvAEVKAALDrfneiYAAYAepdadfdalaaeqgeLQEIIDAADA-------------------W-DLDsqlEIAMD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489631109 124 AKarevmgRLNPNfqrfKEPVKALSGGQRQSVAIARAILFDARILIMDEPT 174
Cdd:PRK11819 151 AL------RCPPW----DAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPT 191
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
147-195 |
3.95e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 44.73 E-value: 3.95e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 489631109 147 LSGGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGEliKQLKRE 195
Cdd:PLN03130 741 ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFD--KCIKDE 787
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
33-224 |
5.09e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 44.38 E-value: 5.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 33 PGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILINGepaeinnpRDAKKYGIetiyqtlavadnvdaaanlylgRELRT 112
Cdd:PTZ00243 1335 PREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNG--------REIGAYGL----------------------RELRR 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 113 PW-----------GTLD---DVAMEAKAREVMGRLnpNFQRFKEPVKALSG---------------GQRQSVAIARAIL- 162
Cdd:PTZ00243 1385 QFsmipqdpvlfdGTVRqnvDPFLEASSAEVWAAL--ELVGLRERVASESEgidsrvleggsnysvGQRQLMCMARALLk 1462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489631109 163 FDARILIMDEPTAALGPQetaqvgeLIKQLKREGIGIF------LISHDIHDVFDLaDRVSVMKNGQV 224
Cdd:PTZ00243 1463 KGSGFILMDEATANIDPA-------LDRQIQATVMSAFsaytviTIAHRLHTVAQY-DKIIVMDHGAV 1522
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
8-90 |
5.62e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 43.24 E-value: 5.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 8 LVEMKNISISFGGIHAVDDASVDLYPGEVVALLGHNGAGKSTLIKILSGA--YKRDAGEILINGEPAEINNPRDAKKYGI 85
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGEGI 80
|
....*
gi 489631109 86 ETIYQ 90
Cdd:PRK09580 81 FMAFQ 85
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
147-216 |
6.34e-05 |
|
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: 43.02 E-value: 6.34e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489631109 147 LSGGQRQSVAIARAI---LFDArILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDiHDVFDLADRV 216
Cdd:cd03270 138 LSGGEAQRIRLATQIgsgLTGV-LYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHD-EDTIRAADHV 208
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
142-216 |
6.58e-05 |
|
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: 42.59 E-value: 6.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 142 EPVKALSGGQRQSVAI----ARAILFDAR--ILIMDEPTAAL-GPQETAQVGELIKQLKREGIG-IFLISHDiHDVFDLA 213
Cdd:cd03240 111 DMRGRCSGGEKVLASLiirlALAETFGSNcgILALDEPTTNLdEENIEESLAEIIEERKSQKNFqLIVITHD-EELVDAA 189
|
...
gi 489631109 214 DRV 216
Cdd:cd03240 190 DHI 192
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
7-73 |
1.14e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.96 E-value: 1.14e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489631109 7 PLVEmkNISISFGGihavddasvdlypGEVVALLGHNGAGKSTLIKILSGAYKRDAGEILIngEPAE 73
Cdd:PRK15064 15 PLFE--NISVKFGG-------------GNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSL--DPNE 64
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
147-222 |
1.37e-04 |
|
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: 41.93 E-value: 1.37e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489631109 147 LSGGQRQSVAIARAILFDARILIMDEPTAALG---PQETAQVGeLIKQLKREGIGIFLISHDIHdVFDLADRVSVMKNG 222
Cdd:cd03290 141 LSGGQRQRICVARALYQNTNIVFLDDPFSALDihlSDHLMQEG-ILKFLQDDKRTLVLVTHKLQ-YLPHADWIIAMKDG 217
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
127-205 |
1.42e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 42.38 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 127 REVMGRLNPNFQRFKEPVKALSGGQRQSVAIARAILFDA---RILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLIS 203
Cdd:pfam13304 217 RERGLILLENGGGGELPAFELSDGTKRLLALLAALLSALpkgGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTT 296
|
..
gi 489631109 204 HD 205
Cdd:pfam13304 297 HS 298
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
26-225 |
1.52e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.91 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 26 DASVDLYPGEVVALLGHNGAGKSTLIKILSGayKRD-----AGEILINGEPAEINNPRDAKKY--------GIETIYQTL 92
Cdd:PLN03140 183 DASGIIKPSRMTLLLGPPSSGKTTLLLALAG--KLDpslkvSGEITYNGYRLNEFVPRKTSAYisqndvhvGVMTVKETL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 93 AVADNVDAAANLY-----LGRELRT----PWGTLDdVAMEAKARE-VMGRLNPNFQrFK--------------EPVKALS 148
Cdd:PLN03140 261 DFSARCQGVGTRYdllseLARREKDagifPEAEVD-LFMKATAMEgVKSSLITDYT-LKilgldickdtivgdEMIRGIS 338
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489631109 149 GGQRQSVAIARAILFDARILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLIS--HDIHDVFDLADRVSVMKNGQVV 225
Cdd:PLN03140 339 GGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSllQPAPETFDLFDDIILLSEGQIV 417
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
147-216 |
1.54e-04 |
|
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: 41.15 E-value: 1.54e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489631109 147 LSGGQRQSVAIARAI---LFDArILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIhDVFDLADRV 216
Cdd:cd03238 88 LSGGELQRVKLASELfsePPGT-LFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNL-DVLSSADWI 158
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
147-244 |
2.97e-04 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 41.05 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 147 LSGGQRQSVAIARAILFDARILIMDEPTAALGpQETAQVGELIKQLKREGIGIFLISHDIHDVFDlADRVSVMKNGQVVG 226
Cdd:cd03288 157 FSVGQRQLFCLARAFVRKSSILIMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVE 234
|
90 100
....*....|....*....|
gi 489631109 227 HARTEDV--TKDEVLGMIIM 244
Cdd:cd03288 235 CDTPENLlaQEDGVFASLVR 254
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
143-216 |
4.48e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 4.48e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489631109 143 PVKALSGGQRQSVAIARAILFDAR---ILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIHdVFDLADRV 216
Cdd:PRK00635 806 PLSSLSGGEIQRLKLAYELLAPSKkptLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMH-VVKVADYV 881
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
144-215 |
5.06e-04 |
|
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: 39.65 E-value: 5.06e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489631109 144 VKALSGGQRQSVAIARAI---LFDARIL-IMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDiHDVFDLADR 215
Cdd:cd03227 75 RLQLSGGEKELSALALILalaSLKPRPLyILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHL-PELAELADK 149
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
21-65 |
6.41e-04 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 40.30 E-value: 6.41e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 489631109 21 IHAV---DDASVD-----LYPGEVVALLGHNGAGKSTLIKILSGAYKRDAGEI 65
Cdd:PRK01889 174 VLAVsalDGEGLDvlaawLSGGKTVALLGSSGVGKSTLVNALLGEEVQKTGAV 226
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
20-83 |
8.84e-04 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 39.40 E-value: 8.84e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 20 GIHAVDDASVDLYPGeVVALLGHNGAGKSTLIK----ILSGAYKR--DAGEILINGEPAEINNPRDAKKY 83
Cdd:pfam13476 5 NFRSFRDQTIDFSKG-LTLITGPNGSGKTTILDaiklALYGKTSRlkRKSGGGFVKGDIRIGLEGKGKAY 73
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
12-238 |
1.01e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 39.99 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 12 KNISIS-FGGIHavdDASVDLYPGeVVALLGHNGAGKSTLIKILSGAYKRDAGEILingEPAEINNPRD--AKKYGIETI 88
Cdd:COG3593 4 EKIKIKnFRSIK---DLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSSSRKF---DEEDFYLGDDpdLPEIEIELT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 89 YQTlavadnvdaaanlYLGRELRTPWGTLDDVAMEAKAREVMGRLNPNFQRFKE-------------------------- 142
Cdd:COG3593 77 FGS-------------LLSRLLRLLLKEEDKEELEEALEELNEELKEALKALNEllseylkelldgldlelelsldeled 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 143 ---------------PVKALSGGQRQSVAIA-RAILFDAR------ILIMDEPTAALGPQETAQVGELIKQLKREGIGIF 200
Cdd:COG3593 144 llkslslriedgkelPLDRLGSGFQRLILLAlLSALAELKrapanpILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVI 223
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 489631109 201 LISHDIH--DVFDLADRVSVMKNGQVVGHARTEDVTKDEV 238
Cdd:COG3593 224 ITTHSPHllSEVPLENIRRLRRDSGGTTSTKLIDLDDEDL 263
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
141-191 |
1.34e-03 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213240 [Multi-domain] Cd Length: 251 Bit Score: 39.20 E-value: 1.34e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 489631109 141 KEPVKALSGGQRQSVA---IARAILFD-ARILIMDEPTAALGPQETAQVGELIKQ 191
Cdd:cd03273 161 KESLTELSGGQRSLVAlslILALLLFKpAPMYILDEVDAALDLSHTQNIGRMIKT 215
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
121-229 |
1.64e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.50 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 121 AMEAKAREVMGRLNPNF------QRFK---------EPVKALSGGQRQSV------AIARAILFDARILIMDEPTAALGP 179
Cdd:PRK01156 761 AMTSLTRKYLFEFNLDFddidvdQDFNitvsrggmvEGIDSLSGGEKTAVafalrvAVAQFLNNDKSLLIMDEPTAFLDE 840
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 489631109 180 QETAQVGELIKQLKREGIGI---FLISH--DIHDVFDLADRVSVMKNGQVVGHAR 229
Cdd:PRK01156 841 DRRTNLKDIIEYSLKDSSDIpqvIMISHhrELLSVADVAYEVKKSSGSSKVIPLR 895
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
34-65 |
2.94e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 37.76 E-value: 2.94e-03
10 20 30
....*....|....*....|....*....|..
gi 489631109 34 GEVVALLGHNGAGKSTLIKILSGAYKRDAGEI 65
Cdd:cd01854 85 GKTSVLVGQSGVGKSTLLNALLPELVLATGEI 116
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
9-206 |
6.50e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 36.91 E-value: 6.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 9 VEMKNISiSFGGIHAVDdasvdlYPGEVVALLGHNGAGKSTLI---------------KILSGAYKRDAG------EILI 67
Cdd:COG0419 5 LRLENFR-SYRDTETID------FDDGLNLIVGPNGAGKSTILeairyalygkarsrsKLRSDLINVGSEeasvelEFEH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 68 NGEP-------AEINNPRDAKKYGIETIYQTLAVadnvdaaanLYLGRELRTPWGTLDDvAMEAKAREVMGRLNPNFQRF 140
Cdd:COG0419 78 GGKRyrierrqGEFAEFLEAKPSERKEALKRLLG---------LEIYEELKERLKELEE-ALESALEELAELQKLKQEIL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489631109 141 K-----EPVKALSGGQRQSVAIARAILfdariLIMDepTAALGPQETAQVGELIKQLKregigifLISHDI 206
Cdd:COG0419 148 AqlsglDPIETLSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDALEELA-------IITHVI 204
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
12-75 |
7.53e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 37.44 E-value: 7.53e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 12 KNISI-SFGGIHavdDASVDLYPGEVVaLLGHNGAGKSTLIK----ILSGAYKRDAGEIL-INGEPAEIN 75
Cdd:COG4717 4 KELEIyGFGKFR---DRTIEFSPGLNV-IYGPNEAGKSTLLAfiraMLLERLEKEADELFkPQGRKPELN 69
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
139-233 |
7.62e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 37.69 E-value: 7.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631109 139 RFKEPVKALSGGQRQSVAIARAILFDAR---ILIMDEPTAALGPQETAQVGELIKQLKREGIGIFLISHDIhDVFDLADR 215
Cdd:TIGR00630 822 RLGQPATTLSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNL-DVIKTADY 900
|
90 100
....*....|....*....|....
gi 489631109 216 V------SVMKNGQVVGHARTEDV 233
Cdd:TIGR00630 901 IidlgpeGGDGGGTVVASGTPEEV 924
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
147-204 |
8.92e-03 |
|
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: 37.42 E-value: 8.92e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 489631109 147 LSGGQRQSVAIARAILFDARILIMDEPTAALGPQETaqvGELIKQLKREGIGIFLISH 204
Cdd:TIGR00954 583 LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVE---GYMYRLCREFGITLFSVSH 637
|
|
| |
