|
Name |
Accession |
Description |
Interval |
E-value |
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
18-268 |
7.69e-139 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 390.99 E-value: 7.69e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 18 ANTQTRVAFHHVHKSFVVNQQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGD 97
Cdd:COG1116 2 SAAAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 98 RAVVFQEHRLFPWLTVEQNIELGLLNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFL 177
Cdd:COG1116 82 RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 178 LDEPFGALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVILKPKPGRVEQIIPVNLPRPRN---RSSFEL 254
Cdd:COG1116 162 MDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSARPGRIVEEIDVDLPRPRDrelRTSPEF 241
|
250
....*....|....
gi 1956008863 255 HQLKEQIFRILTED 268
Cdd:COG1116 242 AALRAEILDLLREE 255
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
24-243 |
1.15e-117 |
|
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: 335.98 E-value: 1.15e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 24 VAFHHVHKSFVVNQQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDRAVVFQ 103
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 104 EHRLFPWLTVEQNIELGLLNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFG 183
Cdd:cd03293 81 QDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 184 ALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVILKPKPGRVEQIIPVNL 243
Cdd:cd03293 161 ALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSARPGRIVAEVEVDL 220
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
20-238 |
2.05e-90 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 271.59 E-value: 2.05e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 20 TQTRVAFHHVHKSFvvnqQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIG-GDR 98
Cdd:COG3842 2 AMPALELENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPpEKR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 99 AV--VFQEHRLFPWLTVEQNIELGLLNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIF 176
Cdd:COG3842 78 NVgmVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1956008863 177 LLDEPFGALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVILkpKPGRVEQI 238
Cdd:COG3842 158 LLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVM--NDGRIEQV 217
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
26-238 |
2.51e-83 |
|
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: 248.59 E-value: 2.51e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 26 FHHVHKSFvvnqQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDR---AVVF 102
Cdd:cd03259 3 LKGLSKTY----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERrniGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 103 QEHRLFPWLTVEQNIELGLLNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPF 182
Cdd:cd03259 79 QDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1956008863 183 GALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVILkpKPGRVEQI 238
Cdd:cd03259 159 SALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVM--NEGRIVQV 212
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
28-235 |
8.39e-83 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 249.01 E-value: 8.39e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 28 HVHKSFVVNQQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDRAVVFQEHRL 107
Cdd:COG4525 8 HVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADRGVVFQKDAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 108 FPWLTVEQNIELGLLNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDA 187
Cdd:COG4525 88 LPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1956008863 188 LTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVILKPKPGRV 235
Cdd:COG4525 168 LTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPGPGRI 215
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
22-238 |
2.20e-78 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 240.75 E-value: 2.20e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 22 TRVAFHHVHKSFvvnqQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIG-GDR-- 98
Cdd:COG3839 2 ASLELENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPpKDRni 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 99 AVVFQEHRLFPWLTVEQNIELGLLNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLL 178
Cdd:COG3839 78 AMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 179 DEPFGALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVILkpKPGRVEQI 238
Cdd:COG3839 158 DEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVM--NDGRIQQV 215
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
43-249 |
5.77e-77 |
|
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: 233.13 E-value: 5.77e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 43 IHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDRAVVFQEHRLFPWLTVEQNIELGL- 121
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVFQNYSLLPWLTVRENIALAVd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 122 -LNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQMQNELLRI 200
Cdd:TIGR01184 81 rVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1956008863 201 QSQQKMTTVFITHDVEEAVTLADRVVILKPKPG-RVEQIIPVNLPRPRNR 249
Cdd:TIGR01184 161 WEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAaNIGQILEVPFPRPRDR 210
|
|
| ABC_ATP_SaoA |
NF040729 |
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC ... |
23-265 |
3.47e-75 |
|
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC transporter in which both the permease subunit SaoP, and the substrate-binding protein SaoB, are nearly always selenoproteins that were unrecognized as such until recently (2022). The SAO system is found in Clostridium difficile and various other anaerobic heterotrophs.
Pssm-ID: 468693 [Multi-domain] Cd Length: 248 Bit Score: 229.24 E-value: 3.47e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 23 RVAFHHVHKSFVVNQQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDRAVVF 102
Cdd:NF040729 1 KLKIQNISKTFINNKKENEVLKDISFDVEEGEFVSLLGPSGCGKTTLLTIIAGFQNATSGEILVNGNEVTKPGPDRGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 103 QEHRLFPWLTVEQNIELGLLNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPF 182
Cdd:NF040729 81 QNYALFPWMTVKENIEYPMKQQKMPKQEREKRLNELLEMAQLTGKENLYPHQISGGMKQRTAVIRALACKPEVLLMDEPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 183 GALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVILKPKPGRVEQIIPVNLPRPRNRSSFELHQLKEQIF 262
Cdd:NF040729 161 GAVDFQMRQILQEELESIWLKDKTTVLMVTHDVDEAVYLSDRVIVMSRDKGKILEDLKIDLPRPRNRESEKYLEYKDHLT 240
|
...
gi 1956008863 263 RIL 265
Cdd:NF040729 241 NIL 243
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
27-254 |
2.22e-73 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 228.11 E-value: 2.22e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 27 HHVHKSFvvnqQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSgIG---GDRAV--V 101
Cdd:COG1118 6 RNISKRF----GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF-TNlppRERRVgfV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 102 FQEHRLFPWLTVEQNIELGLLNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEP 181
Cdd:COG1118 81 FQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1956008863 182 FGALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVILkpKPGRVEQIIPVN--LPRPRNRSSFEL 254
Cdd:COG1118 161 FGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVM--NQGRIEQVGTPDevYDRPATPFVARF 233
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
43-238 |
1.26e-71 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 224.60 E-value: 1.26e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 43 IHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDR---------AVVFQEHRLFPWLTV 113
Cdd:COG4175 43 VNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKElrelrrkkmSMVFQHFALLPHRTV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 114 EQNIELGL----LNEAlTSRDKdilVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALT 189
Cdd:COG4175 123 LENVAFGLeiqgVPKA-ERRER---AREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLI 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1956008863 190 RHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVILkpKPGRVEQI 238
Cdd:COG4175 199 RREMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIM--KDGRIVQI 245
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
24-229 |
4.93e-69 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 212.60 E-value: 4.93e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 24 VAFHHVHKSFVVNQQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGD-RA--- 99
Cdd:COG1136 5 LELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEReLArlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 100 -----VVFQEHRLFPWLTVEQNIELGLLNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPR 174
Cdd:COG1136 85 rrhigFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1956008863 175 IFLLDEPFGALDALTRHQMQNELLRIQSQQKMTTVFITHDvEEAVTLADRVVILK 229
Cdd:COG1136 165 LILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRLR 218
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
24-238 |
3.11e-68 |
|
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: 210.94 E-value: 3.11e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 24 VAFHHVHKSFvvnqQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDR---AV 100
Cdd:cd03300 1 IELENVSKFY----GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKrpvNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 101 VFQEHRLFPWLTVEQNIELGLlneALTSRDKDIL---VQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFL 177
Cdd:cd03300 77 VFQNYALFPHLTVFENIAFGL---RLKKLPKAEIkerVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1956008863 178 LDEPFGALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVILkpKPGRVEQI 238
Cdd:cd03300 154 LDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVM--NKGKIQQI 212
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
24-238 |
3.96e-68 |
|
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: 210.19 E-value: 3.96e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 24 VAFHHVHKSFvvnqQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIG-GDR--AV 100
Cdd:cd03301 1 VELENVTKRF----GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPpKDRdiAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 101 VFQEHRLFPWLTVEQNIELGLlneALTSRDKDIL---VQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFL 177
Cdd:cd03301 77 VFQNYALYPHMTVYDNIAFGL---KLRKVPKDEIderVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1956008863 178 LDEPFGALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVILkpKPGRVEQI 238
Cdd:cd03301 154 MDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVM--NDGQIQQI 212
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
26-238 |
6.59e-68 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 212.64 E-value: 6.59e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 26 FHHVHKSFvvnQQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVS---------GIGg 96
Cdd:COG1125 4 FENVTKRY---PDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRdldpvelrrRIG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 97 draVVFQEHRLFPWLTVEQNIEL--GLLNealtsRDKDILVQKAIELIGLNG-----FEKAYPHQLSGGMSQRVAIARSL 169
Cdd:COG1125 80 ---YVIQQIGLFPHMTVAENIATvpRLLG-----WDKERIRARVDELLELVGldpeeYRDRYPHELSGGQQQRVGVARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1956008863 170 VVQPRIFLLDEPFGALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVILkpKPGRVEQI 238
Cdd:COG1125 152 AADPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVM--REGRIVQY 218
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
19-266 |
8.22e-68 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 210.69 E-value: 8.22e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 19 NTQTRVAFHHVHKSFVVNQqpvkVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDR 98
Cdd:PRK11247 8 NQGTPLLLNAVSKRYGERT----VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 99 AVVFQEHRLFPWLTVEQNIELGLLNEAltsRDKdilVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLL 178
Cdd:PRK11247 84 RLMFQDARLLPWKKVIDNVGLGLKGQW---RDA---ALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 179 DEPFGALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVILkpKPGRVEQIIPVNLPRPRNRSSFELHQLK 258
Cdd:PRK11247 158 DEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLI--EEGKIGLDLTVDLPRPRRRGSARLAELE 235
|
....*....
gi 1956008863 259 EQIF-RILT 266
Cdd:PRK11247 236 AEVLqRVMS 244
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
43-238 |
2.38e-66 |
|
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: 207.50 E-value: 2.38e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 43 IHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDR---------AVVFQEHRLFPWLTV 113
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrkkiSMVFQSFALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 114 EQNIELGLLNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQM 193
Cdd:cd03294 120 LENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREM 199
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1956008863 194 QNELLRIQSQQKMTTVFITHDVEEAVTLADRVVILkpKPGRVEQI 238
Cdd:cd03294 200 QDELLRLQAELQKTIVFITHDLDEALRLGDRIAIM--KDGRLVQV 242
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
23-238 |
5.61e-66 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 209.12 E-value: 5.61e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 23 RVAFHHVHKSFVVNQqpvkVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGG---DRA 99
Cdd:TIGR03265 4 YLSIDNIRKRFGAFT----ALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPqkrDYG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 100 VVFQEHRLFPWLTVEQNIELGLLNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLD 179
Cdd:TIGR03265 80 IVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1956008863 180 EPFGALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVILkpKPGRVEQI 238
Cdd:TIGR03265 160 EPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVM--NHGVIEQV 216
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
42-245 |
8.36e-66 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 205.70 E-value: 8.36e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 42 VIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDRAVVFQEHRLFPWLTVEQNIELGL 121
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGVVFQNEGLLPWRNVQDNVAFGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 122 LNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQMQNELLRIQ 201
Cdd:PRK11248 96 QLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLW 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1956008863 202 SQQKMTTVFITHDVEEAVTLADRVVILKPKPGRVEQIIPVNLPR 245
Cdd:PRK11248 176 QETGKQVLLITHDIEEAVFMATELVLLSPGPGRVVERLPLNFAR 219
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
43-238 |
3.77e-65 |
|
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: 203.34 E-value: 3.77e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 43 IHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIG-GDRAV--VFQEHRLFPWLTVEQNIEL 119
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPvQERNVgfVFQHYALFRHMTVFDNVAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 120 GLLNEALTSR-DKDILVQKA---IELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQMQN 195
Cdd:cd03296 98 GLRVKPRSERpPEAEIRAKVhelLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRR 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1956008863 196 ELLRIQSQQKMTTVFITHDVEEAVTLADRVVILkpKPGRVEQI 238
Cdd:cd03296 178 WLRRLHDELHVTTVFVTHDQEEALEVADRVVVM--NKGRIEQV 218
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
28-229 |
5.19e-65 |
|
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: 202.33 E-value: 5.19e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 28 HVHKSFVVNQQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDR--------- 98
Cdd:cd03255 5 NLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKElaafrrrhi 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 99 AVVFQEHRLFPWLTVEQNIELGLLNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLL 178
Cdd:cd03255 85 GFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1956008863 179 DEPFGALDALTRHQMQNELLRIQSQQKMTTVFITHDvEEAVTLADRVVILK 229
Cdd:cd03255 165 DEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHD-PELAEYADRIIELR 214
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
17-238 |
1.30e-64 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 206.34 E-value: 1.30e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 17 QANTQTRVAFHHVHKSFVVNQqpvkVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGG 96
Cdd:PRK09452 8 PSSLSPLVELRGISKSFDGKE----VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 97 D-RAV--VFQEHRLFPWLTVEQNIELGLLNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQP 173
Cdd:PRK09452 84 EnRHVntVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1956008863 174 RIFLLDEPFGALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVILkpKPGRVEQI 238
Cdd:PRK09452 164 KVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVM--RDGRIEQD 226
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
26-229 |
8.26e-63 |
|
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: 196.96 E-value: 8.26e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 26 FHHVHKSFVVNQQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDR------- 98
Cdd:cd03257 4 VKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLrkirrke 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 99 -AVVFQE--HRLFPWLTVEQNIELGLLNEALTSRDKDILVQKAIELIGLN---GFEKAYPHQLSGGMSQRVAIARSLVVQ 172
Cdd:cd03257 84 iQMVFQDpmSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGlpeEVLNRYPHELSGGQRQRVAIARALALN 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1956008863 173 PRIFLLDEPFGALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVILK 229
Cdd:cd03257 164 PKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMY 220
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
42-238 |
6.56e-62 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 195.02 E-value: 6.56e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 42 VIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGG-DRAV--VFQEHRLFPWLTVEQNIE 118
Cdd:TIGR00968 15 ALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHArDRKIgfVFQHYALFKHLTVRDNIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 119 LGLLNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQMQNELL 198
Cdd:TIGR00968 95 FGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGALDAKVRKELRSWLR 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1956008863 199 RIQSQQKMTTVFITHDVEEAVTLADRVVILkpKPGRVEQI 238
Cdd:TIGR00968 175 KLHDEVHVTTVFVTHDQEEAMEVADRIVVM--SNGKIEQI 212
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
24-229 |
1.74e-61 |
|
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: 202.06 E-value: 1.74e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 24 VAFHHVHKSFVVN-QQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDR---- 98
Cdd:COG1123 261 LEVRNLSKRYPVRgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 99 ----AVVFQ--EHRLFPWLTVEQNIELGLLNEALTSR-DKDILVQKAIELIGLN-GFEKAYPHQLSGGMSQRVAIARSLV 170
Cdd:COG1123 341 rrrvQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLLSRaERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIARALA 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1956008863 171 VQPRIFLLDEPFGALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVILK 229
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMY 479
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
58-238 |
2.06e-61 |
|
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: 196.56 E-value: 2.06e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 58 IVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDR---AVVFQEHRLFPWLTVEQNIELGLLNEALTSRDKDIL 134
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLrhiNMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 135 VQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQMQNELLRIQSQQKMTTVFITHD 214
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170 180
....*....|....*....|....
gi 1956008863 215 VEEAVTLADRVVILkpKPGRVEQI 238
Cdd:TIGR01187 161 QEEAMTMSDRIAIM--RKGKIAQI 182
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
24-238 |
3.42e-61 |
|
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: 193.29 E-value: 3.42e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 24 VAFHHVHKSFVVNQqpvKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDR----- 98
Cdd:cd03295 1 IEFENVTKRYGGGK---KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrrki 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 99 AVVFQEHRLFPWLTVEQNIELGLlneALTSRDKDILVQKAIELIGLNGFEKA-----YPHQLSGGMSQRVAIARSLVVQP 173
Cdd:cd03295 78 GYVIQQIGLFPHMTVEENIALVP---KLLKWPKEKIRERADELLALVGLDPAefadrYPHELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1956008863 174 RIFLLDEPFGALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVILkpKPGRVEQI 238
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIM--KNGEIVQV 217
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
24-229 |
6.54e-61 |
|
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: 192.50 E-value: 6.54e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 24 VAFHHVHKSFvvNQQPVkvIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDR----- 98
Cdd:COG1127 6 IEVRNLTKSF--GDRVV--LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 99 ---AVVFQEHRLFPWLTVEQNIELGLL-NEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPR 174
Cdd:COG1127 82 rriGMLFQGGALFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1956008863 175 IFLLDEPFGALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVILK 229
Cdd:COG1127 162 ILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLA 216
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
29-238 |
2.56e-59 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 191.98 E-value: 2.56e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 29 VHKSFVVNQQpvkVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIG-GDR--AVVFQEH 105
Cdd:PRK11650 9 VRKSYDGKTQ---VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEpADRdiAMVFQNY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 106 RLFPWLTVEQNIELGLLNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGAL 185
Cdd:PRK11650 86 ALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1956008863 186 DALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVILkpKPGRVEQI 238
Cdd:PRK11650 166 DAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVM--NGGVAEQI 216
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
26-229 |
2.96e-58 |
|
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: 183.54 E-value: 2.96e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 26 FHHVHKSFvvNQqpVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDR------- 98
Cdd:cd03229 3 LKNVSKRY--GQ--KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELpplrrri 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 99 AVVFQEHRLFPWLTVEQNIELGLlnealtsrdkdilvqkaieliglngfekayphqlSGGMSQRVAIARSLVVQPRIFLL 178
Cdd:cd03229 79 GMVFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1956008863 179 DEPFGALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVILK 229
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLR 175
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
46-241 |
6.19e-58 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 184.57 E-value: 6.19e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 46 FNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIG-GDR--AVVFQEHRLFPWLTVEQNIELGL- 121
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPpAERpvSMLFQENNLFPHLTVAQNIGLGLr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 122 --LNeaLTSRDKDiLVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQMQNELLR 199
Cdd:COG3840 98 pgLK--LTAEQRA-QVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1956008863 200 IQSQQKMTTVFITHDVEEAVTLADRVVILkpKPGRVEQIIPV 241
Cdd:COG3840 175 LCRERGLTVLMVTHDPEDAARIADRVLLV--ADGRIAADGPT 214
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
32-229 |
7.71e-58 |
|
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: 183.82 E-value: 7.71e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 32 SFVVNQQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSG-----IGGDRAVVFQ--E 104
Cdd:cd03225 6 SFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKlslkeLRRKVGLVFQnpD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 105 HRLFPwLTVEQNIELGLLNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGA 184
Cdd:cd03225 86 DQFFG-PTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAG 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1956008863 185 LDALTRHQMQNELLRIQsQQKMTTVFITHDVEEAVTLADRVVILK 229
Cdd:cd03225 165 LDPAGRRELLELLKKLK-AEGKTIIIVTHDLDLLLELADRVIVLE 208
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
40-229 |
1.60e-57 |
|
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: 183.30 E-value: 1.60e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 40 VKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDRA-----VVFQ--EHRLF-Pwl 111
Cdd:COG1122 14 TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELrrkvgLVFQnpDDQLFaP-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 112 TVEQNIELGLLNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRH 191
Cdd:COG1122 92 TVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRR 171
|
170 180 190
....*....|....*....|....*....|....*...
gi 1956008863 192 QMQNELLRIQsQQKMTTVFITHDVEEAVTLADRVVILK 229
Cdd:COG1122 172 ELLELLKRLN-KEGKTVIIVTHDLDLVAELADRVIVLD 208
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
28-238 |
2.65e-57 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 186.83 E-value: 2.65e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 28 HVHKSFvvnqQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGG-DRAV--VFQE 104
Cdd:PRK10851 7 NIKKSF----GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHArDRKVgfVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 105 HRLFPWLTVEQNIELGLlnEALTSR---DKDILVQKA---IELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLL 178
Cdd:PRK10851 83 YALFRHMTVFDNIAFGL--TVLPRRerpNAAAIKAKVtqlLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 179 DEPFGALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVILkpKPGRVEQI 238
Cdd:PRK10851 161 DEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVM--SQGNIEQA 218
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
45-238 |
1.10e-56 |
|
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: 180.95 E-value: 1.10e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 45 DFNLEIK---EGEFIAIVGSSGCGKSTLLRLLAGLDQ------DFDGRILIDGADVSGIGG-DRAV--VFQEHRLFPWLT 112
Cdd:cd03297 12 DFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKpdggtiVLNGTVLFDSRKKINLPPqQRKIglVFQQYALFPHLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 113 VEQNIELGLlnEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQ 192
Cdd:cd03297 92 VRENLAFGL--KRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1956008863 193 MQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVILkpKPGRVEQI 238
Cdd:cd03297 170 LLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVM--EDGRLQYI 213
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
27-245 |
1.86e-56 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 181.54 E-value: 1.86e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 27 HHVHKSFVVNQQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGgDRA------V 100
Cdd:COG1124 5 RNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRR-RKAfrrrvqM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 101 VFQEHR--LFPWLTVEQNIELGLLNEALTSRDKDILvqKAIELIGLN-GFEKAYPHQLSGGMSQRVAIARSLVVQPRIFL 177
Cdd:COG1124 84 VFQDPYasLHPRHTVDRILAEPLRIHGLPDREERIA--ELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARALILEPELLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1956008863 178 LDEPFGALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVILkpKPGRVEQIIPVNLPR 245
Cdd:COG1124 162 LDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVM--QNGRIVEELTVADLL 227
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
28-228 |
2.43e-55 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 178.08 E-value: 2.43e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 28 HVHKSFVVNQqpvkVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDR--------A 99
Cdd:cd03261 5 GLTKSFGGRT----VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrrrmG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 100 VVFQEHRLFPWLTVEQNIELGLL-NEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLL 178
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLReHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1956008863 179 DEPFGALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVIL 228
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVL 210
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
42-228 |
2.60e-55 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 182.34 E-value: 2.60e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 42 VIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDRA---VVFQEHRLFPWLTVEQNIE 118
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRpinMMFQSYALFPHMTVEQNIA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 119 LGLLNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQMQNELL 198
Cdd:PRK11607 114 FGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVV 193
|
170 180 190
....*....|....*....|....*....|
gi 1956008863 199 RIQSQQKMTTVFITHDVEEAVTLADRVVIL 228
Cdd:PRK11607 194 DILERVGVTCVMVTHDQEEAMTMAGRIAIM 223
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
45-228 |
1.14e-54 |
|
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: 175.76 E-value: 1.14e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 45 DFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIG-GDRAV--VFQEHRLFPWLTVEQNIELGL 121
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPpADRPVsmLFQENNLFAHLTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 122 L-NEALTSRDKDiLVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQMQNELLRI 200
Cdd:cd03298 96 SpGLKLTAEDRQ-AIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDL 174
|
170 180
....*....|....*....|....*...
gi 1956008863 201 QSQQKMTTVFITHDVEEAVTLADRVVIL 228
Cdd:cd03298 175 HAETKMTVLMVTHQPEDAKRLAQRVVFL 202
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
42-237 |
1.21e-53 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 177.88 E-value: 1.21e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 42 VIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQ--DFDGRILIDGADVSGIGGDR---AVVFQEHRLFPWLTVEQN 116
Cdd:TIGR03258 20 VLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKaaGLTGRIAIADRDLTHAPPHKrglALLFQNYALFPHLKVEDN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 117 IELGLLNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQMQNE 196
Cdd:TIGR03258 100 VAFGLRAQKMPKADIAERVADALKLVGLGDAAAHLPAQLSGGMQQRIAIARAIAIEPDVLLLDEPLSALDANIRANMREE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1956008863 197 LLRIQSQ-QKMTTVFITHDVEEAVTLADRVVILkpKPGRVEQ 237
Cdd:TIGR03258 180 IAALHEElPELTILCVTHDQDDALTLADKAGIM--KDGRLAA 219
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
24-249 |
4.64e-53 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 176.37 E-value: 4.64e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 24 VAFHHVHKSFvvnqQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIG-GDRAV-- 100
Cdd:PRK11000 4 VTLRNVTKAY----GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPpAERGVgm 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 101 VFQEHRLFPWLTVEQNIELGLLNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDE 180
Cdd:PRK11000 80 VFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1956008863 181 PFGALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVILkpKPGRVEQI-IPVNLPR-PRNR 249
Cdd:PRK11000 160 PLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVL--DAGRVAQVgKPLELYHyPANR 228
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
24-240 |
7.56e-53 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 175.29 E-value: 7.56e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 24 VAFHHVHKSFVVNqqpvKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADV--SGIGG-DRAV 100
Cdd:PRK11432 7 VVLKNITKRFGSN----TVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVthRSIQQrDICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 101 VFQEHRLFPWLTVEQNIELGLLNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDE 180
Cdd:PRK11432 83 VFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 181 PFGALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVILkpKPGRVEQIIP 240
Cdd:PRK11432 163 PLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVM--NKGKIMQIGS 220
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
24-229 |
2.93e-51 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 167.15 E-value: 2.93e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 24 VAFHHVHKSFvvnQQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDR----- 98
Cdd:COG2884 2 IRFENVSKRY---PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 99 ---AVVFQEHRLFPWLTVEQNIELGLlnEALTSRDKDI--LVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQP 173
Cdd:COG2884 79 rriGVVFQDFRLLPDRTVYENVALPL--RVTGKSRKEIrrRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1956008863 174 RIFLLDEPFGALDALTRHQMQNELLRIQSQQkmTTVFI-THDVEEAVTLADRVVILK 229
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEINRRG--TTVLIaTHDLELVDRMPKRVLELE 211
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
24-226 |
3.61e-51 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 167.48 E-value: 3.61e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 24 VAFHHVHKSFvvnqQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDRA---- 99
Cdd:COG1126 2 IEIENLHKSF----GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINklrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 100 ---VVFQEHRLFPWLTVEQNIELGLLNeaLTSRDKDILVQKAIEL---IGLNGFEKAYPHQLSGGMSQRVAIARSLVVQP 173
Cdd:COG1126 78 kvgMVFQQFNLFPHLTVLENVTLAPIK--VKKMSKAEAEERAMELlerVGLADKADAYPAQLSGGQQQRVAIARALAMEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1956008863 174 RIFLLDEPFGALDAltrhQMQNELLR-IQS--QQKMTTVFITHDVEEAVTLADRVV 226
Cdd:COG1126 156 KVMLFDEPTSALDP----ELVGEVLDvMRDlaKEGMTMVVVTHEMGFAREVADRVV 207
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
45-238 |
5.57e-51 |
|
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: 167.13 E-value: 5.57e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 45 DFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDR---AVVFQEHRLFPWLTVEQNIELGL 121
Cdd:cd03299 17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKrdiSYVPQNYALFPHMTVYKNIAYGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 122 LNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQMQNELLRIQ 201
Cdd:cd03299 97 KKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIR 176
|
170 180 190
....*....|....*....|....*....|....*..
gi 1956008863 202 SQQKMTTVFITHDVEEAVTLADRVVILkpKPGRVEQI 238
Cdd:cd03299 177 KEFGVTVLHVTHDFEEAWALADKVAIM--LNGKLIQV 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
32-235 |
5.64e-51 |
|
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: 174.32 E-value: 5.64e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 32 SFVVNQQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGL---DQDFDGRILIDGADVSG-----IGGDRAVVFQ 103
Cdd:COG1123 11 SVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLLDGRDLLElsealRGRRIGMVFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 104 E--HRLFPwLTVEQNIELGLLNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEP 181
Cdd:COG1123 91 DpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1956008863 182 FGALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVILkpKPGRV 235
Cdd:COG1123 170 TTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVM--DDGRI 221
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
24-229 |
9.16e-51 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 166.39 E-value: 9.16e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 24 VAFHHVHKSFvvnqQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSG--------IG 95
Cdd:COG1131 1 IEVRGLTKRY----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARdpaevrrrIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 96 gdraVVFQEHRLFPWLTVEQNIEL-----GLLNEALTSRdkdilVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLV 170
Cdd:COG1131 77 ----YVPQEPALYPDLTVRENLRFfarlyGLPRKEARER-----IDELLELFGLTDAADRKVGTLSGGMKQRLGLALALL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 171 VQPRIFLLDEPFGALDALTRHQMQNELLRIQSQQKmtTVFI-THDVEEAVTLADRVVILK 229
Cdd:COG1131 148 HDPELLILDEPTSGLDPEARRELWELLRELAAEGK--TVLLsTHYLEEAERLCDRVAIID 205
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
24-224 |
2.94e-50 |
|
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: 164.91 E-value: 2.94e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 24 VAFHHVHKSFVVNQQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGD-RA--- 99
Cdd:COG4181 9 IELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDaRArlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 100 -----VVFQEHRLFPWLTVEQNIELGLlnEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPR 174
Cdd:COG4181 89 arhvgFVFQSFQLLPTLTALENVMLPL--ELAGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1956008863 175 IFLLDEPFGALDALTRHQMQNELLRIQSQQKMTTVFITHDVEeavtLADR 224
Cdd:COG4181 167 ILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPA----LAAR 212
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
42-235 |
4.34e-50 |
|
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: 165.22 E-value: 4.34e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 42 VIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGG-DRA----VVFQEHRLFPWLTVEQN 116
Cdd:COG1120 16 VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRrELArriaYVPQEPPAPFGLTVREL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 117 IELGL-----LNEALTSRDKDIlVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDAltRH 191
Cdd:COG1120 96 VALGRyphlgLFGRPSAEDREA-VEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDL--AH 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1956008863 192 QMqnELL----RIQSQQKMTTVFITHDVEEAVTLADRVVILkpKPGRV 235
Cdd:COG1120 173 QL--EVLellrRLARERGRTVVMVLHDLNLAARYADRLVLL--KDGRI 216
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
24-229 |
2.86e-49 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 162.92 E-value: 2.86e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 24 VAFHHVHKSFVVNqqpVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDR----- 98
Cdd:COG3638 3 LELRNLSKRYPGG---TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 99 ---AVVFQEHRLFPWLTVEQNIELGLLNE-----ALTSRDKDILVQKAIELI---GLNgfEKAY--PHQLSGGMSQRVAI 165
Cdd:COG3638 80 rriGMIFQQFNLVPRLSVLTNVLAGRLGRtstwrSLLGLFPPEDRERALEALervGLA--DKAYqrADQLSGGQQQRVAI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1956008863 166 ARSLVVQPRIFLLDEPFGALD-ALTRHQMQNeLLRIQSQQKMTTVFITHDVEEAVTLADRVVILK 229
Cdd:COG3638 158 ARALVQEPKLILADEPVASLDpKTARQVMDL-LRRIAREDGITVVVNLHQVDLARRYADRIIGLR 221
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
23-235 |
3.61e-49 |
|
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: 166.04 E-value: 3.61e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 23 RVAFHHVHKSFVVnqqpvkvihDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADV--SGIGGDRAV 100
Cdd:COG4148 4 EVDFRLRRGGFTL---------DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdSARGIFLPP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 101 -------VFQEHRLFPWLTVEQNIELGLLNEALTSRDkdILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQP 173
Cdd:COG4148 75 hrrrigyVFQEARLFPHLSVRGNLLYGRKRAPRAERR--ISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1956008863 174 RIFLLDEPFGALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVILkpKPGRV 235
Cdd:COG4148 153 RLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLL--EQGRV 212
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
28-228 |
3.71e-49 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 164.84 E-value: 3.71e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 28 HVHKSFVVNQQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQD---FDGRILIDGADVSGIGGDR------ 98
Cdd:COG0444 6 NLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKElrkirg 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 99 ---AVVFQE--HRLFPWLTVEQNIELGLLNEALTSRDKdiLVQKAIELI---GLNGFE---KAYPHQLSGGMSQRVAIAR 167
Cdd:COG0444 86 reiQMIFQDpmTSLNPVMTVGDQIAEPLRIHGGLSKAE--ARERAIELLervGLPDPErrlDRYPHELSGGMRQRVMIAR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1956008863 168 SLVVQPRIFLLDEPFGALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVIL 228
Cdd:COG0444 164 ALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVM 224
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
23-229 |
1.20e-48 |
|
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: 171.17 E-value: 1.20e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 23 RVAFHHVhkSFVVNQQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIggDR---- 98
Cdd:COG2274 473 DIELENV--SFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQI--DPaslr 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 99 ---AVVFQEHRLFPwLTVEQNIELGllNEALTsrDKDILvqKAIELIGLNGFEKAYPH-----------QLSGGMSQRVA 164
Cdd:COG2274 549 rqiGVVLQDVFLFS-GTIRENITLG--DPDAT--DEEII--EAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLA 621
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1956008863 165 IARSLVVQPRIFLLDEPFGALDALTRHQMQNELLRIqsQQKMTTVFITHDvEEAVTLADRVVILK 229
Cdd:COG2274 622 IARALLRNPRILILDEATSALDAETEAIILENLRRL--LKGRTVIIIAHR-LSTIRLADRIIVLD 683
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
27-229 |
3.76e-48 |
|
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: 160.02 E-value: 3.76e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 27 HHVHKSFvvnqQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLdQDFD-GRILIDGADVSgIGGDRA-----V 100
Cdd:COG4555 5 ENLSKKY----GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGL-LKPDsGSILIDGEDVR-KEPREArrqigV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 101 VFQEHRLFPWLTVEQNIE-LGLLNEaLTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLD 179
Cdd:COG4555 79 LPDERGLYDRLTVRENIRyFAELYG-LFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1956008863 180 EPFGALDALTRHQMQNELLRIQSQQKmTTVFITHDVEEAVTLADRVVILK 229
Cdd:COG4555 158 EPTNGLDVMARRLLREILRALKKEGK-TVLFSSHIMQEVEALCDRVVILH 206
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
24-228 |
9.21e-48 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 161.78 E-value: 9.21e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 24 VAFHHVHKSFVVNQQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDR----- 98
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElraar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 99 ---AVVFQEHRLFPWLTVEQNIELGLLNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRI 175
Cdd:COG1135 82 rkiGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1956008863 176 FLLDEPFGALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVIL 228
Cdd:COG1135 162 LLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVL 214
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
24-228 |
1.15e-47 |
|
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: 157.69 E-value: 1.15e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 24 VAFHHVHKSFVVNQqpvkVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGD----R- 98
Cdd:cd03262 1 IEIKNLHKSFGDFH----VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinelRq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 99 --AVVFQEHRLFPWLTVEQNIELGLLNeaLTSRDKDILVQKAIEL---IGLNGFEKAYPHQLSGGMSQRVAIARSLVVQP 173
Cdd:cd03262 77 kvGMVFQQFNLFPHLTVLENITLAPIK--VKGMSKAEAEERALELlekVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1956008863 174 RIFLLDEPFGALDAltrhQMQNELLRIQ---SQQKMTTVFITHDVEEAVTLADRVVIL 228
Cdd:cd03262 155 KVMLFDEPTSALDP----ELVGEVLDVMkdlAEEGMTMVVVTHEMGFAREVADRVIFM 208
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
24-228 |
1.07e-46 |
|
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: 155.82 E-value: 1.07e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 24 VAFHHVHKSFVVNQQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDR----- 98
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 99 ---AVVFQEHRLFPWLTVEQNIELGLlnEALTSRDKDIL--VQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQP 173
Cdd:cd03258 82 rriGMIFQHFNLLSSRTVFENVALPL--EIAGVPKAEIEerVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1956008863 174 RIFLLDEPFGALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVIL 228
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVM 214
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
46-227 |
4.67e-46 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 154.35 E-value: 4.67e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 46 FNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDR---AVVFQEHRLFPWLTVEQNIELGL- 121
Cdd:PRK10771 18 FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRrpvSMLFQENNLFSHLTVAQNIGLGLn 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 122 LNEALTSRDKDILVQKAiELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQMQNELLRIQ 201
Cdd:PRK10771 98 PGLKLNAAQREKLHAIA-RQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVC 176
|
170 180
....*....|....*....|....*.
gi 1956008863 202 SQQKMTTVFITHDVEEAVTLADRVVI 227
Cdd:PRK10771 177 QERQLTLLMVSHSLEDAARIAPRSLV 202
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
43-182 |
5.19e-46 |
|
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: 151.26 E-value: 5.19e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 43 IHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGI-----GGDRAVVFQEHRLFPWLTVEQNI 117
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDerkslRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1956008863 118 ELGLLNEALTSRDKDILVQKAIELIGLNGFEK----AYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPF 182
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
24-229 |
1.19e-45 |
|
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: 151.00 E-value: 1.19e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 24 VAFHHVhkSFVVNQQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDR----- 98
Cdd:cd03228 1 IEFKNV--SFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrkni 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 99 AVVFQEHRLFPwLTVEQNIelgllnealtsrdkdilvqkaieliglngfekayphqLSGGMSQRVAIARSLVVQPRIFLL 178
Cdd:cd03228 79 AYVPQDPFLFS-GTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1956008863 179 DEPFGALDALTRHQMQNELLRIqsQQKMTTVFITHDVeEAVTLADRVVILK 229
Cdd:cd03228 121 DEATSALDPETEALILEALRAL--AKGKTVIVIAHRL-STIRDADRIIVLD 168
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
28-229 |
1.25e-45 |
|
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: 151.01 E-value: 1.25e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 28 HVHKSFvvnqQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDR----AVVFQ 103
Cdd:cd03230 5 NLSKRY----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVkrriGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 104 EHRLFPWLTVEQNIELgllnealtsrdkdilvqkaieliglngfekayphqlSGGMSQRVAIARSLVVQPRIFLLDEPFG 183
Cdd:cd03230 81 EPSLYENLTVRENLKL------------------------------------SGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1956008863 184 ALDALTRHQMQNELLRIqSQQKMTTVFITHDVEEAVTLADRVVILK 229
Cdd:cd03230 125 GLDPESRREFWELLREL-KKEGKTILLSSHILEEAERLCDRVAILN 169
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
32-230 |
1.71e-45 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 151.89 E-value: 1.71e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 32 SFVVNQQPVkvIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDR-----AVVFQEHR 106
Cdd:COG4619 7 SFRVGGKPI--LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrrqvAYVPQEPA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 107 LFPwLTVEQNielglLNEALTSRDKDILVQKAIELIGLNGFEKAY----PHQLSGGMSQRVAIARSLVVQPRIFLLDEPF 182
Cdd:COG4619 85 LWG-GTVRDN-----LPFPFQLRERKFDRERALELLERLGLPPDIldkpVERLSGGERQRLALIRALLLQPDVLLLDEPT 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1956008863 183 GALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVILKP 230
Cdd:COG4619 159 SALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEA 206
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
26-235 |
1.86e-45 |
|
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: 152.72 E-value: 1.86e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 26 FHHVHKSFVvnqQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDR------- 98
Cdd:cd03256 3 VENLSKTYP---NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrrq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 99 -AVVFQEHRLFPWLTVEQNIELGLLNE-----ALTSRDKDILVQKAIEL---IGLNGFEKAYPHQLSGGMSQRVAIARSL 169
Cdd:cd03256 80 iGMIFQQFNLIERLSVLENVLSGRLGRrstwrSLFGLFPKEEKQRALAAlerVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1956008863 170 VVQPRIFLLDEPFGALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVILkpKPGRV 235
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGL--KDGRI 223
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
32-229 |
4.76e-45 |
|
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: 152.58 E-value: 4.76e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 32 SFVVNQQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVS------------GIggdra 99
Cdd:TIGR04520 7 SFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLdeenlweirkkvGM----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 100 vVFQ--EHRlFPWLTVEQNIELGLLNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFL 177
Cdd:TIGR04520 82 -VFQnpDNQ-FVGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIII 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1956008863 178 LDEPFGALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVtLADRVVILK 229
Cdd:TIGR04520 160 LDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMN 210
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
42-228 |
5.41e-45 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 151.78 E-value: 5.41e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 42 VIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDRAVVFQEH---RLFPwLTVEQNIE 118
Cdd:COG1121 21 VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIGYVPQRAevdWDFP-ITVRDVVL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 119 LGLLNEA-----LTSRDKDIlVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQM 193
Cdd:COG1121 100 MGRYGRRglfrrPSRADREA-VDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEAL 178
|
170 180 190
....*....|....*....|....*....|....*
gi 1956008863 194 QnELLRIQSQQKMTTVFITHDVEEAVTLADRVVIL 228
Cdd:COG1121 179 Y-ELLRELRREGKTILVVTHDLGAVREYFDRVLLL 212
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
41-228 |
1.03e-44 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 149.69 E-value: 1.03e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 41 KVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDRAV---------VFQEHRLFPWL 111
Cdd:TIGR03608 12 VILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASkfrreklgyLFQNFALIENE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 112 TVEQNIELGLLNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRH 191
Cdd:TIGR03608 92 TVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLDPKNRD 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 1956008863 192 QMQNELLRIQSQQKmTTVFITHDVEEAvTLADRVVIL 228
Cdd:TIGR03608 172 EVLDLLLELNDEGK-TIIIVTHDPEVA-KQADRVIEL 206
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
39-242 |
1.23e-43 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 147.71 E-value: 1.23e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 39 PVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDF-----DGRILIDGADVSGIGGDR-------AVVFQEHR 106
Cdd:cd03260 12 DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLLDGKDIYDLDVDVlelrrrvGMVFQKPN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 107 LFPwLTVEQNIELGL-LNEALTSRDKDILVQKAIELIGLNGFEK--AYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFG 183
Cdd:cd03260 92 PFP-GSIYDNVAYGLrLHGIKLKEELDERVEEALRKAALWDEVKdrLHALGLSGGQQQRLCLARALANEPEVLLLDEPTS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1956008863 184 ALDALTRHQMqnELLRIQSQQKMTTVFITHDVEEAVTLADRVVILkpKPGRVEQIIPVN 242
Cdd:cd03260 171 ALDPISTAKI--EELIAELKKEYTIVIVTHNMQQAARVADRTAFL--LNGRLVEFGPTE 225
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
24-228 |
1.14e-42 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 144.70 E-value: 1.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 24 VAFHHVHKSFvvnQQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDR----- 98
Cdd:TIGR02673 2 IEFHNVSKAY---PGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQlpllr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 99 ---AVVFQEHRLFPWLTVEQNIELGLLNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRI 175
Cdd:TIGR02673 79 rriGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1956008863 176 FLLDEPFGALDA-LTRHQMQneLLRIQSQQKMTTVFITHDVEEAVTLADRVVIL 228
Cdd:TIGR02673 159 LLADEPTGNLDPdLSERILD--LLKRLNKRGTTVIVATHDLSLVDRVAHRVIIL 210
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
43-238 |
3.83e-42 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 148.64 E-value: 3.83e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 43 IHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDR---------AVVFQEHRLFPWLTV 113
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevrrkkiAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 114 EQNIELGLLNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQM 193
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1956008863 194 QNELLRIQSQQKMTTVFITHDVEEAVTLADRVVILkpKPGRVEQI 238
Cdd:PRK10070 204 QDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIM--QNGEVVQV 246
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
24-226 |
5.73e-42 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 144.08 E-value: 5.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 24 VAFHHVHKSFvvnqQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSG-------IGG 96
Cdd:PRK09493 2 IEFKNVSKHF----GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkvderlIRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 97 DRAVVFQEHRLFPWLTVEQNIELGLLNEALTSRDKdiLVQKAIELIGLNGF-EKA--YPHQLSGGMSQRVAIARSLVVQP 173
Cdd:PRK09493 78 EAGMVFQQFYLFPHLTALENVMFGPLRVRGASKEE--AEKQARELLAKVGLaERAhhYPSELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1956008863 174 RIFLLDEPFGALDALTRHqmqnELLRIQ---SQQKMTTVFITHDVEEAVTLADRVV 226
Cdd:PRK09493 156 KLMLFDEPTSALDPELRH----EVLKVMqdlAEEGMTMVIVTHEIGFAEKVASRLI 207
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
42-229 |
7.79e-42 |
|
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: 142.67 E-value: 7.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 42 VIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDRAVVFQEH---RLFPwLTVEQNIE 118
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGYVPQRRsidRDFP-ISVRDVVL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 119 LGLLNEA-----LTSRDKDIlVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQM 193
Cdd:cd03235 93 MGLYGHKglfrrLSKADKAK-VDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDI 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 1956008863 194 QnELLRIQSQQKMTTVFITHDVEEAVTLADRVVILK 229
Cdd:cd03235 172 Y-ELLRELRREGMTILVVTHDLGLVLEYFDRVLLLN 206
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
26-229 |
1.18e-41 |
|
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: 140.46 E-value: 1.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 26 FHHVHKSFvvnqQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSgiggdravvfqeh 105
Cdd:cd00267 2 IENLSFRY----GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIA------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 106 rlfpwltveqnielgllnealtsRDKDILVQKAIELIglngfekaypHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGAL 185
Cdd:cd00267 65 -----------------------KLPLEELRRRIGYV----------PQLSGGQRQRVALARALLLNPDLLLLDEPTSGL 111
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1956008863 186 DALTRHQMQnELLRIQSQQKMTTVFITHDVEEAVTLADRVVILK 229
Cdd:cd00267 112 DPASRERLL-ELLRELAEEGRTVIIVTHDPELAELAADRVIVLK 154
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
41-226 |
2.23e-41 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 141.69 E-value: 2.23e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 41 KVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDRAV--------VFQEHRLFPWLT 112
Cdd:TIGR02982 19 QVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVqlrrrigyIFQAHNLLGFLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 113 VEQNIELGL-LNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRH 191
Cdd:TIGR02982 99 ARQNVQMALeLQPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAALDSKSGR 178
|
170 180 190
....*....|....*....|....*....|....*
gi 1956008863 192 QMQNELLRIQSQQKMTTVFITHDvEEAVTLADRVV 226
Cdd:TIGR02982 179 DVVELMQKLAKEQGCTILMVTHD-NRILDVADRIL 212
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
39-237 |
1.41e-40 |
|
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: 146.75 E-value: 1.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 39 PVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLdQDFDGRILIDGADVSGIGGD--RA------VVFQE--HRLF 108
Cdd:COG4172 298 HVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSRRalRPlrrrmqVVFQDpfGSLS 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 109 PWLTVEQNIE--LGLLNEALTSRDKDILVQKAIELIGLN-GFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGAL 185
Cdd:COG4172 377 PRMTVGQIIAegLRVHGPGLSAAERRARVAEALEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSAL 456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1956008863 186 DALTRHQMQNELLRIQSQQKMTTVFITHDVeeAV--TLADRVVILkpKPGR-VEQ 237
Cdd:COG4172 457 DVSVQAQILDLLRDLQREHGLAYLFISHDL--AVvrALAHRVMVM--KDGKvVEQ 507
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
43-228 |
1.56e-40 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 139.15 E-value: 1.56e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 43 IHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAG-LDQDF--DGRILIDGADVS-------GIGgdraVVFQEHRLFPWLT 112
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAFsaSGEVLLNGRRLTalpaeqrRIG----ILFQDDLLFPHLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 113 VEQNIELGLlNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQ 192
Cdd:COG4136 93 VGENLAFAL-PPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQ 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 1956008863 193 MQN---ELLRiqsQQKMTTVFITHDVEEAVtLADRVVIL 228
Cdd:COG4136 172 FREfvfEQIR---QRGIPALLVTHDEEDAP-AAGRVLDL 206
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
40-229 |
5.54e-40 |
|
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: 138.97 E-value: 5.54e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 40 VKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDR--------AVVFQEHRLFPWL 111
Cdd:TIGR02315 15 KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrklrrriGMIFQHYNLIERL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 112 TVEQNIELGLLNEA---------LTSRDKDILVQkAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPF 182
Cdd:TIGR02315 95 TVLENVLHGRLGYKptwrsllgrFSEEDKERALS-ALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILADEPI 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1956008863 183 GALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVILK 229
Cdd:TIGR02315 174 ASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLK 220
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
45-241 |
8.11e-40 |
|
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: 141.40 E-value: 8.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 45 DFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADV--SGIGGD-----RAV--VFQEHRLFPWLTVEQ 115
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdSRKGIFlppekRRIgyVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 116 NIELGLlnEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQMQN 195
Cdd:TIGR02142 95 NLRYGM--KRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1956008863 196 ELLRIQSQQKMTTVFITHDVEEAVTLADRVVILkpKPGRVEQIIPV 241
Cdd:TIGR02142 173 YLERLHAEFGIPILYVSHSLQEVLRLADRVVVL--EDGRVAAAGPI 216
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
42-230 |
1.60e-39 |
|
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: 136.45 E-value: 1.60e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 42 VIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADV----SGIGGDRAVVFQEHRLFPWLTVEQNi 117
Cdd:COG4133 17 LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIrdarEDYRRRLAYLGHADGLKPELTVREN- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 118 eLGLLNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQMQnEL 197
Cdd:COG4133 96 -LRFWAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLA-EL 173
|
170 180 190
....*....|....*....|....*....|...
gi 1956008863 198 LRIQSQQKMTTVFITHDVEEAvtLADRVVILKP 230
Cdd:COG4133 174 IAAHLARGGAVLLTTHQPLEL--AAARVLDLGD 204
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
38-225 |
2.68e-39 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 139.48 E-value: 2.68e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 38 QPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDRA--------VVFQEHR--L 107
Cdd:COG4608 29 GVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELrplrrrmqMVFQDPYasL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 108 FPWLTVEQNIELGLL-NEALTSRDKDILVQKAIELIGLN-GFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGAL 185
Cdd:COG4608 109 NPRMTVGDIIAEPLRiHGLASKAERRERVAELLELVGLRpEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSAL 188
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1956008863 186 DALTRHQMQNELLRIQSQQKMTTVFITHD---VEEavtLADRV 225
Cdd:COG4608 189 DVSIQAQVLNLLEDLQDELGLTYLFISHDlsvVRH---ISDRV 228
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
41-236 |
4.51e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 137.87 E-value: 4.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 41 KVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSG-------IGGDRAVVFQ--EHRLFPWl 111
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkvklsdIRKKVGLVFQypEYQLFEE- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 112 TVEQNIELGLLNEALTSRDKDILVQKAIELIGL--NGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALT 189
Cdd:PRK13637 100 TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKG 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1956008863 190 RHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVILkpKPGRVE 236
Cdd:PRK13637 180 RDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVM--NKGKCE 224
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
13-237 |
1.45e-38 |
|
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: 141.82 E-value: 1.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 13 HQSFQANTQTRVAFHHVHksfVVNQQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVS 92
Cdd:COG4988 326 TAPLPAAGPPSIELEDVS---FSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLS 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 93 GIGGDR-----AVVFQEHRLFPWlTVEQNIELGllNEALTsrdkDILVQKAIELIGLNGFEKAYPH-----------QLS 156
Cdd:COG4988 403 DLDPASwrrqiAWVPQNPYLFAG-TIRENLRLG--RPDAS----DEELEAALEAAGLDEFVAALPDgldtplgeggrGLS 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 157 GGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQMQNELLRIqSQQKmTTVFITHDvEEAVTLADRVVILkpKPGRVE 236
Cdd:COG4988 476 GGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRL-AKGR-TVILITHR-LALLAQADRILVL--DDGRIV 550
|
.
gi 1956008863 237 Q 237
Cdd:COG4988 551 E 551
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
29-229 |
1.45e-38 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 134.40 E-value: 1.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 29 VHKSFVVNQQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIG-GDRA-------- 99
Cdd:TIGR02211 7 LGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSsNERAklrnkklg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 100 VVFQEHRLFPWLTVEQNIELGLLNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLD 179
Cdd:TIGR02211 87 FIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLAD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1956008863 180 EPFGALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLaDRVVILK 229
Cdd:TIGR02211 167 EPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMK 215
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
34-229 |
2.81e-38 |
|
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: 133.69 E-value: 2.81e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 34 VVNQQP--VKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDR--------AVVFQ 103
Cdd:cd03292 6 VTKTYPngTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipylrrkiGVVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 104 EHRLFPWLTVEQNIELGLLNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFG 183
Cdd:cd03292 86 DFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTG 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1956008863 184 ALDALTrhqmQNELLRI--QSQQKMTTVFI-THDVEEAVTLADRVVILK 229
Cdd:cd03292 166 NLDPDT----TWEIMNLlkKINKAGTTVVVaTHAKELVDTTRHRVIALE 210
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
17-228 |
3.50e-38 |
|
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: 140.67 E-value: 3.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 17 QANTQTRVAFHHVhkSFVVNQQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGG 96
Cdd:COG4987 327 PAPGGPSLELEDV--SFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 97 DR-----AVVFQEHRLFPwLTVEQNIELGllNEALTsrDKDILvqKAIELIGLNGFEKAYPH-----------QLSGGMS 160
Cdd:COG4987 405 DDlrrriAVVPQRPHLFD-TTLRENLRLA--RPDAT--DEELW--AALERVGLGDWLAALPDgldtwlgeggrRLSGGER 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1956008863 161 QRVAIARSLVVQPRIFLLDEPFGALDALTRHQMQNELLRiQSQQKmTTVFITHDvEEAVTLADRVVIL 228
Cdd:COG4987 478 RRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLE-ALAGR-TVLLITHR-LAGLERMDRILVL 542
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
23-229 |
1.29e-37 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 139.14 E-value: 1.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 23 RVAFHHVHKSFVVNQQpvkVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDR---- 98
Cdd:COG1132 339 EIEFENVSFSYPGDRP---VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrrq 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 99 -AVVFQEHRLFPwLTVEQNIELGLLNealTSRDKdilVQKAIELIGLNGFEKAYPH-----------QLSGGMSQRVAIA 166
Cdd:COG1132 416 iGVVPQDTFLFS-GTIRENIRYGRPD---ATDEE---VEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIA 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1956008863 167 RSLVVQPRIFLLDEPFGALDALTRHQMQNELLRIqsQQKMTTVFITHDVeEAVTLADRVVILK 229
Cdd:COG1132 489 RALLKDPPILILDEATSALDTETEALIQEALERL--MKGRTTIVIAHRL-STIRNADRILVLD 548
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
42-229 |
1.93e-37 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 132.59 E-value: 1.93e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 42 VIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGD-----RAVVFQEHRL-FPWlTVEQ 115
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAelarrRAVLPQHSSLsFPF-TVEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 116 NIELGLLNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLV------VQPRIFLLDEPFGALDalT 189
Cdd:PRK13548 96 VVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALD--L 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1956008863 190 RHQMQneLLRIQSQ----QKMTTVFITHDVEEAVTLADRVVILK 229
Cdd:PRK13548 174 AHQHH--VLRLARQlaheRGLAVIVVLHDLNLAARYADRIVLLH 215
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
42-229 |
1.53e-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: 1.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 42 VIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGD-----RAVVFQEHRL-FPWlTVEQ 115
Cdd:COG4559 16 LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWelarrRAVLPQHSSLaFPF-TVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 116 NIELGLLNEALTSRDKDILVQKAIELIGLNGF-EKAYPhQLSGGMSQRVAIARSLV-------VQPRIFLLDEPFGALDa 187
Cdd:COG4559 95 VVALGRAPHGSSAAQDRQIVREALALVGLAHLaGRSYQ-TLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALD- 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1956008863 188 lTRHQMQneLLRIQSQ--QKMTTVF-ITHDVEEAVTLADRVVILK 229
Cdd:COG4559 173 -LAHQHA--VLRLARQlaRRGGGVVaVLHDLNLAAQYADRILLLH 214
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
23-228 |
1.73e-36 |
|
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: 128.86 E-value: 1.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 23 RVAFHHVhkSFVVNQQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIggDRAV-- 100
Cdd:cd03245 2 RIEFRNV--SFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQL--DPADlr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 101 -----VFQEHRLFpWLTVEQNIELGllneALTSRDKDILvqKAIELIGLNGFEKAYPH-----------QLSGGMSQRVA 164
Cdd:cd03245 78 rnigyVPQDVTLF-YGTLRDNITLG----APLADDERIL--RAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1956008863 165 IARSLVVQPRIFLLDEPFGALDaltrhqMQNELLRIQSQQKM----TTVFITHDVeEAVTLADRVVIL 228
Cdd:cd03245 151 LARALLNDPPILLLDEPTSAMD------MNSEERLKERLRQLlgdkTLIIITHRP-SLLDLVDRIIVM 211
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
27-228 |
3.39e-36 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 128.98 E-value: 3.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 27 HHVHKSFVVNQqpvkVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGA--DVSGIGGDRAV---- 100
Cdd:PRK11124 6 NGINCFYGAHQ----ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPSDKAIrelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 101 -----VFQEHRLFPWLTVEQN-IE-----LGLlnealtsrDKDILVQKAIELIG---LNGFEKAYPHQLSGGMSQRVAIA 166
Cdd:PRK11124 82 rnvgmVFQQYNLWPHLTVQQNlIEapcrvLGL--------SKDQALARAEKLLErlrLKPYADRFPLHLSGGQQQRVAIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1956008863 167 RSLVVQPRIFLLDEPFGALDALTRHQMQNeLLRIQSQQKMTTVFITHDVEEAVTLADRVVIL 228
Cdd:PRK11124 154 RALMMEPQVLLFDEPTAALDPEITAQIVS-IIRELAETGITQVIVTHEVEVARKTASRVVYM 214
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
32-237 |
1.31e-35 |
|
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: 133.27 E-value: 1.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 32 SFVVNQQPVKVIHDFNLEIKEGEFIAIVGSSGCGKS----TLLRLLAGLDQDFDGRILIDGADVSGI---------GGDR 98
Cdd:COG4172 15 AFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLserelrrirGNRI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 99 AVVFQE--HRLFPWLTVEQNI-ELGLLNEALTSRDkdiLVQKAIELIGLNGFE------KAYPHQLSGGMSQRVAIARSL 169
Cdd:COG4172 95 AMIFQEpmTSLNPLHTIGKQIaEVLRLHRGLSGAA---ARARALELLERVGIPdperrlDAYPHQLSGGQRQRVMIAMAL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1956008863 170 VVQPRIFLLDEPFGALDALTRHQMQNELLRIQSQQKMTTVFITHD---VEEavtLADRVVILkpKPGR-VEQ 237
Cdd:COG4172 172 ANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDlgvVRR---FADRVAVM--RQGEiVEQ 238
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
41-229 |
2.77e-35 |
|
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: 124.47 E-value: 2.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 41 KVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGG-----DRAVVFQehrlfpwltveq 115
Cdd:cd03214 13 TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPkelarKIAYVPQ------------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 116 nielgllnealtsrdkdilvqkAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDAltRHQMqn 195
Cdd:cd03214 81 ----------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDI--AHQI-- 134
|
170 180 190
....*....|....*....|....*....|....*...
gi 1956008863 196 ELL----RIQSQQKMTTVFITHDVEEAVTLADRVVILK 229
Cdd:cd03214 135 ELLellrRLARERGKTVVMVLHDLNLAARYADRVILLK 172
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
26-228 |
3.67e-35 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 128.77 E-value: 3.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 26 FHHVHKSFVVNQQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDR------- 98
Cdd:PRK11153 4 LKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkarrq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 99 -AVVFQEHRLFPWLTVEQNIELGLlneALTSRDKDILVQKA---IELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPR 174
Cdd:PRK11153 84 iGMIFQHFNLLSSRTVFDNVALPL---ELAGTPKAEIKARVtelLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1956008863 175 IFLLDEPFGALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVIL 228
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVI 214
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
26-228 |
3.49e-34 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 123.58 E-value: 3.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 26 FHHVHKSFVVNQqpvkVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLD-----------QDFDGRILIDGADVSGI 94
Cdd:COG4161 5 LKNINCFYGSHQ----ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLEtpdsgqlniagHQFDFSQKPSEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 95 GGDRAVVFQEHRLFPWLTVEQN-IE-----LGLLNEALTSRDKDILVQkaielIGLNGFEKAYPHQLSGGMSQRVAIARS 168
Cdd:COG4161 81 RQKVGMVFQQYNLWPHLTVMENlIEapckvLGLSKEQAREKAMKLLAR-----LRLTDKADRFPLHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 169 LVVQPRIFLLDEPFGALDALTRHQMQnELLRIQSQQKMTTVFITHDVEEAVTLADRVVIL 228
Cdd:COG4161 156 LMMEPQVLLFDEPTAALDPEITAQVV-EIIRELSQTGITQVIVTHEVEFARKVASQVVYM 214
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
19-229 |
5.40e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 123.95 E-value: 5.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 19 NTQTRVAFHHVHKSFVVNQQPVkvIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSG----- 93
Cdd:PRK13632 3 NKSVMIKVENVSFSYPNSENNA--LKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKenlke 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 94 ----IGgdraVVFQE-HRLFPWLTVEQNIELGLLNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARS 168
Cdd:PRK13632 81 irkkIG----IIFQNpDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1956008863 169 LVVQPRIFLLDEPFGALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVtLADRVVILK 229
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFS 216
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
42-228 |
7.95e-34 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 122.94 E-value: 7.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 42 VIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIdgADVSgIGGDRAV----------------VFQEH 105
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRV--GDIT-IDTARSLsqqkglirqlrqhvgfVFQNF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 106 RLFPWLTVEQNIELGLLneALTSRDKDILVQKAIEL---IGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPF 182
Cdd:PRK11264 95 NLFPHRTVLENIIEGPV--IVKGEPKEEATARARELlakVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1956008863 183 GALDAltrhQMQNELL---RIQSQQKMTTVFITHDVEEAVTLADRVVIL 228
Cdd:PRK11264 173 SALDP----ELVGEVLntiRQLAQEKRTMVIVTHEMSFARDVADRAIFM 217
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
42-228 |
9.60e-34 |
|
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: 121.77 E-value: 9.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 42 VIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDRAV------VFQEHRLFPWLTVEQ 115
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERAragigyVPEGRRIFPELTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 116 NIELGLLNEALTSRDKDIlvQKAIELiglngF--------EKAYphQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDA 187
Cdd:cd03224 95 NLLLGAYARRRAKRKARL--ERVYEL-----FprlkerrkQLAG--TLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1956008863 188 LTRHQMQNELLRIqSQQKMTTVFITHDVEEAVTLADRVVIL 228
Cdd:cd03224 166 KIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVL 205
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
43-238 |
9.96e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 123.69 E-value: 9.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 43 IHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDG-----ADVSGIGGDRAVVFQE-HRLFPWLTVEQN 116
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGdllteENVWDIRHKIGMVFQNpDNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 117 IELGLLNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQMQNE 196
Cdd:PRK13650 103 VAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKT 182
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1956008863 197 LLRIQSQQKMTTVFITHDVEEaVTLADRVVILkpKPGRVEQI 238
Cdd:PRK13650 183 IKGIRDDYQMTVISITHDLDE-VALSDRVLVM--KNGQVEST 221
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
20-229 |
1.06e-33 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 127.44 E-value: 1.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 20 TQTRVAFHHVHKSFVvnqqPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVS------- 92
Cdd:COG1129 1 AEPLLEMRGISKSFG----GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRfrsprda 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 93 ---GIggdrAVVFQEHRLFPWLTVEQNIELGllNEALTSR--DKDILVQKAIELIGLNGFEKAyPHQLSGGMS----QRV 163
Cdd:COG1129 77 qaaGI----AIIHQELNLVPNLSVAENIFLG--REPRRGGliDWRAMRRRARELLARLGLDID-PDTPVGDLSvaqqQLV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1956008863 164 AIARSLVVQPRIFLLDEPfgaLDALTRHQMQN--ELLRIQSQQKMTTVFITHDVEEAVTLADRVVILK 229
Cdd:COG1129 150 EIARALSRDARVLILDEP---TASLTEREVERlfRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLR 214
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
28-228 |
1.91e-33 |
|
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: 120.94 E-value: 1.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 28 HVHKSFVVNQQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVS--------GIGgdra 99
Cdd:cd03266 6 ALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVkepaearrRLG---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 100 VVFQEHRLFPWLTVEQNIEL-----GLLNEALTSRdkdilVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPR 174
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYfaglyGLKGDELTAR-----LEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1956008863 175 IFLLDEPFGALDALTRHQMQnELLRIQSQQKMTTVFITHDVEEAVTLADRVVIL 228
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALR-EFIRQLRALGKCILFSTHIMQEVERLCDRVVVL 209
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
41-229 |
2.20e-33 |
|
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: 120.44 E-value: 2.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 41 KVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDRAV--VFQE--HRLFPwLTVEQn 116
Cdd:cd03226 14 EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSIgyVMQDvdYQLFT-DSVRE- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 117 iELGLLNEALTSRDKDIlvQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDaltRHQMQN- 195
Cdd:cd03226 92 -ELLLGLKELDAGNEQA--ETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD---YKNMERv 165
|
170 180 190
....*....|....*....|....*....|....*
gi 1956008863 196 -ELLRIQSQQKMTTVFITHDVEEAVTLADRVVILK 229
Cdd:cd03226 166 gELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLA 200
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
43-229 |
2.59e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 122.82 E-value: 2.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 43 IHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIdGADVSGIGGDR----------AVVFQ--EHRLFPw 110
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGKKNkklkplrkkvGIVFQfpEHQLFE- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 111 LTVEQNIELGLLNEALTSRDKDILVQKAIELIGLNG--FEKAyPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDAL 188
Cdd:PRK13634 101 ETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEelLARS-PFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1956008863 189 TRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVILK 229
Cdd:PRK13634 180 GRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMH 220
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
27-228 |
2.70e-33 |
|
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: 121.68 E-value: 2.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 27 HHVHKSFvvnqQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDRAV------ 100
Cdd:COG0411 8 RGLTKRF----GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIArlgiar 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 101 VFQEHRLFPWLTVEQNIELG------------LLNEALTSRDKDILVQKAIELI---GLNGFEKAYPHQLSGGMSQRVAI 165
Cdd:COG0411 84 TFQNPRLFPELTVLENVLVAaharlgrgllaaLLRLPRARREEREARERAEELLervGLADRADEPAGNLSYGQQRRLEI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1956008863 166 ARSLVVQPRIFLLDEPFGALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVIL 228
Cdd:COG0411 164 ARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVL 226
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
28-228 |
3.48e-33 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 121.00 E-value: 3.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 28 HVHKSFvvnqQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDRAV------V 101
Cdd:cd03219 5 GLTKRF----GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIArlgigrT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 102 FQEHRLFPWLTVEQNIELGLL-------NEALTSRDKDILVQKA---IELIGLNGFEKAYPHQLSGGMSQRVAIARSLVV 171
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAQartgsglLLARARREEREARERAeelLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1956008863 172 QPRIFLLDEPFGALDALTRHQMQNELLRIqSQQKMTTVFITHDVEEAVTLADRVVIL 228
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVL 216
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
24-228 |
5.55e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 121.83 E-value: 5.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 24 VAFHHVhkSFVVNQQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGL---DQDFDGRILIDGADVSG-----IG 95
Cdd:PRK13640 6 VEFKHV--SFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTAktvwdIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 96 GDRAVVFQE-HRLFPWLTVEQNIELGLLNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPR 174
Cdd:PRK13640 84 EKVGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPK 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1956008863 175 IFLLDEPFGALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVtLADRVVIL 228
Cdd:PRK13640 164 IIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVL 216
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
28-229 |
1.61e-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: 118.76 E-value: 1.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 28 HVHKSFvvNQQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADV--------SGIGgdra 99
Cdd:cd03263 5 NLTKTY--KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIrtdrkaarQSLG---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 100 VVFQEHRLFPWLTVEQNIELGLLNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLD 179
Cdd:cd03263 79 YCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1956008863 180 EPFGALDALTRHQMQNELLRIQSQQkmTTVFITHDVEEAVTLADRVVILK 229
Cdd:cd03263 159 EPTSGLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMS 206
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
29-228 |
3.74e-32 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 120.45 E-value: 3.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 29 VHKSFVVNQQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVsgIGGDRA--------- 99
Cdd:PRK11308 17 VKRGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDL--LKADPEaqkllrqki 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 100 -VVFQE--HRLFPWLTVEQNIELGLL-NEALTSRDKDILVQKAIELIGLNG-FEKAYPHQLSGGMSQRVAIARSLVVQPR 174
Cdd:PRK11308 95 qIVFQNpyGSLNPRKKVGQILEEPLLiNTSLSAAERREKALAMMAKVGLRPeHYDRYPHMFSGGQRQRIAIARALMLDPD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1956008863 175 IFLLDEPFGALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVIL 228
Cdd:PRK11308 175 VVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVM 228
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
24-235 |
4.47e-32 |
|
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: 118.03 E-value: 4.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 24 VAFHHVHksFVVNQQP-VKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADV---------SG 93
Cdd:cd03249 1 IEFKNVS--FRYPSRPdVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIrdlnlrwlrSQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 94 IGgdraVVFQEHRLFPwLTVEQNIELGLlNEAltsrdKDILVQKAIELIGLNGFEKAYPH-----------QLSGGMSQR 162
Cdd:cd03249 79 IG----LVSQEPVLFD-GTIAENIRYGK-PDA-----TDEEVEEAAKKANIHDFIMSLPDgydtlvgergsQLSGGQKQR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1956008863 163 VAIARSLVVQPRIFLLDEPFGALDALTRHQMQNELLRIqsQQKMTTVFITHDVeEAVTLADRVVILkpKPGRV 235
Cdd:cd03249 148 IAIARALLRNPKILLLDEATSALDAESEKLVQEALDRA--MKGRTTIVIAHRL-STIRNADLIAVL--QNGQV 215
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
43-229 |
4.89e-32 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 117.85 E-value: 4.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 43 IHDFNLEIKEGEFIAIVGSSGCGKST----LLRLLAGLDQDFDGRILIDGADVSGI---GGDRAVVFQEHR--LFPWLTV 113
Cdd:TIGR02770 2 VQDLNLSLKRGEVLALVGESGSGKSLtclaILGLLPPGLTQTSGEILLDGRPLLPLsirGRHIATIMQNPRtaFNPLFTM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 114 -EQNIELGLLNEALTSRDKDILVQkAIELIGLNGFE---KAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALT 189
Cdd:TIGR02770 82 gNHAIETLRSLGKLSKQARALILE-ALEAVGLPDPEevlKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1956008863 190 RHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVILK 229
Cdd:TIGR02770 161 QARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMD 200
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
42-228 |
5.22e-32 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 116.56 E-value: 5.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 42 VIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRilidgadVSGIGGDR-AVVFQEHRL---FPwLTVEQNI 117
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGT-------VRRAGGARvAYVPQRSEVpdsLP-LTVRDLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 118 ELGL-----LNEALTSRDKDIlVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQ 192
Cdd:NF040873 79 AMGRwarrgLWRRLTRDDRAA-VDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRER 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 1956008863 193 MqNELLRIQSQQKMTTVFITHDvEEAVTLADRVVIL 228
Cdd:NF040873 158 I-IALLAEEHARGATVVVVTHD-LELVRRADPCVLL 191
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
24-228 |
5.91e-32 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 118.37 E-value: 5.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 24 VAFHHVHKSFVVNQQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDRA---- 99
Cdd:TIGR02769 8 VTHTYRTGGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRrafr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 100 ----VVFQE--HRLFPWLTVEQNIELGLLNeaLTSRDKDILVQKAIELIGLNGFE----KAYPHQLSGGMSQRVAIARSL 169
Cdd:TIGR02769 88 rdvqLVFQDspSAVNPRMTVRQIIGEPLRH--LTSLDESEQKARIAELLDMVGLRsedaDKLPRQLSGGQLQRINIARAL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1956008863 170 VVQPRIFLLDEPFGALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVIL 228
Cdd:TIGR02769 166 AVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVM 224
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
30-228 |
7.86e-32 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 118.58 E-value: 7.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 30 HKSFVVNQQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDG-----ADVSGIGGDRAVVFQE 104
Cdd:PRK13635 10 HISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGmvlseETVWDVRRQVGMVFQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 105 -HRLFPWLTVEQNIELGLLNEALtSRDKDI-LVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPF 182
Cdd:PRK13635 90 pDNQFVGATVQDDVAFGLENIGV-PREEMVeRVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEAT 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1956008863 183 GALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTlADRVVIL 228
Cdd:PRK13635 169 SMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVM 213
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
24-229 |
9.73e-32 |
|
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: 114.83 E-value: 9.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 24 VAFHHVHKSFvvnqQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDRAvvfq 103
Cdd:cd03216 1 LELRGITKRF----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDA---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 104 ehrlfpwltveqnIELGllnealtsrdkdilvqkaIELIglngfekaypHQLSGGMSQRVAIARSLVVQPRIFLLDEPFG 183
Cdd:cd03216 73 -------------RRAG------------------IAMV----------YQLSVGERQMVEIARALARNARLLILDEPTA 111
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1956008863 184 aldALTRHQMQN--ELLRIQSQQKMTTVFITHDVEEAVTLADRVVILK 229
Cdd:cd03216 112 ---ALTPAEVERlfKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLR 156
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
28-229 |
1.10e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 117.88 E-value: 1.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 28 HVHKSFV---VNQqpVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAG---LDQdfdGRILIDGADVSG-------- 93
Cdd:COG1101 6 NLSKTFNpgtVNE--KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGslpPDS---GSILIDGKDVTKlpeykrak 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 94 -IGgdRavVFQEHRL--FPWLTVEQNIELGL-------LNEALTSRDKDILvQKAIELIGLnGFE---KAYPHQLSGGms 160
Cdd:COG1101 81 yIG--R--VFQDPMMgtAPSMTIEENLALAYrrgkrrgLRRGLTKKRRELF-RELLATLGL-GLEnrlDTKVGLLSGG-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 161 QRVAIarSLV----VQPRIFLLDEPFGALD--------ALTRhqmqnellRIQSQQKMTTVFITHDVEEAVTLADRVVIL 228
Cdd:COG1101 153 QRQAL--SLLmatlTKPKLLLLDEHTAALDpktaalvlELTE--------KIVEENNLTTLMVTHNMEQALDYGNRLIMM 222
|
.
gi 1956008863 229 K 229
Cdd:COG1101 223 H 223
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
39-228 |
1.34e-31 |
|
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: 116.62 E-value: 1.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 39 PVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDRAV------VFQEHRLFPWLT 112
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIArlgigyVPEGRRIFPSLT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 113 VEQNIELGllneALTSRDKDiLVQKAIELIglngFE-----KAYPHQ----LSGGMSQRVAIARSLVVQPRIFLLDEPFG 183
Cdd:COG0410 95 VEENLLLG----AYARRDRA-EVRADLERV----YElfprlKERRRQragtLSGGEQQMLAIGRALMSRPKLLLLDEPSL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1956008863 184 ALDALTRHQMQNELLRIQsQQKMTTVFITHDVEEAVTLADRVVIL 228
Cdd:COG0410 166 GLAPLIVEEIFEIIRRLN-REGVTILLVEQNARFALEIADRAYVL 209
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
24-235 |
1.39e-31 |
|
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: 116.56 E-value: 1.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 24 VAFHHVHKSFVVNQQpvkVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDR----- 98
Cdd:cd03253 1 IEFENVTFAYDPGRP---VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSlrrai 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 99 AVVFQEHRLFPwLTVEQNIELGLLNealTSRDKDILVQKAIELIG-LNGFEKAYPHQ-------LSGGMSQRVAIARSLV 170
Cdd:cd03253 78 GVVPQDTVLFN-DTIGYNIRYGRPD---ATDEEVIEAAKAAQIHDkIMRFPDGYDTIvgerglkLSGGEKQRVAIARAIL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1956008863 171 VQPRIFLLDEPFGALDALTRHQMQNELLRIQSQQkmTTVFITHDVEEAVTlADRVVILkpKPGRV 235
Cdd:cd03253 154 KNPPILLLDEATSALDTHTEREIQAALRDVSKGR--TTIVIAHRLSTIVN-ADKIIVL--KDGRI 213
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
41-229 |
2.14e-31 |
|
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: 115.37 E-value: 2.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 41 KVIHDFNLEIKEGeFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIG-GDRAVVF---QEHRLFPWLTVEQN 116
Cdd:cd03264 14 RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPqKLRRRIGylpQEFGVYPNFTVREF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 117 IE-LGLLNEaLTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQMQN 195
Cdd:cd03264 93 LDyIAWLKG-IPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRN 171
|
170 180 190
....*....|....*....|....*....|....
gi 1956008863 196 eLLRIQSQQKmTTVFITHDVEEAVTLADRVVILK 229
Cdd:cd03264 172 -LLSELGEDR-IVILSTHIVEDVESLCNQVAVLN 203
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
36-228 |
6.61e-31 |
|
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: 113.08 E-value: 6.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 36 NQQPVkvIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIG----GDR-AVVFQEHRLFPW 110
Cdd:cd03246 13 AEPPV--LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDpnelGDHvGYLPQDDELFSG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 111 lTVEQNIelgllnealtsrdkdilvqkaieliglngfekayphqLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDaLTR 190
Cdd:cd03246 91 -SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLD-VEG 131
|
170 180 190
....*....|....*....|....*....|....*...
gi 1956008863 191 HQMQNELLRIQSQQKMTTVFITHDvEEAVTLADRVVIL 228
Cdd:cd03246 132 ERALNQAIAALKAAGATRIVIAHR-PETLASADRILVL 168
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
27-229 |
7.98e-31 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 115.32 E-value: 7.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 27 HHVHKSFVVN-----QQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGigGDRAV- 100
Cdd:COG4167 8 RNLSKTFKYRtglfrRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEY--GDYKYr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 101 ------VFQ--EHRLFPWLTVEQNIELGL-LNEALTSRDKDILVQKAIELIGLNGfEKA--YPHQLSGGMSQRVAIARSL 169
Cdd:COG4167 86 ckhirmIFQdpNTSLNPRLNIGQILEEPLrLNTDLTAEEREERIFATLRLVGLLP-EHAnfYPHMLSSGQKQRVALARAL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 170 VVQPRIFLLDEPFGALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVILK 229
Cdd:COG4167 165 ILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMH 224
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
41-228 |
8.73e-31 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 119.70 E-value: 8.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 41 KVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDR-----AVVFQEHRLFPWlTVEQ 115
Cdd:TIGR02857 336 PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSwrdqiAWVPQHPFLFAG-TIAE 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 116 NIELGlLNEAltsrdKDILVQKAIELIGLNGFEKAYP-----------HQLSGGMSQRVAIARSLVVQPRIFLLDEPFGA 184
Cdd:TIGR02857 415 NIRLA-RPDA-----SDAEIREALERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLALARAFLRDAPLLLLDEPTAH 488
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1956008863 185 LDALTRHQMQNELLRIQSQQkmTTVFITHDvEEAVTLADRVVIL 228
Cdd:TIGR02857 489 LDAETEAEVLEALRALAQGR--TVLLVTHR-LALAALADRIVVL 529
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
47-261 |
1.13e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 115.56 E-value: 1.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 47 NLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGA----DVSGIGGDR---AVVFQ--EHRLF-PwlTVEQN 116
Cdd:PRK13639 22 NFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpikyDKKSLLEVRktvGIVFQnpDDQLFaP--TVEED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 117 IELGLLNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQMQNe 196
Cdd:PRK13639 100 VAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMK- 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1956008863 197 LLRIQSQQKMTTVFITHDVEEAVTLADRVVIL---------KPKP--GRVEQIIPVNLPRPRNRSSFELHQLKEQI 261
Cdd:PRK13639 179 LLYDLNKEGITIIISTHDVDLVPVYADKVYVMsdgkiikegTPKEvfSDIETIRKANLRLPRVAHLIEILNKEDNL 254
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
29-229 |
1.51e-30 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 119.83 E-value: 1.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 29 VHKSFVVNQQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDR---------A 99
Cdd:PRK10535 10 IRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAlaqlrrehfG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 100 VVFQEHRLFPWLTVEQNIELGLLNEALTSRDKdilVQKAIELIGLNGFEKA---YPHQLSGGMSQRVAIARSLVVQPRIF 176
Cdd:PRK10535 90 FIFQRYHLLSHLTAAQNVEVPAVYAGLERKQR---LLRAQELLQRLGLEDRveyQPSQLSGGQQQRVSIARALMNGGQVI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1956008863 177 LLDEPFGALDALTRHQMQNELLRIQsQQKMTTVFITHDVEEAVTlADRVVILK 229
Cdd:PRK10535 167 LADEPTGALDSHSGEEVMAILHQLR-DRGHTVIIVTHDPQVAAQ-AERVIEIR 217
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
42-225 |
1.82e-30 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 113.76 E-value: 1.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 42 VIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGI-GGDRA--------VVFQEHRLFPWLT 112
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLsSAAKAelrnqklgFIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 113 VEQNIELGLLneaLTSRDKDILVQKAIELIGLNGFEKAYPH---QLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALT 189
Cdd:PRK11629 104 ALENVAMPLL---IGKKKPAEINSRALEMLAAVGLEHRANHrpsELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN 180
|
170 180 190
....*....|....*....|....*....|....*.
gi 1956008863 190 RHQMQNELLRIQSQQKMTTVFITHDVEeavtLADRV 225
Cdd:PRK11629 181 ADSIFQLLGELNRLQGTAFLVVTHDLQ----LAKRM 212
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
41-228 |
2.03e-30 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. 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. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 115.18 E-value: 2.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 41 KVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADV--------SGIGgdraVVFQEHRLFPWLT 112
Cdd:TIGR01188 7 KAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVvreprkvrRSIG----IVPQYASVDEDLT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 113 VEQNIEL-----GLLNEALTSRDKDILvqkaiELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDA 187
Cdd:TIGR01188 83 GRENLEMmgrlyGLPKDEAEERAEELL-----ELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1956008863 188 LTRHQMQnELLRIQSQQKMTTVFITHDVEEAVTLADRVVIL 228
Cdd:TIGR01188 158 RTRRAIW-DYIRALKEEGVTILLTTHYMEEADKLCDRIAII 197
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
40-229 |
3.09e-30 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 112.85 E-value: 3.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 40 VKVIHDF------NLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVS--------GIGgdraVVFQEH 105
Cdd:cd03265 7 VKKYGDFeavrgvSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVreprevrrRIG----IVFQDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 106 RLFPWLTVEQNIEL-----GLLNEALTSRdkdilVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDE 180
Cdd:cd03265 83 SVDDELTGWENLYIharlyGVPGAERRER-----IDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1956008863 181 PFGALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVILK 229
Cdd:cd03265 158 PTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIID 206
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
41-225 |
3.53e-30 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 113.59 E-value: 3.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 41 KVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGL-----DQDFDGRILIDGADVSGIGGD-----RAV--VFQEHRLF 108
Cdd:COG1117 25 QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndlipGARVEGEILLDGEDIYDPDVDvvelrRRVgmVFQKPNPF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 109 PwLTVEQNIELGL-LNEALTSRDKDILVQKAIELIGL----------NGFEkayphqLSGGMSQRVAIARSLVVQPRIFL 177
Cdd:COG1117 105 P-KSIYDNVAYGLrLHGIKSKSELDEIVEESLRKAALwdevkdrlkkSALG------LSGGQQQRLCIARALAVEPEVLL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1956008863 178 LDEPFGALDALTRHQMQnELLRiQSQQKMTTVFITHDVEEAVTLADRV 225
Cdd:COG1117 178 MDEPTSALDPISTAKIE-ELIL-ELKKDYTIVIVTHNMQQAARVSDYT 223
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
41-228 |
5.79e-30 |
|
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: 112.25 E-value: 5.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 41 KVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVS----------GIGgdraVVFQEHRLFPW 110
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITklpmhkrarlGIG----YLPQEASIFRK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 111 LTVEQNIELGLlneALTSRDKDILVQKAIELIGLNGFE-----KAYphQLSGGMSQRVAIARSLVVQPRIFLLDEPFGAL 185
Cdd:cd03218 90 LTVEENILAVL---EIRGLSKKEREEKLEELLEEFHIThlrksKAS--SLSGGERRRVEIARALATNPKFLLLDEPFAGV 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1956008863 186 DALTRHQMQNeLLRIQSQQKMtTVFIT-HDVEEAVTLADRVVIL 228
Cdd:cd03218 165 DPIAVQDIQK-IIKILKDRGI-GVLITdHNVRETLSITDRAYII 206
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
24-228 |
7.16e-30 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 113.24 E-value: 7.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 24 VAFHHVHKSFVVNQQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDRA---- 99
Cdd:PRK10419 9 LSHHYAHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRkafr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 100 ----VVFQEH--RLFPWLTVEQNIELGLLNeaLTSRDKDILVQKAIELIGLNGFEKAY----PHQLSGGMSQRVAIARSL 169
Cdd:PRK10419 89 rdiqMVFQDSisAVNPRKTVREIIREPLRH--LLSLDKAERLARASEMLRAVDLDDSVldkrPPQLSGGQLQRVCLARAL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1956008863 170 VVQPRIFLLDEPFGALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVIL 228
Cdd:PRK10419 167 AVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVM 225
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
42-229 |
2.20e-29 |
|
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: 110.78 E-value: 2.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 42 VIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDR-----AVVFQEHRLFPWlTVEQN 116
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlrsmiGVVLQDTFLFSG-TIMEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 117 IELGllneALTSRDKDilVQKAIELIGLNGF----EKAYPHQ-------LSGGMSQRVAIARSLVVQPRIFLLDEPFGAL 185
Cdd:cd03254 97 IRLG----RPNATDEE--VIEAAKEAGAHDFimklPNGYDTVlgenggnLSQGERQLLAIARAMLRDPKILILDEATSNI 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1956008863 186 DALTRHQMQNELLRIqsQQKMTTVFITHDVeEAVTLADRVVILK 229
Cdd:cd03254 171 DTETEKLIQEALEKL--MKGRTSIIIAHRL-STIKNADKILVLD 211
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
41-229 |
2.48e-29 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 110.00 E-value: 2.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 41 KVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDRAVV---FQEHRLFPWLTVEQNI 117
Cdd:cd03268 14 RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIgalIEAPGFYPNLTARENL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 118 ELGLLneALTSRDKDIlvQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQMQNEL 197
Cdd:cd03268 94 RLLAR--LLGIRKKRI--DEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELI 169
|
170 180 190
....*....|....*....|....*....|...
gi 1956008863 198 LRIQSQQKmtTVFI-THDVEEAVTLADRVVILK 229
Cdd:cd03268 170 LSLRDQGI--TVLIsSHLLSEIQKVADRIGIIN 200
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
24-228 |
3.08e-29 |
|
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: 110.65 E-value: 3.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 24 VAFHHVhkSFVVNQQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIggDRA---- 99
Cdd:cd03252 1 ITFEHV--RFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALA--DPAwlrr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 100 ---VVFQEHRLFPwLTVEQNIELGllNEALTSRDkdilVQKAIELIGLNGFEKAYPH-----------QLSGGMSQRVAI 165
Cdd:cd03252 77 qvgVVLQENVLFN-RSIRDNIALA--DPGMSMER----VIEAAKLAGAHDFISELPEgydtivgeqgaGLSGGQRQRIAI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1956008863 166 ARSLVVQPRIFLLDEPFGALDALTRHQMQNELLRIQSQQkmTTVFITHDVeEAVTLADRVVIL 228
Cdd:cd03252 150 ARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGR--TVIIIAHRL-STVKNADRIIVM 209
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
42-228 |
1.11e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 110.18 E-value: 1.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 42 VIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGG-----DRA-VVFQ--EHRLFPWLtV 113
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENlwdirNKAgMVFQnpDNQIVATI-V 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 114 EQNIELGLLNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQM 193
Cdd:PRK13633 104 EEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREV 183
|
170 180 190
....*....|....*....|....*....|....*
gi 1956008863 194 QNELLRIQSQQKMTTVFITHDVEEAVTlADRVVIL 228
Cdd:PRK13633 184 VNTIKELNKKYGITIILITHYMEEAVE-ADRIIVM 217
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
24-218 |
1.96e-28 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 108.33 E-value: 1.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 24 VAFHHVHKSFVVNQQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGD-----R 98
Cdd:PRK10584 7 VEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraklR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 99 A----VVFQEHRLFPWLTVEQNIELGLLNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPR 174
Cdd:PRK10584 87 AkhvgFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1956008863 175 IFLLDEPFGALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEA 218
Cdd:PRK10584 167 VLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLA 210
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
42-214 |
3.18e-28 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 112.84 E-value: 3.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 42 VIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGD---RAVVF--QEHRLFPwLTVEQN 116
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDevrRRVSVcaQDAHLFD-TTVREN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 117 IELGllneALTSRDKDILvqKAIELIGLNGFEKAYPH-----------QLSGGMSQRVAIARSLVVQPRIFLLDEPFGAL 185
Cdd:TIGR02868 429 LRLA----RPDATDEELW--AALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLLDEPTEHL 502
|
170 180
....*....|....*....|....*....
gi 1956008863 186 DALTRHQMQNELLriQSQQKMTTVFITHD 214
Cdd:TIGR02868 503 DAETADELLEDLL--AALSGRTVVLITHH 529
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
19-228 |
4.85e-28 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 112.04 E-value: 4.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 19 NTQTRVAFHHVHKSFvvnqQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVS------ 92
Cdd:COG3845 1 MMPPALELRGITKRF----GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRirsprd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 93 ----GIGgdraVVFQEHRLFPWLTVEQNIELGLLNEALTSRDKDILVQKAIELIGLNGFE---KAYPHQLSGGMSQRVAI 165
Cdd:COG3845 77 aialGIG----MVHQHFMLVPNLTVAENIVLGLEPTKGGRLDRKAARARIRELSERYGLDvdpDAKVEDLSVGEQQRVEI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1956008863 166 ARSLVVQPRIFLLDEP------------FGALDALTRhqmqnellriqsqQKMTTVFITHDVEEAVTLADRVVIL 228
Cdd:COG3845 153 LKALYRGARILILDEPtavltpqeadelFEILRRLAA-------------EGKSIIFITHKLREVMAIADRVTVL 214
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
31-229 |
6.41e-28 |
|
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: 106.85 E-value: 6.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 31 KSFVVNQQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGdrAVVFQehrlfPW 110
Cdd:cd03220 26 LGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGL--GGGFN-----PE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 111 LTVEQNIELGLLNEALTSRDKDILVQKAIELIGLNGFE----KAYphqlSGGMSQRVAIARSLVVQPRIFLLDEPFGALD 186
Cdd:cd03220 99 LTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIdlpvKTY----SSGMKARLAFAIATALEPDILLIDEVLAVGD 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1956008863 187 ALTRHQMQnELLRIQSQQKMTTVFITHDVEEAVTLADRVVILK 229
Cdd:cd03220 175 AAFQEKCQ-RRLRELLKQGKTVILVSHDPSSIKRLCDRALVLE 216
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
38-228 |
8.09e-28 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 109.03 E-value: 8.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 38 QPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGD--RAV------VFQE--HRL 107
Cdd:PRK15079 32 KTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDewRAVrsdiqmIFQDplASL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 108 FPWLTVEQNIE--LGLLNEALTSRDKDILVQKAIELIGL--NGFEKaYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFG 183
Cdd:PRK15079 112 NPRMTIGEIIAepLRTYHPKLSRQEVKDRVKAMMLKVGLlpNLINR-YPHEFSGGQCQRIGIARALILEPKLIICDEPVS 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1956008863 184 ALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVIL 228
Cdd:PRK15079 191 ALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVM 235
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
27-239 |
1.10e-27 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 106.71 E-value: 1.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 27 HHVHKSFvvnqQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLdQDFD-GRILIDGADVSGIGGDR-----AV 100
Cdd:COG4604 5 KNVSKRY----GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRL-LPPDsGEVLVDGLDVATTPSRElakrlAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 101 VFQEHRLFPWLTVEQNIELGLL---NEALTSRDKDIlVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFL 177
Cdd:COG4604 80 LRQENHINSRLTVRELVAFGRFpysKGRLTAEDREI-IDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1956008863 178 LDEPFGALDalTRH--QMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVILKP----KPGRVEQII 239
Cdd:COG4604 159 LDEPLNNLD--MKHsvQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDgrvvAQGTPEEII 224
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
40-239 |
1.15e-27 |
|
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: 111.05 E-value: 1.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 40 VKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDG----RILIDGADVSGIGGD---RA-----VVFQEHRL 107
Cdd:TIGR03269 297 VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevnvRVGDEWVDMTKPGPDgrgRAkryigILHQEYDL 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 108 FPWLTVEQNielglLNEALTSRDKDIL-VQKAIELIGLNGF--EKA------YPHQLSGGMSQRVAIARSLVVQPRIFLL 178
Cdd:TIGR03269 377 YPHRTVLDN-----LTEAIGLELPDELaRMKAVITLKMVGFdeEKAeeildkYPDELSEGERHRVALAQVLIKEPRIVIL 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1956008863 179 DEPFGALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVILKP----KPGRVEQII 239
Cdd:TIGR03269 452 DEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDgkivKIGDPEEIV 516
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
24-229 |
1.44e-27 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 105.44 E-value: 1.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 24 VAFHHVHKSFvvnqQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDRAVVFQ 103
Cdd:cd03269 1 LEVENVTKRF----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 104 EHR-LFPWLTV-EQNIELGLLnEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEP 181
Cdd:cd03269 77 EERgLYPKMKViDQLVYLAQL-KGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1956008863 182 FGALDALTRHQMQNELLRIQSQQKmTTVFITHDVEEAVTLADRVVILK 229
Cdd:cd03269 156 FSGLDPVNVELLKDVIRELARAGK-TVILSTHQMELVEELCDRVLLLN 202
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
24-228 |
2.07e-27 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 105.78 E-value: 2.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 24 VAFHHVhkSFVVNQQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDR----- 98
Cdd:cd03251 1 VEFKNV--TFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlrrqi 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 99 AVVFQEHRLFPWlTVEQNIELGLLNEaltSRDKdilVQKAIELIGLNGFEKAYPH-----------QLSGGMSQRVAIAR 167
Cdd:cd03251 79 GLVSQDVFLFND-TVAENIAYGRPGA---TREE---VEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1956008863 168 SLVVQPRIFLLDEPFGALDALTRHQMQNELLRIqsQQKMTTVFITHDVeEAVTLADRVVIL 228
Cdd:cd03251 152 ALLKDPPILILDEATSALDTESERLVQAALERL--MKNRTTFVIAHRL-STIENADRIVVL 209
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
35-229 |
2.48e-27 |
|
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: 104.47 E-value: 2.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 35 VNQQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILidgadvsgIGGDRAVVFQEhrlfPWL--- 111
Cdd:cd03250 13 GEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVS--------VPGSIAYVSQE----PWIqng 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 112 TVEQNIELGL------LNEALTS----RDKDILVQKAIELIGLNGFekayphQLSGGMSQRVAIARSLVVQPRIFLLDEP 181
Cdd:cd03250 81 TIRENILFGKpfdeerYEKVIKAcalePDLEILPDGDLTEIGEKGI------NLSGGQKQRISLARAVYSDADIYLLDDP 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1956008863 182 FGALDALT-RHQMQNELLRIQSQQKmTTVFITHDVeEAVTLADRVVILK 229
Cdd:cd03250 155 LSAVDAHVgRHIFENCILGLLLNNK-TRILVTHQL-QLLPHADQIVVLD 201
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
41-229 |
2.59e-27 |
|
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: 104.05 E-value: 2.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 41 KVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVS----------GIG---GDRavvfQEHRL 107
Cdd:cd03215 14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTrrsprdairaGIAyvpEDR----KREGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 108 FPWLTVEQNIELgllnealtsrdkdilvqkaieliglngfekayPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDA 187
Cdd:cd03215 90 VLDLSVAENIAL--------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDV 137
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1956008863 188 LTRHQMQnELLRIQSQQKMTTVFITHDVEEAVTLADRVVILK 229
Cdd:cd03215 138 GAKAEIY-RLIRELADAGKAVLLISSELDELLGLCDRILVMY 178
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
39-228 |
7.29e-27 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 106.36 E-value: 7.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 39 PVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLdQDFDGRIL-----IDGADVSGI---------GGDRAVVFQE 104
Cdd:PRK11022 19 PFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGL-IDYPGRVMaekleFNGQDLQRIsekerrnlvGAEVAMIFQD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 105 --HRLFPWLTVEQNIElgllnEALTSR---DKDILVQKAIELIGLNGFE------KAYPHQLSGGMSQRVAIARSLVVQP 173
Cdd:PRK11022 98 pmTSLNPCYTVGFQIM-----EAIKVHqggNKKTRRQRAIDLLNQVGIPdpasrlDVYPHQLSGGMSQRVMIAMAIACRP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1956008863 174 RIFLLDEPFGALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVIL 228
Cdd:PRK11022 173 KLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVM 227
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
42-228 |
1.25e-26 |
|
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: 103.37 E-value: 1.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 42 VIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVS----------GIggdrAVVFQEHRLFPWL 111
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITklppheraraGI----AYVPQGREIFPRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 112 TVEQNIELGLlnEALTSRDKDIlvqkaIELIglngFE-----KAYPHQ----LSGGMSQRVAIARSLVVQPRIFLLDEPF 182
Cdd:TIGR03410 91 TVEENLLTGL--AALPRRSRKI-----PDEI----YElfpvlKEMLGRrggdLSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1956008863 183 GALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVIL 228
Cdd:TIGR03410 160 EGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVM 205
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
57-228 |
1.78e-26 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 105.73 E-value: 1.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 57 AIVGSSGCGKSTLLRLLAGLDQDFDGRILIDG---ADVSG----------IGgdraVVFQEHRLFPWLTVEQNIELGLln 123
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAEKgiclppekrrIG----YVFQDARLFPHYKVRGNLRYGM-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 124 ealtSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQMQNELLRIQSQ 203
Cdd:PRK11144 102 ----AKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLARE 177
|
170 180
....*....|....*....|....*
gi 1956008863 204 QKMTTVFITHDVEEAVTLADRVVIL 228
Cdd:PRK11144 178 INIPILYVSHSLDEILRLADRVVVL 202
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
41-228 |
5.00e-26 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 102.92 E-value: 5.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 41 KVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDR--------AVVFQEHRLFPWLT 112
Cdd:PRK11831 21 CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRlytvrkrmSMLFQSGALFTDMN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 113 VEQNIELGL-----LNEALTSRdkdiLVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDA 187
Cdd:PRK11831 101 VFDNVAYPLrehtqLPAPLLHS----TVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDP 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1956008863 188 LTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVIL 228
Cdd:PRK11831 177 ITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIV 217
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
48-187 |
6.30e-26 |
|
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: 100.90 E-value: 6.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 48 LEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGD--RAVVFQEHR--LFPWLTVEQNieLGLLN 123
Cdd:TIGR01189 21 FTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEphENILYLGHLpgLKPELSALEN--LHFWA 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1956008863 124 EALTSRDKDILvqKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDA 187
Cdd:TIGR01189 99 AIHGGAQRTIE--DALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
41-249 |
7.20e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 102.94 E-value: 7.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 41 KVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDR---------AVVFQ--EHRLFP 109
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKyirpvrkriGMVFQfpESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 110 wLTVEQNIELGLLNEALtsrDKDILVQKAIELIGLNGFEK----AYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGAL 185
Cdd:PRK13646 101 -DTVEREIIFGPKNFKM---NLDEVKNYAHRLLMDLGFSRdvmsQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1956008863 186 DALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVILKpKPGRVEQIIPVNLPRPRNR 249
Cdd:PRK13646 177 DPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMK-EGSIVSQTSPKELFKDKKK 239
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
41-235 |
7.50e-26 |
|
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: 102.08 E-value: 7.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 41 KVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAG-LDQDFDGRILIDGADVSG---------IGgdraVVFQE--HRLF 108
Cdd:COG1119 17 TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVRLFGERRGGedvwelrkrIG----LVSPAlqLRFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 109 PWLTVEQNIELGL-----LNEALTSRDKDiLVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFG 183
Cdd:COG1119 93 RDETVLDVVLSGFfdsigLYREPTDEQRE-RARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1956008863 184 ALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVILkpKPGRV 235
Cdd:COG1119 172 GLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLL--KDGRV 221
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
41-228 |
9.66e-26 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 101.26 E-value: 9.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 41 KVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVS----------GIGgdraVVFQEHRLFPW 110
Cdd:COG1137 17 TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIThlpmhkrarlGIG----YLPQEASIFRK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 111 LTVEQNIELGLlnEaLTSRDKDILVQKAIELI---GLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDA 187
Cdd:COG1137 93 LTVEDNILAVL--E-LRKLSKKEREERLEELLeefGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1956008863 188 LTRHQMQNELLRIQSQQkmTTVFIT-HDVEEAVTLADRVVIL 228
Cdd:COG1137 170 IAVADIQKIIRHLKERG--IGVLITdHNVRETLGICDRAYII 209
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
37-229 |
1.22e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 102.09 E-value: 1.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 37 QQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGA-----DVSGIGGDRAVVFQE-HRLFPW 110
Cdd:PRK13642 17 ESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGElltaeNVWNLRRKIGMVFQNpDNQFVG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 111 LTVEQNIELGLLNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTR 190
Cdd:PRK13642 97 ATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGR 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 1956008863 191 HQMQNELLRIQSQQKMTTVFITHDVEEAVTlADRVVILK 229
Cdd:PRK13642 177 QEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMK 214
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
20-213 |
1.70e-25 |
|
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: 105.29 E-value: 1.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 20 TQTRVAFHHVHKSFvvnqQPVKVI-HDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLdqdFD---GRILIDGADVSGIG 95
Cdd:COG5265 354 GGGEVRFENVSFGY----DPERPIlKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRF---YDvtsGRILIDGQDIRDVT 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 96 GD--RA---VVFQEHRLFPwLTVEQNIELGLLNealTSRDKdilVQKAIELIGLNGFEKAYPHQ-----------LSGGM 159
Cdd:COG5265 427 QAslRAaigIVPQDTVLFN-DTIAYNIAYGRPD---ASEEE---VEAAARAAQIHDFIESLPDGydtrvgerglkLSGGE 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1956008863 160 SQRVAIARSLVVQPRIFLLDEPFGALDALTRHQMQNELLRIqSQQKmTTVFITH 213
Cdd:COG5265 500 KQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREV-ARGR-TTLVIAH 551
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
18-228 |
1.89e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 101.37 E-value: 1.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 18 ANTQTRVAFHHVhkSFVVNQQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRIL-----IDGADVS 92
Cdd:PRK13648 2 EDKNSIIVFKNV--SFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFynnqaITDDNFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 93 GIGGDRAVVFQE-HRLFPWLTVEQNIELGLLNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVV 171
Cdd:PRK13648 80 KLRKHIGIVFQNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1956008863 172 QPRIFLLDEPFGALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTlADRVVIL 228
Cdd:PRK13648 160 NPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVM 215
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
24-215 |
2.08e-25 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 100.33 E-value: 2.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 24 VAFHHVHKSFVVNQQPVKVIhDFNLeiKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDR----- 98
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGV-TFHM--RPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpflr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 99 ---AVVFQEHRLFPWLTVEQNIELGLLNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRI 175
Cdd:PRK10908 79 rqiGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1956008863 176 FLLDEPFGALD-ALTRHQMQneLLRIQSQQKMTTVFITHDV 215
Cdd:PRK10908 159 LLADEPTGNLDdALSEGILR--LFEEFNRVGVTVLMATHDI 197
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
43-229 |
4.59e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 100.69 E-value: 4.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 43 IHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADV----SGIGGDR---AVVFQ--EHRLFPwLTV 113
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysrKGLMKLResvGMVFQdpDNQLFS-ASV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 114 EQNIELGLLNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQM 193
Cdd:PRK13636 101 YQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEI 180
|
170 180 190
....*....|....*....|....*....|....*.
gi 1956008863 194 QNELLRIQSQQKMTTVFITHDVEEAVTLADRVVILK 229
Cdd:PRK13636 181 MKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMK 216
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
42-228 |
5.87e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 99.53 E-value: 5.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 42 VIHDFNLEIKEGEFIAIVGSSGCGKSTLLRL---LAGLDQD--FDGRILIDG-----ADVSGIGGDRAV--VFQEHRLFP 109
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrLLELNEEarVEGEVRLFGrniysPDVDPIEVRREVgmVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 110 WLTVEQNIELGL-LNEALTSRDK-DILVQKAIELIGL----NGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFG 183
Cdd:PRK14267 99 HLTIYDNVAIGVkLNGLVKSKKElDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1956008863 184 ALDALTRHQMQNELLRIQSQqkMTTVFITHDVEEAVTLADRVVIL 228
Cdd:PRK14267 179 NIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFL 221
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
43-228 |
8.06e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 99.68 E-value: 8.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 43 IHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRIL---IDGADVSGIGGDR---AVVFQE-HRLFPWLTVEQ 115
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLvsgIDTGDFSKLQGIRklvGIVFQNpETQFVGRTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 116 NIELGLLNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQMQN 195
Cdd:PRK13644 98 DLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLE 177
|
170 180 190
....*....|....*....|....*....|...
gi 1956008863 196 ELLRIQSQQKmTTVFITHDVEEaVTLADRVVIL 228
Cdd:PRK13644 178 RIKKLHEKGK-TIVYITHNLEE-LHDADRIIVM 208
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
14-238 |
1.14e-24 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 103.01 E-value: 1.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 14 QSFQANTQTRVAFHHVHKSFVVNQQPVKVIHDFNLEIKEGEFIAIVGSSGCGKS----TLLRLL--AGLDQDFDGRIL-- 85
Cdd:PRK10261 3 HSDELDARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGLVQCDKMLLrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 86 -----IDGADVSGI------GGDRAVVFQE--HRLFPWLTV-EQNIELGLLNEALTSRDKDILVQKAIELIGLNGFEKA- 150
Cdd:PRK10261 83 rsrqvIELSEQSAAqmrhvrGADMAMIFQEpmTSLNPVFTVgEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTIl 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 151 --YPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVIL 228
Cdd:PRK10261 163 srYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVM 242
|
250
....*....|....
gi 1956008863 229 KP----KPGRVEQI 238
Cdd:PRK10261 243 YQgeavETGSVEQI 256
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
18-228 |
1.17e-24 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 102.73 E-value: 1.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 18 ANTQTRVAFHHVHKSFVVNQQPVkviHDFNLEIKEGEFIAIVGSSGCGKSTLLRLlagLDQDFD---GRILIDGADVSGI 94
Cdd:PRK13657 329 GRVKGAVEFDDVSFSYDNSRQGV---EDVSFEAKPGQTVAIVGPTGAGKSTLINL---LQRVFDpqsGRILIDGTDIRTV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 95 G--GDR---AVVFQEHRLFPwLTVEQNIELG--------LLNEALTSRDKDILVQKAIEL---IGLNGfekaypHQLSGG 158
Cdd:PRK13657 403 TraSLRrniAVVFQDAGLFN-RSIEDNIRVGrpdatdeeMRAAAERAQAHDFIERKPDGYdtvVGERG------RQLSGG 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 159 MSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQMQNELLRIqsQQKMTTVFITHDVeEAVTLADRVVIL 228
Cdd:PRK13657 476 ERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDEL--MKGRTTFIIAHRL-STVRNADRILVF 542
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
41-237 |
1.38e-24 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 97.86 E-value: 1.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 41 KVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDR-----------AVVFQE----H 105
Cdd:PRK10247 21 KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyrqqvsycaqtPTLFGDtvydN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 106 RLFPWLTVEQNIELGLLNEALTSRD-KDILVQKAIEliglngfekayphQLSGGMSQRVAIARSLVVQPRIFLLDEPFGA 184
Cdd:PRK10247 101 LIFPWQIRNQQPDPAIFLDDLERFAlPDTILTKNIA-------------ELSGGEKQRISLIRNLQFMPKVLLLDEITSA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1956008863 185 LDALTRHQMQNELLRIQSQQKMTTVFITHDVEEaVTLADRVVILKPKPGRVEQ 237
Cdd:PRK10247 168 LDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE-INHADKVITLQPHAGEMQE 219
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
41-235 |
1.54e-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: 1.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 41 KVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGL--DQDFDGRILIDGADVSGIGGDRAV--VFQEHRLFPWLTVEQN 116
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLDKRSFRKIIgyVPQDDILHPTLTVRET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 117 IELgllnealtsrdkdilvqkAIELIGlngfekayphqLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQMQnE 196
Cdd:cd03213 103 LMF------------------AAKLRG-----------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVM-S 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1956008863 197 LLRIQSQQKMTTVFITHDV-EEAVTLADRVVILkpKPGRV 235
Cdd:cd03213 153 LLRRLADTGRTIICSIHQPsSEIFELFDKLLLL--SQGRV 190
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
24-229 |
1.56e-24 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 96.61 E-value: 1.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 24 VAFHHVHKSFVVNQQPVkvIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDR----A 99
Cdd:cd03247 1 LSINNVSFSYPEQEQQV--LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALssliS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 100 VVFQEHRLFPwLTVEQNIELgllnealtsrdkdilvqkaieliglngfekayphQLSGGMSQRVAIARSLVVQPRIFLLD 179
Cdd:cd03247 79 VLNQRPYLFD-TTLRNNLGR----------------------------------RFSGGERQRLALARILLQDAPIVLLD 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1956008863 180 EPFGALDALTrhqmQNELLRI--QSQQKMTTVFITHDVeEAVTLADRVVILK 229
Cdd:cd03247 124 EPTVGLDPIT----ERQLLSLifEVLKDKTLIWITHHL-TGIEHMDKILFLE 170
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
24-229 |
1.74e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 99.42 E-value: 1.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 24 VAFHHVHKSFVVNQQ-PVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDR---- 98
Cdd:PRK13643 2 IKFEKVNYTYQPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 99 -----AVVFQ--EHRLFPWlTVEQNIELGLLNEALTSRDKDILVQKAIELIGLNG-FEKAYPHQLSGGMSQRVAIARSLV 170
Cdd:PRK13643 82 vrkkvGVVFQfpESQLFEE-TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1956008863 171 VQPRIFLLDEPFGALDALTRHQMQnELLRIQSQQKMTTVFITHDVEEAVTLADRVVILK 229
Cdd:PRK13643 161 MEPEVLVLDEPTAGLDPKARIEMM-QLFESIHQSGQTVVLVTHLMDDVADYADYVYLLE 218
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
19-237 |
2.50e-24 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 102.11 E-value: 2.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 19 NTQTRVAFHHVHKSFVvNQQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIggDR 98
Cdd:TIGR00958 474 NLEGLIEFQDVSFSYP-NRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQY--DH 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 99 -------AVVFQEHRLFPWlTVEQNIELGLlnealtSRDKDILVQKAIELIGLNGFEKAYPH-----------QLSGGMS 160
Cdd:TIGR00958 551 hylhrqvALVGQEPVLFSG-SVRENIAYGL------TDTPDEEIMAAAKAANAHDFIMEFPNgydtevgekgsQLSGGQK 623
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1956008863 161 QRVAIARSLVVQPRIFLLDEPFGALDALTRHQMQNEllriQSQQKMTTVFITHDVeEAVTLADRVVILkpKPGRVEQ 237
Cdd:TIGR00958 624 QRIAIARALVRKPRVLILDEATSALDAECEQLLQES----RSRASRTVLLIAHRL-STVERADQILVL--KKGSVVE 693
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
45-228 |
2.53e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 98.66 E-value: 2.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 45 DFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGA---------DVSGIGGDRAVVFQ--EHRLFPWlTV 113
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTlitstsknkDIKQIRKKVGLVFQfpESQLFEE-TV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 114 EQNIELGLLNEALTSRDKDILVQKAIELIGL--NGFEKAyPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRH 191
Cdd:PRK13649 104 LKDVAFGPQNFGVSQEEAEALAREKLALVGIseSLFEKN-PFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRK 182
|
170 180 190
....*....|....*....|....*....|....*..
gi 1956008863 192 QMQnELLRIQSQQKMTTVFITHDVEEAVTLADRVVIL 228
Cdd:PRK13649 183 ELM-TLFKKLHQSGMTIVLVTHLMDDVANYADFVYVL 218
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
42-229 |
2.63e-24 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 101.71 E-value: 2.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 42 VIHDFNLEIKEGEFIAIVGSSGCGKST----LLRLLAGldqdfDGRILIDGADVSGIGGDR--------AVVFQE--HRL 107
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQPLHNLNRRQllpvrhriQVVFQDpnSSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 108 FPWLTVEQNIELGLL--NEALTSRDKDILVQKAIELIGLNGFEKA-YPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGA 184
Cdd:PRK15134 376 NPRLNVLQIIEEGLRvhQPTLSAAQREQQVIAVMEEVGLDPETRHrYPAEFSGGQRQRIAIARALILKPSLIILDEPTSS 455
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1956008863 185 LDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVILK 229
Cdd:PRK15134 456 LDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLR 500
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
48-235 |
3.38e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 98.27 E-value: 3.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 48 LEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSG-----IGGDRAVVFQE--HRLFPwLTVEQNIELG 120
Cdd:PRK13647 26 LSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAenekwVRSKVGLVFQDpdDQVFS-STVWDDVAFG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 121 LLNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQMQnELLRI 200
Cdd:PRK13647 105 PVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLM-EILDR 183
|
170 180 190
....*....|....*....|....*....|....*
gi 1956008863 201 QSQQKMTTVFITHDVEEAVTLADRVVILkpKPGRV 235
Cdd:PRK13647 184 LHNQGKTVIVATHDVDLAAEWADQVIVL--KEGRV 216
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
41-224 |
4.37e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 97.54 E-value: 4.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 41 KVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQ-----DFDGRILIDGADVSGIGGDR-------AVVFQEHRLF 108
Cdd:PRK14239 19 KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIYSPRTDTvdlrkeiGMVFQQPNPF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 109 PwLTVEQNIELGLLNEALtsRDKDILvQKAIE--LIGLNGFE--KAYPHQ----LSGGMSQRVAIARSLVVQPRIFLLDE 180
Cdd:PRK14239 99 P-MSIYENVVYGLRLKGI--KDKQVL-DEAVEksLKGASIWDevKDRLHDsalgLSGGQQQRVCIARVLATSPKIILLDE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1956008863 181 PFGALDALTRHQMQNELLRIQSQQKMTTVfiTHDVEEAVTLADR 224
Cdd:PRK14239 175 PTSALDPISAGKIEETLLGLKDDYTMLLV--TRSMQQASRISDR 216
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
32-237 |
4.51e-24 |
|
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: 100.98 E-value: 4.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 32 SFVVNQQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDRavvFQEH------ 105
Cdd:COG4618 337 TVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREE---LGRHigylpq 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 106 --RLFPWlTVEQNIelgllnealtSRDKDILVQKAI---------ELIGlnGFEKAY-------PHQLSGGMSQRVAIAR 167
Cdd:COG4618 414 dvELFDG-TIAENI----------ARFGDADPEKVVaaaklagvhEMIL--RLPDGYdtrigegGARLSGGQRQRIGLAR 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1956008863 168 SLVVQPRIFLLDEPFGALD-----ALTRhqmqneLLRIQSQQKMTTVFITHDVeEAVTLADRVVILkpKPGRVEQ 237
Cdd:COG4618 481 ALYGDPRLVVLDEPNSNLDdegeaALAA------AIRALKARGATVVVITHRP-SLLAAVDKLLVL--RDGRVQA 546
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
21-230 |
5.51e-24 |
|
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: 96.35 E-value: 5.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 21 QTRVAFHHVHKSFVVNQQ---PVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGA----DVSG 93
Cdd:COG4778 2 TTLLEVENLSKTFTLHLQggkRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 94 IGgDRAV----------VFQEHRLFPWLTVeqnieLGLLNEALTSR--DKDILVQKAIELIG-LNGFEK---AYPHQLSG 157
Cdd:COG4778 82 AS-PREIlalrrrtigyVSQFLRVIPRVSA-----LDVVAEPLLERgvDREEARARARELLArLNLPERlwdLPPATFSG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1956008863 158 GMSQRVAIARSLVVQPRIFLLDEPFGALDALTRhQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVILKP 230
Cdd:COG4778 156 GEQQRVNIARGFIADPPLLLLDEPTASLDAANR-AVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTP 227
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
24-229 |
1.33e-23 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 95.92 E-value: 1.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 24 VAFHHVHKSFVVNQQP------------------VKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRIL 85
Cdd:COG1134 5 IEVENVSKSYRLYHEPsrslkelllrrrrtrreeFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 86 IDGaDVS---GIGGdravVFQehrlfPWLTVEQNIELG--LLNeaLTSRDKDILVQKAIELIGLNGFE----KAYphqlS 156
Cdd:COG1134 85 VNG-RVSallELGA----GFH-----PELTGRENIYLNgrLLG--LSRKEIDEKFDEIVEFAELGDFIdqpvKTY----S 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1956008863 157 GGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQMQNELLRIQSQQKmTTVFITHDVEEAVTLADRVVILK 229
Cdd:COG1134 149 SGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGR-TVIFVSHSMGAVRRLCDRAIWLE 220
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
45-229 |
1.70e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 96.44 E-value: 1.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 45 DFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDRAV---------VFQ--EHRLFPwLTV 113
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLkklrkkvslVFQfpEAQLFE-NTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 114 EQNIELGLLNEALTSRDKDILVQKAIELIGLNG--FEKAyPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRH 191
Cdd:PRK13641 104 LKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEdlISKS-PFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRK 182
|
170 180 190
....*....|....*....|....*....|....*...
gi 1956008863 192 QMQNELLRIQsQQKMTTVFITHDVEEAVTLADRVVILK 229
Cdd:PRK13641 183 EMMQLFKDYQ-KAGHTVILVTHNMDDVAEYADDVLVLE 219
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
21-229 |
2.10e-23 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 95.85 E-value: 2.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 21 QTRVAFHHVHKSFVVNQqpvkVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGL---DQDFDGRILIDGADVSGIG-- 95
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQ----ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGrl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 96 -----GDRA---VVFQEHRLFPWLTVEQNIELGLLNEA---------LTSRDKDILVQkAIELIGLNGFEKAYPHQLSGG 158
Cdd:PRK09984 78 ardirKSRAntgYIFQQFNLVNRLSVLENVLIGALGSTpfwrtcfswFTREQKQRALQ-ALTRVGMVHFAHQRVSTLSGG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1956008863 159 MSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVILK 229
Cdd:PRK09984 157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALR 227
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
21-228 |
2.59e-23 |
|
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: 94.85 E-value: 2.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 21 QTRVAFHHVhkSFVVNQQP-VKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSG-----I 94
Cdd:cd03248 9 KGIVKFQNV--TFAYPTRPdTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQyehkyL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 95 GGDRAVVFQEHRLFPwLTVEQNIELGLLNEALTSRDKdiLVQKAIELIGLNGFEKAYP-------HQLSGGMSQRVAIAR 167
Cdd:cd03248 87 HSKVSLVGQEPVLFA-RSLQDNIAYGLQSCSFECVKE--AAQKAHAHSFISELASGYDtevgekgSQLSGGQKQRVAIAR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1956008863 168 SLVVQPRIFLLDEPFGALDALTRHQMQNELLriQSQQKMTTVFITHDVeEAVTLADRVVIL 228
Cdd:cd03248 164 ALIRNPQVLILDEATSALDAESEQQVQQALY--DWPERRTVLVIAHRL-STVERADQILVL 221
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
31-228 |
2.84e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 97.60 E-value: 2.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 31 KSFVVNQQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSG-----IGGDRAVVFQEH 105
Cdd:PRK09536 7 SDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEAlsaraASRRVASVPQDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 106 RLFPWLTVEQNIELGllNEALTSR------DKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLD 179
Cdd:PRK09536 87 SLSFEFDVRQVVEMG--RTPHRSRfdtwteTDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1956008863 180 EPFGALDalTRHQMQN-ELLRIQSQQKMTTVFITHDVEEAVTLADRVVIL 228
Cdd:PRK09536 165 EPTASLD--INHQVRTlELVRRLVDDGKTAVAAIHDLDLAARYCDELVLL 212
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
41-229 |
3.13e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 98.17 E-value: 3.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 41 KVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVS----------GIG---GDRavvfQEHRL 107
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRirsprdairaGIAyvpEDR----KGEGL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 108 FPWLTVEQNIELGLLNEA-----LTSRDKDILVQKAIELIGLngfeKA-YPHQ----LSGGMSQRVAIARSLVVQPRIFL 177
Cdd:COG1129 342 VLDLSIRENITLASLDRLsrgglLDRRRERALAEEYIKRLRI----KTpSPEQpvgnLSGGNQQKVVLAKWLATDPKVLI 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1956008863 178 LDEPfgaldalTR----------HQMQNELlriqSQQKMTTVFITHDVEEAVTLADRVVILK 229
Cdd:COG1129 418 LDEP-------TRgidvgakaeiYRLIREL----AAEGKAVIVISSELPELLGLSDRILVMR 468
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
37-228 |
3.37e-23 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 95.24 E-value: 3.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 37 QQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGigGDRA-------VVFQE--HRL 107
Cdd:PRK15112 23 RQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHF--GDYSyrsqrirMIFQDpsTSL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 108 FPWLTVEQNIELGL-LNEALTSRDKDILVQKAIELIGL-NGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGAL 185
Cdd:PRK15112 101 NPRQRISQILDFPLrLNTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1956008863 186 DALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVIL 228
Cdd:PRK15112 181 DMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVM 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
26-226 |
7.57e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.06 E-value: 7.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 26 FHHVHKSFvvnqqPVKVI-HDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILID-GADVsgiggdrAVVFQ 103
Cdd:COG0488 1 LENLSKSF-----GGRPLlDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPkGLRI-------GYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 104 EHRLFPWLTVEQNIELGL------------LNEALTSRDKDILVQKAIE------------------LIGLnGFEKAYPH 153
Cdd:COG0488 69 EPPLDDDLTVLDTVLDGDaelraleaeleeLEAKLAEPDEDLERLAELQeefealggweaearaeeiLSGL-GFPEEDLD 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1956008863 154 Q----LSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQMQNELLRIQSqqkmTTVFITHDVEeavtLADRVV 226
Cdd:COG0488 148 RpvseLSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPG----TVLVVSHDRY----FLDRVA 216
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
41-229 |
7.61e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 93.93 E-value: 7.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 41 KVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGD---RAVVF--QEHRLFPWLTVEQ 115
Cdd:PRK11231 16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRqlaRRLALlpQHHLTPEGITVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 116 NIELGL-----LNEALTSRDKDiLVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDalTR 190
Cdd:PRK11231 96 LVAYGRspwlsLWGRLSAEDNA-RVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLD--IN 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1956008863 191 HQMQ-NELLRIQSQQKMTTVFITHDVEEAVTLADRVVILK 229
Cdd:PRK11231 173 HQVElMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLA 212
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-237 |
9.46e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 97.08 E-value: 9.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 19 NTQTRVAFHHVHKSFVVNQQPVKVIHDFNLEIKEGEFIAIVGSSGCGKS----TLLRLLA-------GLDQDFDGRILI- 86
Cdd:PRK15134 1 MTQPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPsppvvypSGDIRFHGESLLh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 87 -DGADVSGIGGDR-AVVFQEH--RLFPWLTVE-QNIELGLLN----------EALTSRDKDILVQKAIELiglngfeKAY 151
Cdd:PRK15134 81 aSEQTLRGVRGNKiAMIFQEPmvSLNPLHTLEkQLYEVLSLHrgmrreaargEILNCLDRVGIRQAAKRL-------TDY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 152 PHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVILkpK 231
Cdd:PRK15134 154 PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVM--Q 231
|
....*..
gi 1956008863 232 PGR-VEQ 237
Cdd:PRK15134 232 NGRcVEQ 238
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
32-239 |
1.24e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 93.56 E-value: 1.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 32 SFVVNQQpvKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQdFDGRILIDG-------------ADVSGIGGDR 98
Cdd:PRK14258 14 SFYYDTQ--KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGrveffnqniyerrVNLNRLRRQV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 99 AVVFQEHRLFPwLTVEQNIELGLlnEALTSRDK---DILVQKAIELIGLNGFEKAYPHQ----LSGGMSQRVAIARSLVV 171
Cdd:PRK14258 91 SMVHPKPNLFP-MSVYDNVAYGV--KIVGWRPKleiDDIVESALKDADLWDEIKHKIHKsaldLSGGQQQRLCIARALAV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1956008863 172 QPRIFLLDEPFGALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVILKPKPGRVEQII 239
Cdd:PRK14258 168 KPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNENRIGQLV 235
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
37-239 |
1.45e-22 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 94.59 E-value: 1.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 37 QQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQD----------FDGrilIDGADVSG------IGGDRAV 100
Cdd:COG4170 17 QGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvtadrfrWNG---IDLLKLSPrerrkiIGREIAM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 101 VFQEHR--LFPWLTVEQNIELGLLNEALTSRDKDILVQK---AIEL---IGLNGFE---KAYPHQLSGGMSQRVAIARSL 169
Cdd:COG4170 94 IFQEPSscLDPSAKIGDQLIEAIPSWTFKGKWWQRFKWRkkrAIELlhrVGIKDHKdimNSYPHELTEGECQKVMIAMAI 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1956008863 170 VVQPRIFLLDEPFGALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVIL----KPKPGRVEQII 239
Cdd:COG4170 174 ANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLycgqTVESGPTEQIL 247
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
41-237 |
3.02e-22 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 92.72 E-value: 3.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 41 KVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGI---GGDRAV---------------VF 102
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkDGQLKVadknqlrllrtrltmVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 103 QEHRLFPWLTVEQNI-ELGLLNEALTSRDKDILVQKAIELIGLNGFEKA-YPHQLSGGMSQRVAIARSLVVQPRIFLLDE 180
Cdd:PRK10619 99 QHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGkYPVHLSGGQQQRVSIARALAMEPEVLLFDE 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 181 PFGALDAltrhQMQNELLRIQSQ---QKMTTVFITHDVEEAVTLADRVVILkpKPGRVEQ 237
Cdd:PRK10619 179 PTSALDP----ELVGEVLRIMQQlaeEGKTMVVVTHEMGFARHVSSHVIFL--HQGKIEE 232
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
40-228 |
3.43e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 92.94 E-value: 3.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 40 VKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDG-----ADVSGIGGDRAVVFQ--EHRLFPwLT 112
Cdd:PRK13652 17 KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGepitkENIREVRKFVGLVFQnpDDQIFS-PT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 113 VEQNIELGLLNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQ 192
Cdd:PRK13652 96 VEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKE 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 1956008863 193 MQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVIL 228
Cdd:PRK13652 176 LIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVM 211
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
44-191 |
5.45e-22 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 90.63 E-value: 5.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 44 HDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGD--RAVVFQEHR--LFPWLTVEQNIel 119
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEyhQDLLYLGHQpgIKTELTALENL-- 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1956008863 120 gLLNEALTSR-DKDILVQkAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDA-----LTRH 191
Cdd:PRK13538 96 -RFYQRLHGPgDDEALWE-ALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKqgvarLEAL 171
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
40-229 |
5.49e-22 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 91.48 E-value: 5.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 40 VKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDR------AVVFQEHRLFPWLTV 113
Cdd:PRK11614 18 IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKimreavAIVPEGRRVFSRMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 114 EQNIELGLLnealtSRDKDILVQKAIELIGLngFEKAYPHQ------LSGGMSQRVAIARSLVVQPRIFLLDEPFGALDA 187
Cdd:PRK11614 98 EENLAMGGF-----FAERDQFQERIKWVYEL--FPRLHERRiqragtMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1956008863 188 LTRHQMQNELLRIQsQQKMTTVFITHDVEEAVTLADRVVILK 229
Cdd:PRK11614 171 IIIQQIFDTIEQLR-EQGMTIFLVEQNANQALKLADRGYVLE 211
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
40-192 |
5.54e-22 |
|
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: 91.18 E-value: 5.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 40 VKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQD---FDGRILIDGADVS-GIGGDR-AVVFQEHRLFPWLTVE 114
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKpDQFQKCvAYVRQDDILLPGLTVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 115 QNI----ELGLLNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTR 190
Cdd:cd03234 100 ETLtytaILRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTA 179
|
..
gi 1956008863 191 HQ 192
Cdd:cd03234 180 LN 181
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
53-213 |
5.93e-22 |
|
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: 90.24 E-value: 5.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 53 GEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGD--RAVVFQEHR--LFPWLTVEQNIELGllnEALTS 128
Cdd:cd03231 26 GEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiaRGLLYLGHApgIKTTLSVLENLRFW---HADHS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 129 RDKdilVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQMQnELLRIQSQQKMTT 208
Cdd:cd03231 103 DEQ---VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFA-EAMAGHCARGGMV 178
|
....*
gi 1956008863 209 VFITH 213
Cdd:cd03231 179 VLTTH 183
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
41-229 |
7.67e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 92.46 E-value: 7.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 41 KVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGAD-----------------------------V 91
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDeknkkktkekekvleklviqktrfkkikkI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 92 SGIGGDRAVVFQ--EHRLFPwLTVEQNIELGLLNEALTSRDKDILVQKAIELIGLN-GFEKAYPHQLSGGMSQRVAIARS 168
Cdd:PRK13651 101 KEIRRRVGVVFQfaEYQLFE-QTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDeSYLQRSPFELSGGQKRRVALAGI 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1956008863 169 LVVQPRIFLLDEPFGALDALTRHQMQNELLRIQSQQKmTTVFITHDVEEAVTLADRVVILK 229
Cdd:PRK13651 180 LAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNVLEWTKRTIFFK 239
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
40-260 |
8.54e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 91.13 E-value: 8.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 40 VKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGL-----DQDFDGRILIDGAD-----VSGIGGDRAVVFQEHRLFP 109
Cdd:PRK14247 16 VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDifkmdVIELRRRVQMVFQIPNPIP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 110 WLTVEQNIELGL-LNEALTSRDK-DILVQKAIELIGLNGFEK----AYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFG 183
Cdd:PRK14247 96 NLSIFENVALGLkLNRLVKSKKElQERVRWALEKAQLWDEVKdrldAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1956008863 184 ALDALTRHQMqnELLRIQSQQKMTTVFITHDVEEAVTLADRVVILkpKPGRVEQIIPVN--LPRPRnrssfelHQLKEQ 260
Cdd:PRK14247 176 NLDPENTAKI--ESLFLELKKDMTIVLVTHFPQQAARISDYVAFL--YKGQIVEWGPTRevFTNPR-------HELTEK 243
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
27-228 |
1.07e-21 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 91.43 E-value: 1.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 27 HHVHksfvVNQQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGldqDFDGRILIDGADVSG---IGGD------ 97
Cdd:PRK13547 5 DHLH----VARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG---DLTGGGAPRGARVTGdvtLNGEplaaid 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 98 -------RAVVFQE-HRLFPWlTVEQNIELGLLNEA-----LTSRDKDILVQkAIELIGLNGFEKAYPHQLSGGMSQRVA 164
Cdd:PRK13547 78 aprlarlRAVLPQAaQPAFAF-SAREIVLLGRYPHArragaLTHRDGEIAWQ-ALALAGATALVGRDVTTLSGGELARVQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1956008863 165 IARSL---------VVQPRIFLLDEPFGALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVIL 228
Cdd:PRK13547 156 FARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAML 228
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
42-228 |
1.25e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 90.88 E-value: 1.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 42 VIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGA-----------DVSGIGGDRAVVFQEHRLFPW 110
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkdifqiDAIKLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 111 LTVEQNIELGLLNEALTS-RDKDILVQKAIELIGLngFEKAY------PHQLSGGMSQRVAIARSLVVQPRIFLLDEPFG 183
Cdd:PRK14246 105 LSIYDNIAYPLKSHGIKEkREIKKIVEECLRKVGL--WKEVYdrlnspASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1956008863 184 ALDALTRHQMqnELLRIQSQQKMTTVFITHDVEEAVTLADRVVIL 228
Cdd:PRK14246 183 MIDIVNSQAI--EKLITELKNEIAIVIVSHNPQQVARVADYVAFL 225
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
42-245 |
2.61e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 92.95 E-value: 2.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 42 VIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILI-DGADVsgiggdravvfqehrLF----PWLTveqn 116
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARV---------------LFlpqrPYLP---- 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 117 ieLGLLNEALT-----SRDKDILVQKAIELIGLNGF------EKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGAL 185
Cdd:COG4178 439 --LGTLREALLypataEAFSDAELREALEAVGLGHLaerldeEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSAL 516
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 186 DALTRHQMQnELLRiQSQQKMTTVFITHDvEEAVTLADRVVILKPKPGRveQIIPVNLPR 245
Cdd:COG4178 517 DEENEAALY-QLLR-EELPGTTVISVGHR-STLAAFHDRVLELTGDGSW--QLLPAEAPA 571
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
39-228 |
3.13e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 91.07 E-value: 3.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 39 PVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILID----GADVSGIGGDR---------------- 98
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKKNNHELITnpyskkiknfkelrrr 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 99 -AVVFQ--EHRLFPwLTVEQNIELGLLNEALTSRDKDILVQKAIELIGLN-GFEKAYPHQLSGGMSQRVAIARSLVVQPR 174
Cdd:PRK13631 118 vSMVFQfpEYQLFK-DTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDdSYLERSPFGLSGGQKRRVAIAGILAIQPE 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1956008863 175 IFLLDEPFGALDALTRHQMQNELLRIQSQQKmtTVF-ITHDVEEAVTLADRVVIL 228
Cdd:PRK13631 197 ILIFDEPTAGLDPKGEHEMMQLILDAKANNK--TVFvITHTMEHVLEVADEVIVM 249
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
41-228 |
3.16e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 90.45 E-value: 3.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 41 KVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILI-DGADVSGIGGDRAV---------VFQ--EHRLF 108
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgDYAIPANLKKIKEVkrlrkeiglVFQfpEYQLF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 109 PwLTVEQNIELGLLNealTSRDKDILVQKAIELIGLNGFEKAY----PHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGA 184
Cdd:PRK13645 105 Q-ETIEKDIAFGPVN---LGENKQEAYKKVPELLKLVQLPEDYvkrsPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1956008863 185 LDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVIL 228
Cdd:PRK13645 181 LDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVM 224
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
23-228 |
4.96e-21 |
|
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: 92.09 E-value: 4.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 23 RVAFHHVhkSFVVNQQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDR---- 98
Cdd:TIGR02203 330 DVEFRNV--TFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASlrrq 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 99 -AVVFQEHRLFPwLTVEQNIELGLLNEALTSRDKDILVQK-AIEL-----------IGLNGfekaypHQLSGGMSQRVAI 165
Cdd:TIGR02203 408 vALVSQDVVLFN-DTIANNIAYGRTEQADRAEIERALAAAyAQDFvdklplgldtpIGENG------VLLSGGQRQRLAI 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1956008863 166 ARSLVVQPRIFLLDEPFGALDALTRHQMQNELLRIqsQQKMTTVFITHDVeEAVTLADRVVIL 228
Cdd:TIGR02203 481 ARALLKDAPILILDEATSALDNESERLVQAALERL--MQGRTTLVIAHRL-STIEKADRIVVM 540
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
47-217 |
7.83e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 91.44 E-value: 7.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 47 NLEIKEGEFIAIVGSSGCGKSTLLRLLAGLdQDFDGRILIDGADVSGIGGDR-----AVVFQEHRLFPWlTVEQNIELGl 121
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELDPESwrkhlSWVGQNPQLPHG-TLRDNVLLG- 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 122 lNEALTsrdkDILVQKAIELIGLNGFEKAYPH-----------QLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTR 190
Cdd:PRK11174 447 -NPDAS----DEQLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSE 521
|
170 180
....*....|....*....|....*..
gi 1956008863 191 HQMQNELLRIQSQQkmTTVFITHDVEE 217
Cdd:PRK11174 522 QLVMQALNAASRRQ--TTLMVTHQLED 546
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
42-229 |
8.42e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 89.89 E-value: 8.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 42 VIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADV--------SGIGgdraVVFQEHRLFPWLTV 113
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVpararlarARIG----VVPQFDNLDLEFTV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 114 EQNIELGLLNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQM 193
Cdd:PRK13536 132 RENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLI 211
|
170 180 190
....*....|....*....|....*....|....*.
gi 1956008863 194 QnELLRIQSQQKMTTVFITHDVEEAVTLADRVVILK 229
Cdd:PRK13536 212 W-ERLRSLLARGKTILLTTHFMEEAERLCDRLCVLE 246
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
40-229 |
9.13e-21 |
|
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: 87.77 E-value: 9.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 40 VKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRIL-------IDGADVSGIGGDRAVVFQEHRlfPWL- 111
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnknesEPSFEATRSRNRYSVAYAAQK--PWLl 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 112 --TVEQNIELG---------LLNEALTSR-DKDILVQKAIELIGLNGFekayphQLSGGMSQRVAIARSLVVQPRIFLLD 179
Cdd:cd03290 92 naTVEENITFGspfnkqrykAVTDACSLQpDIDLLPFGDQTEIGERGI------NLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1956008863 180 EPFGALDA-LTRHQMQNELLRIQSQQKMTTVFITHDVeEAVTLADRVVILK 229
Cdd:cd03290 166 DPFSALDIhLSDHLMQEGILKFLQDDKRTLVLVTHKL-QYLPHADWIIAMK 215
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
38-235 |
9.20e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 88.91 E-value: 9.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 38 QPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGA--DVSGIG-----GDRAVVFQ--EHRLF 108
Cdd:PRK13638 12 QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGllalrQQVATVFQdpEQQIF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 109 pWLTVEQNIELGLLNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDAL 188
Cdd:PRK13638 92 -YTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1956008863 189 TRHQMQNELLRIqSQQKMTTVFITHDVEEAVTLADRVVILKP-------KPGRV 235
Cdd:PRK13638 171 GRTQMIAIIRRI-VAQGNHVIISSHDIDLIYEISDAVYVLRQgqilthgAPGEV 223
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
27-229 |
1.19e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 89.01 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 27 HHVHKSFvvnqQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAG-LDQDfDGRILIDGADVsgiggDRAVVFQ-- 103
Cdd:COG4152 5 KGLTKRF----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGiLAPD-SGEVLWDGEPL-----DPEDRRRig 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 104 ----EHRLFPWLTV-EQNIELGllneALTSRDKDILVQKAIELI---GLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRI 175
Cdd:COG4152 75 ylpeERGLYPKMKVgEQLVYLA----RLKGLSKAEAKRRADEWLerlGLGDRANKKVEELSKGNQQKVQLIAALLHDPEL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1956008863 176 FLLDEPFGALDALTRHQMQNELLRIQSQQKmTTVFITHDVEEAVTLADRVVILK 229
Cdd:COG4152 151 LILDEPFSGLDPVNVELLKDVIRELAAKGT-TVIFSSHQMELVEELCDRIVIIN 203
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
32-213 |
1.34e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 91.04 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 32 SFVVNQQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAgldQDFD---GRILIDGADVSGIGGD--RA---VVFQ 103
Cdd:PRK11160 345 SFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLT---RAWDpqqGEILLNGQPIADYSEAalRQaisVVSQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 104 EHRLFPwLTVEQNIELGlLNEALTSRDKDILVQKAIE-LI----GLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLL 178
Cdd:PRK11160 422 RVHLFS-ATLRDNLLLA-APNASDEALIEVLQQVGLEkLLeddkGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLL 499
|
170 180 190
....*....|....*....|....*....|....*
gi 1956008863 179 DEPFGALDALTRHQMQnELLRIQSQQKmTTVFITH 213
Cdd:PRK11160 500 DEPTEGLDAETERQIL-ELLAEHAQNK-TVLMITH 532
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
10-228 |
2.41e-20 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 90.18 E-value: 2.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 10 EKHHQSFQANTQTRVAFHHVHKSFVVNQqpvKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGA 89
Cdd:TIGR01193 460 NKKKRTELNNLNGDIVINDVSYSYGYGS---NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGF 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 90 DVSGIggDRAV-------VFQEHRLFPWlTVEQNIELGllNEALTSRDKdilVQKAIELIGLNGFEKAYPH--------- 153
Cdd:TIGR01193 537 SLKDI--DRHTlrqfinyLPQEPYIFSG-SILENLLLG--AKENVSQDE---IWAACEIAEIKDDIENMPLgyqtelsee 608
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1956008863 154 --QLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQMQNELLRIQSQqkmTTVFITHDVEEAvTLADRVVIL 228
Cdd:TIGR01193 609 gsSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVA-KQSDKIIVL 681
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
42-187 |
2.48e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 86.08 E-value: 2.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 42 VIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDRAVVFQEHR--LFPWLTVEQNIEL 119
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGHRnaMKPALTVAENLEF 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 120 --GLLNEALTSrdkdilVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDA 187
Cdd:PRK13539 97 waAFLGGEELD------IAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
39-235 |
4.31e-20 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 86.52 E-value: 4.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 39 PVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADvsgiGGDRAVVF---QEHRLF---PWLT 112
Cdd:PRK11701 18 PRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRD----GQLRDLYAlseAERRRLlrtEWGF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 113 VEQNIELGL---------LNE---ALTSRDKDILVQKAIEL-----IGLNGFEKAyPHQLSGGMSQRVAIARSLVVQPRI 175
Cdd:PRK11701 94 VHQHPRDGLrmqvsaggnIGErlmAVGARHYGDIRATAGDWlerveIDAARIDDL-PTTFSGGMQQRLQIARNLVTHPRL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1956008863 176 FLLDEPFGALDAltrhQMQNELL----RIQSQQKMTTVFITHDVEEAVTLADRVVILkpKPGRV 235
Cdd:PRK11701 173 VFMDEPTGGLDV----SVQARLLdllrGLVRELGLAVVIVTHDLAVARLLAHRLLVM--KQGRV 230
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
24-228 |
4.32e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 87.55 E-value: 4.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 24 VAFHHVHKSFvvnqQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGiggdRA---- 99
Cdd:PRK13537 8 IDFRNVEKRY----GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS----RArhar 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 100 ----VVFQEHRLFPWLTVEQNIELGLLNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRI 175
Cdd:PRK13537 80 qrvgVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1956008863 176 FLLDEPFGALDALTRHQMQNELLRIQSQQKmTTVFITHDVEEAVTLADRVVIL 228
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVI 211
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
37-237 |
7.29e-20 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 85.91 E-value: 7.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 37 QQPVKVIHDFNLEIKEGEFIAIVGSSGCGKS----TLLRLL-AGLDQdFDGRILIDGADVSGI---GGDRAVVFQEHR-- 106
Cdd:PRK10418 13 QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILpAGVRQ-TAGRVLLDGKPVAPCalrGRKIATIMQNPRsa 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 107 LFPWLTVEQNIELGLLNEALTSRDKDILvqKAIELIGLNGFE---KAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFG 183
Cdd:PRK10418 92 FNPLHTMHTHARETCLALGKPADDATLT--AALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1956008863 184 ALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVILkpKPGR-VEQ 237
Cdd:PRK10418 170 DLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVM--SHGRiVEQ 222
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
42-231 |
8.80e-20 |
|
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: 83.74 E-value: 8.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 42 VIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRIlidgadvsGIGGDRAVVFQEHRlfPWLTveqnieLGL 121
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI--------GMPEGEDLLFLPQR--PYLP------LGT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 122 LNEALtsrdkdilvqkaieliglngfekAYP--HQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDaltrHQMQNELLR 199
Cdd:cd03223 80 LREQL-----------------------IYPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALD----EESEDRLYQ 132
|
170 180 190
....*....|....*....|....*....|..
gi 1956008863 200 IQSQQKMTTVFITHDvEEAVTLADRVVILKPK 231
Cdd:cd03223 133 LLKELGITVISVGHR-PSLWKFHDRVLDLDGE 163
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
40-233 |
1.48e-19 |
|
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: 85.15 E-value: 1.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 40 VKVIHDFNLEIKEGEF-----IAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSgiggdravvFQEHRLFP--WLT 112
Cdd:cd03237 7 KKTLGEFTLEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS---------YKPQYIKAdyEGT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 113 VEQnielgLLNEALtsRDKDILVQKAIELIGLNGFEKAYPHQ---LSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALT 189
Cdd:cd03237 78 VRD-----LLSSIT--KDFYTHPYFKTEIAKPLQIEQILDREvpeLSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQ 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1956008863 190 RHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVILKPKPG 233
Cdd:cd03237 151 RLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFEGEPS 194
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
40-229 |
2.85e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 86.91 E-value: 2.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 40 VKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGL--DQDFDGRILIDGADV----------SGIggdrAVVFQEHRL 107
Cdd:PRK13549 18 VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEELqasnirdterAGI----AIIHQELAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 108 FPWLTVEQNIELGllNEALTSR--DKDILVQKAIEL-----IGLNGFEKAYphQLSGGMSQRVAIARSLVVQPRIFLLDE 180
Cdd:PRK13549 94 VKELSVLENIFLG--NEITPGGimDYDAMYLRAQKLlaqlkLDINPATPVG--NLGLGQQQLVEIAKALNKQARLLILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1956008863 181 PFGAL-DALTRHQMqnELLRIQSQQKMTTVFITHDVEEAVTLADRVVILK 229
Cdd:PRK13549 170 PTASLtESETAVLL--DIIRDLKAHGIACIYISHKLNEVKAISDTICVIR 217
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
43-223 |
4.99e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 84.06 E-value: 4.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 43 IHDFNLEIKEGEFIAIVGSSGCGKSTLLRL---LAGLDQDF--DGRILIDGADVSGIGGDRA-------VVFQEHRLFPw 110
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPGFrvEGKVTFHGKNLYAPDVDPVevrrrigMVFQKPNPFP- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 111 LTVEQNIELGLLNEALTSrDKDILVQKAIELIGLNGFEKAYPHQ----LSGGMSQRVAIARSLVVQPRIFLLDEPFGALD 186
Cdd:PRK14243 105 KSIYDNIAYGARINGYKG-DMDELVERSLRQAALWDEVKDKLKQsglsLSGGQQQRLCIARAIAVQPEVILMDEPCSALD 183
|
170 180 190
....*....|....*....|....*....|....*..
gi 1956008863 187 ALTRHQMQnELLRiQSQQKMTTVFITHDVEEAVTLAD 223
Cdd:PRK14243 184 PISTLRIE-ELMH-ELKEQYTIIIVTHNMQQAARVSD 218
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
40-264 |
8.84e-19 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 85.26 E-value: 8.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 40 VKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGL--DQDFDGRILIDGADV--SGIGGDR----AVVFQEHRLFPWL 111
Cdd:TIGR02633 14 VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLkaSNIRDTEragiVIIHQELTLVPEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 112 TVEQNIELG---LLNEALTSRDKDIL-VQKAIELIGLNGFEKAYP-HQLSGGMSQRVAIARSLVVQPRIFLLDEPFGald 186
Cdd:TIGR02633 94 SVAENIFLGneiTLPGGRMAYNAMYLrAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQARLLILDEPSS--- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 187 ALTRHQMQN--ELLRIQSQQKMTTVFITHDVEEAVTLADRVVILK------PKPGR---VEQIIPVNLPRP-RNRSSFEL 254
Cdd:TIGR02633 171 SLTEKETEIllDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRdgqhvaTKDMStmsEDDIITMMVGREiTSLYPHEP 250
|
250
....*....|
gi 1956008863 255 HQLKEQIFRI 264
Cdd:TIGR02633 251 HEIGDVILEA 260
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
40-228 |
9.41e-19 |
|
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: 85.24 E-value: 9.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 40 VKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQ--DFDGRILI----------------DGADVSGIGGDR--- 98
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIYhvalcekcgyverpskVGEPCPVCGGTLepe 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 99 -------------------AVVFQE-HRLFPWLTVEQNIeLGLLNEALTSRDKDilVQKAIELIGLNGFEKAYPH---QL 155
Cdd:TIGR03269 93 evdfwnlsdklrrrirkriAIMLQRtFALYGDDTVLDNV-LEALEEIGYEGKEA--VGRAVDLIEMVQLSHRITHiarDL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1956008863 156 SGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVIL 228
Cdd:TIGR03269 170 SGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWL 242
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
23-228 |
1.16e-18 |
|
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: 82.16 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 23 RVAFHHVHKSFVVNQQPVkvIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDR---- 98
Cdd:cd03244 2 DIEFKNVSLRYRPNLPPV--LKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDlrsr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 99 -AVVFQEHRLFPWlTVEQNieLGLLNEAltsRDKDILvqKAIELIGLNGFEKAYPHQL-----------SGGMSQRVAIA 166
Cdd:cd03244 80 iSIIPQDPVLFSG-TIRSN--LDPFGEY---SDEELW--QALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1956008863 167 RSLVVQPRIFLLDEPFGALDALTRHQMQNEllrIQSQQKMTTVF-ITHDVeEAVTLADRVVIL 228
Cdd:cd03244 152 RALLRKSKILVLDEATASVDPETDALIQKT---IREAFKDCTVLtIAHRL-DTIIDSDRILVL 210
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
39-235 |
1.41e-18 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 82.57 E-value: 1.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 39 PVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGldqdfdgRILIDGADVSGIGGDRAVVF------QEHRLF---P 109
Cdd:TIGR02323 15 GGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAG-------RLAPDHGTATYIMRSGAELElyqlseAERRRLmrtE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 110 WLTVEQNIELGL---------LNE---ALTSRDKDILVQKAIELIGLNGFEKA----YPHQLSGGMSQRVAIARSLVVQP 173
Cdd:TIGR02323 88 WGFVHQNPRDGLrmrvsaganIGErlmAIGARHYGNIRATAQDWLEEVEIDPTriddLPRAFSGGMQQRLQIARNLVTRP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1956008863 174 RIFLLDEPFGALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVILkpKPGRV 235
Cdd:TIGR02323 168 RLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVM--QQGRV 227
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
27-229 |
2.34e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 84.33 E-value: 2.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 27 HHVHKSFvvnqQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDRA------V 100
Cdd:PRK15439 15 RSISKQY----SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAhqlgiyL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 101 VFQEHRLFPWLTVEQNIELGLLNEALTSRDkdiLVQKAIEL-IGLNgfekayPHQLSGGMS----QRVAIARSLVVQPRI 175
Cdd:PRK15439 91 VPQEPLLFPNLSVKENILFGLPKRQASMQK---MKQLLAALgCQLD------LDSSAGSLEvadrQIVEILRGLMRDSRI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1956008863 176 FLLDEPFGaldALTRHQMQNELLRIQS--QQKMTTVFITHDVEEAVTLADRVVILK 229
Cdd:PRK15439 162 LILDEPTA---SLTPAETERLFSRIREllAQGVGIVFISHKLPEIRQLADRISVMR 214
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
47-238 |
2.37e-18 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 81.96 E-value: 2.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 47 NLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDR----AVV--FQEHRLFPWLTVEQNIEL- 119
Cdd:PRK11300 25 NLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQiarmGVVrtFQHVRLFREMTVIENLLVa 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 120 -----------GLLNEALTSRDKDILVQKA---IELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGAL 185
Cdd:PRK11300 105 qhqqlktglfsGLLKTPAFRRAESEALDRAatwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGL 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1956008863 186 DALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRV-VILKPKP---GRVEQI 238
Cdd:PRK11300 185 NPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIyVVNQGTPlanGTPEEI 241
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
40-228 |
2.42e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 84.52 E-value: 2.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 40 VKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGG--------DRAVVFQE--HRLFP 109
Cdd:PRK10261 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPgklqalrrDIQFIFQDpyASLDP 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 110 WLTVEQNIE-----LGLLN-EALTSRdkdilVQKAIELIGLNGfEKA--YPHQLSGGMSQRVAIARSLVVQPRIFLLDEP 181
Cdd:PRK10261 417 RQTVGDSIMeplrvHGLLPgKAAAAR-----VAWLLERVGLLP-EHAwrYPHEFSGGQRQRICIARALALNPKVIIADEA 490
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1956008863 182 FGALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVIL 228
Cdd:PRK10261 491 VSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVM 537
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
40-228 |
2.61e-18 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 82.85 E-value: 2.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 40 VKVIHDFNLEIKEGEFIAIVGSSGCGKS----TLLRLLA-----GLDQDFDGR-IL-IDGADVSGIGGDR-AVVFQE--H 105
Cdd:PRK09473 29 VTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAangriGGSATFNGReILnLPEKELNKLRAEQiSMIFQDpmT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 106 RLFPWLTV-EQNIELGLLNEALTSRD---KDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEP 181
Cdd:PRK09473 109 SLNPYMRVgEQLMEVLMLHKGMSKAEafeESVRMLDAVKMPEARKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEP 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1956008863 182 FGALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVIL 228
Cdd:PRK09473 189 TTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVM 235
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
25-229 |
4.47e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 83.42 E-value: 4.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 25 AFHHVHKSFvvnqqP-VKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADV----------SG 93
Cdd:PRK11288 6 SFDGIGKTF-----PgVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfasttaalaAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 94 IggdrAVVFQEHRLFPWLTVEQNIELGLLNEALTSRDKDILVQKA---IELIGLNGFEKAYPHQLSGGMSQRVAIARSLV 170
Cdd:PRK11288 81 V----AIIYQELHLVPEMTVAENLYLGQLPHKGGIVNRRLLNYEAreqLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1956008863 171 VQPRIFLLDEPFGALDALTRHQMQNELLRIQSQQKMtTVFITHDVEEAVTLADRVVILK 229
Cdd:PRK11288 157 RNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRV-ILYVSHRMEEIFALCDAITVFK 214
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
41-228 |
6.32e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 80.32 E-value: 6.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 41 KVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVS----------GIGgdraVVFQEHRLFPW 110
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllplhararrGIG----YLPQEASIFRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 111 LTVEQNIELGL-LNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALT 189
Cdd:PRK10895 93 LSVYDNLMAVLqIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPIS 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1956008863 190 RHQMQN--ELLRiqsqQKMTTVFIT-HDVEEAVTLADRVVIL 228
Cdd:PRK10895 173 VIDIKRiiEHLR----DSGLGVLITdHNVRETLAVCERAYIV 210
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
42-229 |
1.06e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 80.42 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 42 VIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGD----RAVVFQEHRLFPW-LTVEQN 116
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKevarRIGLLAQNATTPGdITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 117 IELGLL-NEALTSR----DKDIlVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDalTRH 191
Cdd:PRK10253 102 VARGRYpHQPLFTRwrkeDEEA-VTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD--ISH 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1956008863 192 QMqnELLRIQSQ----QKMTTVFITHDVEEAVTLADRVVILK 229
Cdd:PRK10253 179 QI--DLLELLSElnreKGYTLAAVLHDLNQACRYASHLIALR 218
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
41-238 |
2.25e-17 |
|
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: 78.22 E-value: 2.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 41 KVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDR-----AVVFQEHRLFPWlTVEQ 115
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDlrsslTIIPQDPTLFSG-TIRS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 116 NieLGLLNEaltSRDKDILVQKAIELIGLNgfekayphqLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQMQn 195
Cdd:cd03369 101 N--LDPFDE---YSDEEIYGALRVSEGGLN---------LSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQ- 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1956008863 196 ELLRiQSQQKMTTVFITHDVEeavTLADRVVILKPKPGRVEQI 238
Cdd:cd03369 166 KTIR-EEFTNSTILTIAHRLR---TIIDYDKILVMDAGEVKEY 204
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
46-229 |
3.71e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 78.34 E-value: 3.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 46 FNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLdQDFDGRILIDGADVSGIGGD-----RAVVFQEHRLFPWLTVEQNIELG 120
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAelarhRAYLSQQQSPPFAMPVFQYLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 121 LLNEALTSRDKDILVQKAIELiglnGFEKAYP---HQLSGGMSQRVAIARSLV-VQPRI------FLLDEPFGALDalTR 190
Cdd:COG4138 94 QPAGASSEAVEQLLAQLAEAL----GLEDKLSrplTQLSGGEWQRVRLAAVLLqVWPTInpegqlLLLDEPMNSLD--VA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1956008863 191 HQ-MQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVILK 229
Cdd:COG4138 168 QQaALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLK 207
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
38-228 |
5.03e-17 |
|
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: 77.76 E-value: 5.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 38 QPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGAD--------VSGIGgdraVVFQEHRLFP 109
Cdd:cd03267 32 REVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVpwkrrkkfLRRIG----VVFGQKTQLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 110 W-LTVeqnIELGLLNEALTSRDKDIL---VQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGAL 185
Cdd:cd03267 108 WdLPV---IDSFYLLAAIYDLPPARFkkrLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1956008863 186 DALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVIL 228
Cdd:cd03267 185 DVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVI 227
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
41-214 |
5.53e-17 |
|
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: 80.36 E-value: 5.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 41 KVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILI-DGADVsgiggdrAVVFQEHRLFPWLTVEQNIEL 119
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPqPGIKV-------GYLPQEPQLDPTKTVRENVEE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 120 GL---------LNE-----ALTSRDKDIL------VQKAIELIGLNGFEK---------------AYPHQLSGGMSQRVA 164
Cdd:TIGR03719 92 GVaeikdaldrFNEisakyAEPDADFDKLaaeqaeLQEIIDAADAWDLDSqleiamdalrcppwdADVTKLSGGERRRVA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1956008863 165 IARSLVVQPRIFLLDEPFGALDALTRHQMQNELLRIQSqqkmTTVFITHD 214
Cdd:TIGR03719 172 LCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG----TVVAVTHD 217
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
53-228 |
1.13e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 79.54 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 53 GEFIAIVGSSGCGKSTLLRLLAGLDQ--DFDGRILIDGADVSGIGGDR-AVVFQEHRLFPWLTVEQNI---ELGLLNEAL 126
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQgnNFTGTILANNRKPTKQILKRtGFVTQDDILYPHLTVRETLvfcSLLRLPKSL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 127 TSRDKDILVQKAIELIGLNGFEK-----AYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQMQNELLRIQ 201
Cdd:PLN03211 174 TKQEKILVAESVISELGLTKCENtiignSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLA 253
|
170 180
....*....|....*....|....*..
gi 1956008863 202 SQQKMTTVFITHDVEEAVTLADRVVIL 228
Cdd:PLN03211 254 QKGKTIVTSMHQPSSRVYQMFDSVLVL 280
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
46-228 |
1.14e-16 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 79.67 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 46 FNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVS----GIGGDRAVVFQEHRLFPWLTVEQNIelgL 121
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIEtnldAVRQSLGMCPQHNILFHHLTVAEHI---L 1025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 122 LNEALTSRDKD---ILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQMQNELL 198
Cdd:TIGR01257 1026 FYAQLKGRSWEeaqLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLL 1105
|
170 180 190
....*....|....*....|....*....|
gi 1956008863 199 RIQSQQkmTTVFITHDVEEAVTLADRVVIL 228
Cdd:TIGR01257 1106 KYRSGR--TIIMSTHHMDEADLLGDRIAII 1133
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
41-214 |
1.42e-16 |
|
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: 74.41 E-value: 1.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 41 KVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDgadvsgiggdravvfqehrlfpwltveQNIELG 120
Cdd:cd03221 14 LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG---------------------------STVKIG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 121 llnealtsrdkdilvqkaieliglngfekaYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQMQNELLRI 200
Cdd:cd03221 67 ------------------------------YFEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEY 116
|
170
....*....|....
gi 1956008863 201 QSqqkmTTVFITHD 214
Cdd:cd03221 117 PG----TVILVSHD 126
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
33-228 |
1.45e-16 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 77.92 E-value: 1.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 33 FVVNQQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQD----------FDGrilIDGADVSG------IGG 96
Cdd:PRK15093 13 FKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvtadrmrFDD---IDLLRLSPrerrklVGH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 97 DRAVVFQEHRlfPWLTVEQNIELGLLNEALTSRDKDILVQ-------KAIELIGLNGFE------KAYPHQLSGGMSQRV 163
Cdd:PRK15093 90 NVSMIFQEPQ--SCLDPSERVGRQLMQNIPGWTYKGRWWQrfgwrkrRAIELLHRVGIKdhkdamRSFPYELTEGECQKV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1956008863 164 AIARSLVVQPRIFLLDEPFGALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVIL 228
Cdd:PRK15093 168 MIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVL 232
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
34-228 |
4.26e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 77.37 E-value: 4.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 34 VVNQQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVS----------GIG---GDRav 100
Cdd:COG3845 265 VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITglsprerrrlGVAyipEDR-- 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 101 vfQEHRLFPWLTVEQNIELGLLNEALTSR----DKDILVQKAIELIglngfeKAY------PHQ----LSGGMSQRVAIA 166
Cdd:COG3845 343 --LGRGLVPDMSVAENLILGRYRRPPFSRggflDRKAIRAFAEELI------EEFdvrtpgPDTparsLSGGNQQKVILA 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1956008863 167 RSLVVQPRIFLLDEPFGALDALTRHQMQNELLRiQSQQKMTTVFITHDVEEAVTLADRVVIL 228
Cdd:COG3845 415 RELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLE-LRDAGAAVLLISEDLDEILALSDRIAVM 475
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
32-186 |
8.73e-16 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 74.11 E-value: 8.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 32 SFVVNQQPVKVIHDFNleIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDRAVVFQEH--RLFP 109
Cdd:PRK13543 18 AFSRNEEPVFGPLDFH--VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHlpGLKA 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1956008863 110 WLTVEQNieLGLLNeALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALD 186
Cdd:PRK13543 96 DLSTLEN--LHFLC-GLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
36-212 |
9.97e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 76.62 E-value: 9.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 36 NQQPVK-VIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQ---DFDGRILIDG--ADVSGIGGDRAVVFQEHRLFP 109
Cdd:TIGR00955 33 RERPRKhLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPkgvKGSGSVLLNGmpIDAKEMRAISAYVQQDDLFIP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 110 WLTVEQNIELGL---LNEALTSRDKDILVQKAIE----------LIGLNGFEKAyphqLSGGMSQRVAIARSLVVQPRIF 176
Cdd:TIGR00955 113 TLTVREHLMFQAhlrMPRRVTKKEKRERVDEVLQalglrkcantRIGVPGRVKG----LSGGERKRLAFASELLTDPPLL 188
|
170 180 190
....*....|....*....|....*....|....*.
gi 1956008863 177 LLDEPFGALDALTRHQMQNELLRIqsQQKMTTVFIT 212
Cdd:TIGR00955 189 FCDEPTSGLDSFMAYSVVQVLKGL--AQKGKTIICT 222
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
31-229 |
1.34e-15 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 76.29 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 31 KSFVVNQQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDR-----AVVFQEH 105
Cdd:PRK10789 319 RQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwrsrlAVVSQTP 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 106 RLFPwLTVEQNIELGL-------LNEA--LTSRDKDIL--VQKAIELIGLNGFekayphQLSGGMSQRVAIARSLVVQPR 174
Cdd:PRK10789 399 FLFS-DTVANNIALGRpdatqqeIEHVarLASVHDDILrlPQGYDTEVGERGV------MLSGGQKQRISIARALLLNAE 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1956008863 175 IFLLDEPFGALDALTRHQ-MQNelLRIQSQQKmtTVFITHDVEEAVTLADRVVILK 229
Cdd:PRK10789 472 ILILDDALSAVDGRTEHQiLHN--LRQWGEGR--TVIISAHRLSALTEASEILVMQ 523
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
41-229 |
1.49e-15 |
|
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: 73.07 E-value: 1.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 41 KVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDF---DGRILIDGADVSGIG----GDRAVVFQEHRLFPWLTV 113
Cdd:cd03233 21 PILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAekypGEIIYVSEEDVHFPTLTV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 114 EQNIELGLLnealtsrdkdilvqkaieligLNGfeKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQM 193
Cdd:cd03233 101 RETLDFALR---------------------CKG--NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEI 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 1956008863 194 QNELLRIQSQQKMTTVF-ITHDVEEAVTLADRVVILK 229
Cdd:cd03233 158 LKCIRTMADVLKTTTFVsLYQASDEIYDLFDKVLVLY 194
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
40-228 |
2.85e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 75.21 E-value: 2.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 40 VKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGL--DQDFDGRILIDGADVS----------GIggdrAVVFQEHRL 107
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVypHGSYEGEILFDGEVCRfkdirdsealGI----VIIHQELAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 108 FPWLTVEQNIELGllNEalTSR----DKDILVQKAIELIGLNGFEKAyPHQLSG----GMSQRVAIARSLVVQPRIFLLD 179
Cdd:NF040905 90 IPYLSIAENIFLG--NE--RAKrgviDWNETNRRARELLAKVGLDES-PDTLVTdigvGKQQLVEIAKALSKDVKLLILD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1956008863 180 EPFGAL-DALTRHQMqnELLRIQSQQKMTTVFITHDVEEAVTLADRVVIL 228
Cdd:NF040905 165 EPTAALnEEDSAALL--DLLLELKAQGITSIIISHKLNEIRRVADSITVL 212
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
56-214 |
3.15e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 75.16 E-value: 3.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 56 IAIVGSSGCGKSTLLRLLAGLDQDFDGR-ILIDGADVsGIggdravVFQEHRLFPWLTVEQNIELGL---------LNE- 124
Cdd:PRK11819 36 IGVLGLNGAGKSTLLRIMAGVDKEFEGEaRPAPGIKV-GY------LPQEPQLDPEKTVRENVEEGVaevkaaldrFNEi 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 125 ----ALTSRDKDIL------VQKAIELIGL----NGFEKAY-----PH------QLSGGMSQRVAIARSLVVQPRIFLLD 179
Cdd:PRK11819 109 yaayAEPDADFDALaaeqgeLQEIIDAADAwdldSQLEIAMdalrcPPwdakvtKLSGGERRRVALCRLLLEKPDMLLLD 188
|
170 180 190
....*....|....*....|....*....|....*
gi 1956008863 180 EPFGALDALTRHQMQNELlriqSQQKMTTVFITHD 214
Cdd:PRK11819 189 EPTNHLDAESVAWLEQFL----HDYPGTVVAVTHD 219
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
27-229 |
7.90e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 72.13 E-value: 7.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 27 HHVHKSFVVNQQPVKV-----IHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGD---R 98
Cdd:PRK10575 6 NHSDTTFALRNVSFRVpgrtlLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKafaR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 99 AVVFQEHRLFP--WLTVEQNIELG-------LLNEALTSRDKdilVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSL 169
Cdd:PRK10575 86 KVAYLPQQLPAaeGMTVRELVAIGrypwhgaLGRFGAADREK---VEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1956008863 170 VVQPRIFLLDEPFGALDalTRHQMQNELL--RIQSQQKMTTVFITHDVEEAVTLADRVVILK 229
Cdd:PRK10575 163 AQDSRCLLLDEPTSALD--IAHQVDVLALvhRLSQERGLTVIAVLHDINMAARYCDYLVALR 222
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
42-228 |
9.30e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 73.60 E-value: 9.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 42 VIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIG-----GDRAVVFQEhrlfPWL---TV 113
Cdd:PRK10790 356 VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLShsvlrQGVAMVQQD----PVVladTF 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 114 EQNIELGllnealtsrdKDI---LVQKAIELIGLNGFEKAYP-----------HQLSGGMSQRVAIARSLVVQPRIFLLD 179
Cdd:PRK10790 432 LANVTLG----------RDIseeQVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLLALARVLVQTPQILILD 501
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1956008863 180 EPFGALDALTRHQMQNELLRIqsQQKMTTVFITHDVEEAVTlADRVVIL 228
Cdd:PRK10790 502 EATANIDSGTEQAIQQALAAV--REHTTLVVIAHRLSTIVE-ADTILVL 547
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
19-229 |
1.11e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 73.28 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 19 NTQTRVAFHHVHKSFvvnqQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVS------ 92
Cdd:PRK09700 1 MATPYISMAGIGKSF----GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNkldhkl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 93 ----GIGgdraVVFQEHRLFPWLTVEQNIELGLLneaLTSR-------DKDILVQKAIELIGLNGFeKAYPHQLSGGMS- 160
Cdd:PRK09700 77 aaqlGIG----IIYQELSVIDELTVLENLYIGRH---LTKKvcgvniiDWREMRVRAAMMLLRVGL-KVDLDEKVANLSi 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1956008863 161 ---QRVAIARSLVVQPRIFLLDEPfgaLDALTRHQMqNELLRIQSQQK---MTTVFITHDVEEAVTLADRVVILK 229
Cdd:PRK09700 149 shkQMLEIAKTLMLDAKVIIMDEP---TSSLTNKEV-DYLFLIMNQLRkegTAIVYISHKLAEIRRICDRYTVMK 219
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
41-236 |
1.27e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 71.14 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 41 KVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSgIGGDRAVVfqehrlfpwltveqnielg 120
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQ-FGREASLI------------------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 121 llnEALtSRDKDILVqkAIELIGLNGFEKAY-----PHQLSGGMSQRVAIARSLVVQPRIFLLDEpFGA-LDALTRHQMQ 194
Cdd:COG2401 104 ---DAI-GRKGDFKD--AVELLNAVGLSDAVlwlrrFKELSTGQKFRFRLALLLAERPKLLVIDE-FCShLDRQTAKRVA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1956008863 195 NELLRIQSQQKMTTVFITH--DVEEAvtLADRVVILKPKPGRVE 236
Cdd:COG2401 177 RNLQKLARRAGITLVVATHhyDVIDD--LQPDLLIFVGYGGVPE 218
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
24-238 |
1.32e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 73.08 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 24 VAFHHVHKSFVVNqqPVkvihdfNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDR----- 98
Cdd:PRK10522 328 VTFAYQDNGFSVG--PI------NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDyrklf 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 99 AVVFQEHRLFPWLTVEQNIELgllnealtsrdKDILVQKAIELIGLNGFEKAYPH-----QLSGGMSQRVAIARSLVVQP 173
Cdd:PRK10522 400 SAVFTDFHLFDQLLGPEGKPA-----------NPALVEKWLERLKMAHKLELEDGrisnlKLSKGQKKRLALLLALAEER 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1956008863 174 RIFLLDEPFGALDALTRHQMQNELLRiQSQQKMTTVF-ITHDvEEAVTLADRvvILKPKPGRVEQI 238
Cdd:PRK10522 469 DILLLDEWAADQDPHFRREFYQVLLP-LLQEMGKTIFaISHD-DHYFIHADR--LLEMRNGQLSEL 530
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
37-260 |
1.77e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 73.14 E-value: 1.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 37 QQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGA----DV------SGIGgdraVVFQEHR 106
Cdd:PTZ00265 395 RKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShnlkDInlkwwrSKIG----VVSQDPL 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 107 LFPwLTVEQNIELGL-------------------------------------LNEALTSRDKDILVQ--KAIELIG---- 143
Cdd:PTZ00265 471 LFS-NSIKNNIKYSLyslkdlealsnyynedgndsqenknkrnscrakcagdLNDMSNTTDSNELIEmrKNYQTIKdsev 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 144 --------LNGFEKAYP-----------HQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQMQNELLRIQSQQ 204
Cdd:PTZ00265 550 vdvskkvlIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNE 629
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1956008863 205 KMTTVFITHDVeEAVTLADRVVIL--KPKPGRVEQIIPVNLPRPRNRSSFELHQLKEQ 260
Cdd:PTZ00265 630 NRITIIIAHRL-STIRYANTIFVLsnRERGSTVDVDIIGEDPTKDNKENNNKNNKDDN 686
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
57-228 |
2.33e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 71.28 E-value: 2.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 57 AIVGSSGCGKSTLLRLLAGLDQD-----FDGRILIDGA------DVSGIGGDRAVVFQEHRLFPwLTVEQNIELGLLNEA 125
Cdd:PRK14271 51 SLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRsifnyrDVLEFRRRVGMLFQRPNPFP-MSIMDNVLAGVRAHK 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 126 LTSRDK-DILVQKAIELIGLNGFEKA----YPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQMQnELLRI 200
Cdd:PRK14271 130 LVPRKEfRGVAQARLTEVGLWDAVKDrlsdSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIE-EFIRS 208
|
170 180
....*....|....*....|....*...
gi 1956008863 201 QSqQKMTTVFITHDVEEAVTLADRVVIL 228
Cdd:PRK14271 209 LA-DRLTVIIVTHNLAQAARISDRAALF 235
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
48-228 |
2.42e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 72.68 E-value: 2.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 48 LEIKEGEFIAIVGSSGCGKSTLLRLLAG---LDqdfDGRILIDGaDV----------------------SGIGGDRAVVF 102
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGevlLD---DGRIIYEQ-DLivarlqqdpprnvegtvydfvaEGIEEQAEYLK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 103 QEHRLFPWLTV---EQNI-ELGLLNEAL--------TSRDKDILvqkaiELIGLNGFEKAypHQLSGGMSQRVAIARSLV 170
Cdd:PRK11147 100 RYHDISHLVETdpsEKNLnELAKLQEQLdhhnlwqlENRINEVL-----AQLGLDPDAAL--SSLSGGWLRKAALGRALV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1956008863 171 VQPRIFLLDEPFGALDALTRHQMQNELLRIQSqqkmTTVFITHDVEEAVTLADRVVIL 228
Cdd:PRK11147 173 SNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG----SIIFISHDRSFIRNMATRIVDL 226
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
5-213 |
4.07e-14 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 71.97 E-value: 4.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 5 LNTNTEKHHQSFQANT-QTRVAFHHVHKSFVVNQQPVkvIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGR 83
Cdd:PRK11176 322 LDLEQEKDEGKRVIERaKGDIEFRNVTFTYPGKEVPA--LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGE 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 84 ILIDGADV-----SGIGGDRAVVFQEHRLFPwLTVEQNIelgllneALTSRDK----DIlvQKAIEL------------- 141
Cdd:PRK11176 400 ILLDGHDLrdytlASLRNQVALVSQNVHLFN-DTIANNI-------AYARTEQysreQI--EEAARMayamdfinkmdng 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1956008863 142 ----IGLNGFekayphQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQMQNELLRIQSQQkmTTVFITH 213
Cdd:PRK11176 470 ldtvIGENGV------LLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAH 537
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
40-228 |
5.56e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 70.50 E-value: 5.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 40 VKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGAD--------VSGIGgdraVVF-QEHRLFPW 110
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVpfkrrkefARRIG----VVFgQRSQLWWD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 111 LTVEQNIEL-----GLLNEALTSRdkdilVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGAL 185
Cdd:COG4586 111 LPAIDSFRLlkaiyRIPDAEYKKR-----LDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1956008863 186 DALTRHQMQnELLRIQSQQKMTTVFIT-HDVEEAVTLADRVVIL 228
Cdd:COG4586 186 DVVSKEAIR-EFLKEYNRERGTTILLTsHDMDDIEALCDRVIVI 228
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
24-234 |
1.54e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 70.44 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 24 VAFHHVHKSFVVNQQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRllagldqDFDGRILIDGADV-----SGIGGDR 98
Cdd:PTZ00265 1226 IVFKNEHTNDMTNEQDYQGDEEQNVGMKNVNEFSLTKEGGSGEDSTVF-------KNSGKILLDGVDIcdynlKDLRNLF 1298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 99 AVVFQEHRLFPwLTVEQNIELGllNEALTSRDkdilVQKAIELIGLNGFEKAYPHQ-----------LSGGMSQRVAIAR 167
Cdd:PTZ00265 1299 SIVSQEPMLFN-MSIYENIKFG--KEDATRED----VKRACKFAAIDEFIESLPNKydtnvgpygksLSGGQKQRIAIAR 1371
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1956008863 168 SLVVQPRIFLLDEPFGALDALTRHQMQNELLRIQSQQKMTTVFITHDVeEAVTLADRVVILKpKPGR 234
Cdd:PTZ00265 1372 ALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI-ASIKRSDKIVVFN-NPDR 1436
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
24-236 |
2.46e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 69.32 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 24 VAFHHVHKSFvvnqQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIdGADVSgIGgdravVF- 102
Cdd:COG0488 316 LELEGLSKSY----GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK-IG-----YFd 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 103 QEHRLF-PWLTVEQNIELGllnealtSRDKDIlvQKAIELIGLNGF--EKAY-P-HQLSGGMSQRVAIARSLVVQPRIFL 177
Cdd:COG0488 385 QHQEELdPDKTVLDELRDG-------APGGTE--QEVRGYLGRFLFsgDDAFkPvGVLSGGEKARLALAKLLLSPPNVLL 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1956008863 178 LDEPFGALDALTRHQMQNELLRIQSqqkmTTVFITHD---VEeavTLADRVVILkpKPGRVE 236
Cdd:COG0488 456 LDEPTNHLDIETLEALEEALDDFPG----TVLLVSHDryfLD---RVATRILEF--EDGGVR 508
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
42-228 |
2.50e-13 |
|
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: 69.97 E-value: 2.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 42 VIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIG-----GDRAVVFQEHRLFPWlTVEQN 116
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGlhdlrFKITIIPQDPVLFSG-SLRMN 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 117 ielglLNEALTSRDKDILVqkAIELIGLNGFEKAYP----HQ-------LSGGMSQRVAIARSLVVQPRIFLLDEPFGAL 185
Cdd:TIGR00957 1380 -----LDPFSQYSDEEVWW--ALELAHLKTFVSALPdkldHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAV 1452
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1956008863 186 DALTRHQMQNEllrIQSQQKMTTVF-ITHDVEeavTLAD--RVVIL 228
Cdd:TIGR00957 1453 DLETDNLIQST---IRTQFEDCTVLtIAHRLN---TIMDytRVIVL 1492
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
45-228 |
2.51e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 69.62 E-value: 2.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 45 DFNLEIKEGEFIAIVGSSGCGKSTLLRLLAG-LDQDFDGRILIDGAdvsgiggdRAVVFQehrlFPWL---TVEQNIELG 120
Cdd:PLN03232 635 DINLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVIRGS--------VAYVPQ----VSWIfnaTVRENILFG 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 121 ----------LLNEALTSRDKDILVQKAIELIGLNGFekayphQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTR 190
Cdd:PLN03232 703 sdfeserywrAIDVTALQHDLDLLPGRDLTEIGERGV------NISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVA 776
|
170 180 190
....*....|....*....|....*....|....*...
gi 1956008863 191 HQMQNELLRIQSQQKmTTVFITHDVeEAVTLADRVVIL 228
Cdd:PLN03232 777 HQVFDSCMKDELKGK-TRVLVTNQL-HFLPLMDRIILV 812
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
46-229 |
3.69e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 67.27 E-value: 3.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 46 FNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLdQDFDGRILIDGADVSGIGGD-----RAVVFQEHRLFPWLTVEQNIELG 120
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAelarhRAYLSQQQTPPFAMPVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 121 LLNEALTSRDKDILVQKAiELIGLNGFEKAYPHQLSGGMSQRVAIARS-LVVQPRI------FLLDEPFGALD-----AL 188
Cdd:PRK03695 94 QPDKTRTEAVASALNEVA-EALGLDDKLGRSVNQLSGGEWQRVRLAAVvLQVWPDInpagqlLLLDEPMNSLDvaqqaAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1956008863 189 TRhqmqneLLRIQSQQKMTTVFITHDVEEAVTLADRVVILK 229
Cdd:PRK03695 173 DR------LLSELCQQGIAVVMSSHDLNHTLRHADRVWLLK 207
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-229 |
3.95e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.88 E-value: 3.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 20 TQTRVAFHHVHKSFvvnqqP-VKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVS------ 92
Cdd:PRK10762 1 MQALLQLKGIDKAF-----PgVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpks 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 93 ----GIGgdraVVFQEHRLFPWLTVEQNIELGllnEALTSRDKDILVQKAIE-----LIGLNgfEKAYPHQLSGGMS--- 160
Cdd:PRK10762 76 sqeaGIG----IIHQELNLIPQLTIAENIFLG---REFVNRFGRIDWKKMYAeadklLARLN--LRFSSDKLVGELSige 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1956008863 161 -QRVAIARSLVVQPRIFLLDEPfgaLDALTRHQMQ------NELlriqSQQKMTTVFITHDVEEAVTLADRVVILK 229
Cdd:PRK10762 147 qQMVEIAKVLSFESKVIIMDEP---TDALTDTETEslfrviREL----KSQGRGIVYISHRLKEIFEICDDVTVFR 215
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
41-213 |
4.63e-13 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 67.01 E-value: 4.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 41 KVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLD--QDFDGRILIDGADVSGIGGD-RA-----VVFQ---EhrlFP 109
Cdd:COG0396 14 EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDeRAragifLAFQypvE---IP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 110 WLTVEQnielgLLNEALTSRDKDIL--------VQKAIELIGLN----------GFekayphqlSGGMSQRVAIARSLVV 171
Cdd:COG0396 91 GVSVSN-----FLRTALNARRGEELsareflklLKEKMKELGLDedfldryvneGF--------SGGEKKRNEILQMLLL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1956008863 172 QPRIFLLDEPFGALDAltrhqmqnELLRIQSQ-------QKMTTVFITH 213
Cdd:COG0396 158 EPKLAILDETDSGLDI--------DALRIVAEgvnklrsPDRGILIITH 198
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
45-228 |
1.02e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 67.38 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 45 DFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGG----DRAVVF-----QEHRLFPWLTVEQ 115
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTaqrlARGLVYlpedrQSSGLYLDAPLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 116 NIELGLLNE----ALTSRDKDILVQKAIEL-IGLNGFEKAYpHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTR 190
Cdd:PRK15439 361 NVCALTHNRrgfwIKPARENAVLERYRRALnIKFNHAEQAA-RTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSAR 439
|
170 180 190
....*....|....*....|....*....|....*...
gi 1956008863 191 HQMQnELLRIQSQQKMTTVFITHDVEEAVTLADRVVIL 228
Cdd:PRK15439 440 NDIY-QLIRSIAAQNVAVLFISSDLEEIEQMADRVLVM 476
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
38-236 |
1.49e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 67.50 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 38 QPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILidgADVSgiggdRAVVFQEhrlfPWL---TVE 114
Cdd:PTZ00243 671 EPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW---AERS-----IAYVPQQ----AWImnaTVR 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 115 QNIElgLLNEALTSRDKDIL--VQKAIELIGLNG------FEKAYphQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALD 186
Cdd:PTZ00243 739 GNIL--FFDEEDAARLADAVrvSQLEADLAQLGGgleteiGEKGV--NLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1956008863 187 ALTRHQMQNELLRIQSQQKmTTVFITHDVeEAVTLADRVVILkpKPGRVE 236
Cdd:PTZ00243 815 AHVGERVVEECFLGALAGK-TRVLATHQV-HVVPRADYVVAL--GDGRVE 860
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
42-228 |
1.80e-12 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 67.24 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 42 VIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGadvsgiggdrAVVFQEHrlFPWL---TVEQNIE 118
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG----------RISFSPQ--TSWImpgTIKDNII 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 119 LGL----------LNEALTSRDKDILVQKAIELIGLNGFekayphQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDAL 188
Cdd:TIGR01271 509 FGLsydeyrytsvIKACQLEEDIALFPEKDKTVLGEGGI------TLSGGQRARISLARAVYKDADLYLLDSPFTHLDVV 582
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1956008863 189 TRHQM-QNELLRIQSQQkmTTVFITHDVEEaVTLADRVVIL 228
Cdd:TIGR01271 583 TEKEIfESCLCKLMSNK--TRILVTSKLEH-LKKADKILLL 620
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
42-228 |
1.92e-12 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 65.65 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 42 VIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGadvsgiggdrAVVFQEHrlFPWL---TVEQNIE 118
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG----------RISFSSQ--FSWImpgTIKENII 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 119 LGLLNEALTSR--------DKDI--LVQKAIELIGLNGFekayphQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDAL 188
Cdd:cd03291 120 FGVSYDEYRYKsvvkacqlEEDItkFPEKDNTVLGEGGI------TLSGGQRARISLARAVYKDADLYLLDSPFGYLDVF 193
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1956008863 189 TRHQMQNELLRIQSQQKmTTVFITHDVEEaVTLADRVVIL 228
Cdd:cd03291 194 TEKEIFESCVCKLMANK-TRILVTSKMEH-LKKADKILIL 231
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
43-215 |
2.65e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 66.89 E-value: 2.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 43 IHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGAdvsgiggdRAVVFQEhrlfPWL---TVEQNIEL 119
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--------VAYVPQQ----AWIqndSLRENILF 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 120 G-LLNE----------ALTSrDKDILVQKAIELIGLNGFekayphQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDA- 187
Cdd:TIGR00957 722 GkALNEkyyqqvleacALLP-DLEILPSGDRTEIGEKGV------NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAh 794
|
170 180
....*....|....*....|....*...
gi 1956008863 188 LTRHQMQNELLRIQSQQKMTTVFITHDV 215
Cdd:TIGR00957 795 VGKHIFEHVIGPEGVLKNKTRILVTHGI 822
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
40-233 |
3.00e-12 |
|
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: 63.36 E-value: 3.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 40 VKVIHDFNL-----EIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSgiggdravvfqehrlfpwltve 114
Cdd:cd03222 7 VKRYGVFFLlvelgVVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV---------------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 115 qnielgllnealtsrdkdilvqkaieliglngfEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQMQ 194
Cdd:cd03222 65 ---------------------------------YKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAA 111
|
170 180 190
....*....|....*....|....*....|....*....
gi 1956008863 195 NELLRIQSQQKMTTVFITHDVEEAVTLADRVVILKPKPG 233
Cdd:cd03222 112 RAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEGEPG 150
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
45-234 |
5.26e-12 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 65.58 E-value: 5.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 45 DFNL-----EIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDfDGRILIDGADVS----GIGGDRAvvfqehrlfpwLTVEQ 115
Cdd:COG1245 353 GFSLeveggEIREGEVLGIVGPNGIGKTTFAKILAGVLKP-DEGEVDEDLKISykpqYISPDYD-----------GTVEE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 116 nielgLLNEALTSRDKDILVQkaIELIGLNGFEKAYPHQ---LSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQ 192
Cdd:COG1245 421 -----FLRSANTDDFGSSYYK--TEIIKPLGLEKLLDKNvkdLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLA 493
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1956008863 193 MQNELLRIQSQQKMTTVFITHDVEEAVTLADRVVILKPKPGR 234
Cdd:COG1245 494 VAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMVFEGEPGV 535
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
40-228 |
6.01e-12 |
|
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: 65.23 E-value: 6.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 40 VKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGL-DQDFDGRILIDGADVS------GIGGDRAVVFQE---HRLFP 109
Cdd:TIGR02633 273 RKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDirnpaqAIRAGIAMVPEDrkrHGIVP 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 110 WLTVEQNIELGLLNE-ALTSRDKDILVQKAI-ELIGLNGFEKAYPH----QLSGGMSQRVAIARSLVVQPRIFLLDEPFG 183
Cdd:TIGR02633 353 ILGVGKNITLSVLKSfCFKMRIDAAAELQIIgSAIQRLKVKTASPFlpigRLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1956008863 184 ALDALTRHQMQnELLRIQSQQKMTTVFITHDVEEAVTLADRVVIL 228
Cdd:TIGR02633 433 GVDVGAKYEIY-KLINQLAQEGVAIIVVSSELAEVLGLSDRVLVI 476
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
43-229 |
9.37e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 63.75 E-value: 9.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 43 IHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDRAVVF--QEHRL---FPWLtVEQNI 117
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYvpQSEEVdwsFPVL-VEDVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 118 ------ELGLLNEAlTSRDKDIlVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRH 191
Cdd:PRK15056 102 mmgrygHMGWLRRA-KKRDRQI-VTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEA 179
|
170 180 190
....*....|....*....|....*....|....*...
gi 1956008863 192 QMQNeLLRIQSQQKMTTVFITHDVEEAVTLADRVVILK 229
Cdd:PRK15056 180 RIIS-LLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVK 216
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
45-234 |
3.02e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 63.29 E-value: 3.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 45 DFNL-----EIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDgADVS----GIGGDRAVvfqehrlfpwlTVEQ 115
Cdd:PRK13409 352 DFSLeveggEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKISykpqYIKPDYDG-----------TVED 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 116 NieLGLLNEALTSR--DKDILVQKAIELIglngFEKaYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQM 193
Cdd:PRK13409 420 L--LRSITDDLGSSyyKSEIIKPLQLERL----LDK-NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAV 492
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1956008863 194 QNELLRIQSQQKMTTVFITHDVEEAVTLADRVVILKPKPGR 234
Cdd:PRK13409 493 AKAIRRIAEEREATALVVDHDIYMIDYISDRLMVFEGEPGK 533
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
36-212 |
3.86e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 63.22 E-value: 3.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 36 NQQPVkvIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAG-LDQDFDGRILIDGAdvsgiggdRAVVFQEHRLFPwLTVE 114
Cdd:PLN03130 628 AERPT--LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRGT--------VAYVPQVSWIFN-ATVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 115 QNIELGLLNEA--------LTS--RDKDILVQKAIELIGLNGFekayphQLSGGMSQRVAIARSLVVQPRIFLLDEPFGA 184
Cdd:PLN03130 697 DNILFGSPFDPeryeraidVTAlqHDLDLLPGGDLTEIGERGV------NISGGQKQRVSMARAVYSNSDVYIFDDPLSA 770
|
170 180
....*....|....*....|....*...
gi 1956008863 185 LDALTRHQMQNELLRIQSQQKmTTVFIT 212
Cdd:PLN03130 771 LDAHVGRQVFDKCIKDELRGK-TRVLVT 797
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
23-217 |
5.33e-11 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 62.60 E-value: 5.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 23 RVAFHHVHKSFVVNQQPVKVIHDF----------------NLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILI 86
Cdd:PRK13545 4 KVKFEHVTKKYKMYNKPFDKLKDLffrskdgeyhyalnniSFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 87 DG-----ADVSGIGGDravvfqehrlfpwLTVEQNIELGLLNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQ 161
Cdd:PRK13545 84 KGsaaliAISSGLNGQ-------------LTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKS 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1956008863 162 RVAIARSLVVQPRIFLLDEPFGALDALTRHQMQNELLRIQSQQKmTTVFITHDVEE 217
Cdd:PRK13545 151 RLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQGK-TIFFISHSLSQ 205
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
47-228 |
6.68e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 61.95 E-value: 6.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 47 NLEIKEGEFIAIVGSSGCGKSTLLRLLAGldqdfdgrilidgaDVSGIGGDRAVVFQE-HRL-FPWLT--VEQniELGLL 122
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAG--------------ELPLLSGERQSQFSHiTRLsFEQLQklVSD--EWQRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 123 NEALTSRDKDILVQKAIELIgLNGFEKA-----YPHQ-------------LSGGMSQRVAIARSLVVQPRIFLLDEPFGA 184
Cdd:PRK10938 87 NTDMLSPGEDDTGRTTAEII-QDEVKDParceqLAQQfgitalldrrfkyLSTGETRKTLLCQALMSEPDLLILDEPFDG 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1956008863 185 LDALTRHQMQnELLRIQSQQKMTTVFITHDVEEAVTLADRVVIL 228
Cdd:PRK10938 166 LDVASRQQLA-ELLASLHQSGITLVLVLNRFDEIPDFVQFAGVL 208
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
41-213 |
1.26e-10 |
|
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: 59.46 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 41 KVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGlDQDF---DGRILIDGADVS----------GIGgdraVVFQEHRL 107
Cdd:cd03217 14 EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HPKYevtEGEILFKGEDITdlppeerarlGIF----LAFQYPPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 108 FPWLTVEQniELGLLNEaltsrdkdilvqkaieliglnGFekayphqlSGGMSQRVAIARSLVVQPRIFLLDEPFGALD- 186
Cdd:cd03217 89 IPGVKNAD--FLRYVNE---------------------GF--------SGGEKKRNEILQLLLLEPDLAILDEPDSGLDi 137
|
170 180
....*....|....*....|....*...
gi 1956008863 187 -ALtrhQMQNELLRIQSQQKMTTVFITH 213
Cdd:cd03217 138 dAL---RLVAEVINKLREEGKSVLIITH 162
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
47-218 |
2.35e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 60.52 E-value: 2.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 47 NLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADV--SGIGGDRAVVF--QEHRLFPWLTVEQNIEL--- 119
Cdd:NF033858 286 SFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdaGDIATRRRVGYmsQAFSLYGELTVRQNLELhar 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 120 --GLLNEALTSRdkdilVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQMQNEL 197
Cdd:NF033858 366 lfHLPAAEIAAR-----VAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLL 440
|
170 180
....*....|....*....|..
gi 1956008863 198 LRIQSQQKMtTVFI-THDVEEA 218
Cdd:NF033858 441 IELSREDGV-TIFIsTHFMNEA 461
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
41-229 |
2.95e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 60.31 E-value: 2.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 41 KVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSgIGGDRAVVFQ------EHR----LFPW 110
Cdd:PRK11288 267 GLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID-IRSPRDAIRAgimlcpEDRkaegIIPV 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 111 LTVEQNIELG----------LLNEALTSRDKDILVQK-------AIELIGlngfekayphQLSGGMSQRVAIARSLVVQP 173
Cdd:PRK11288 346 HSVADNINISarrhhlragcLINNRWEAENADRFIRSlniktpsREQLIM----------NLSGGNQQKAILGRWLSEDM 415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1956008863 174 RIFLLDEPFGALDALTRHQMQNELLRIqSQQKMTTVFITHDVEEAVTLADRVVILK 229
Cdd:PRK11288 416 KVILLDEPTRGIDVGAKHEIYNVIYEL-AAQGVAVLFVSSDLPEVLGVADRIVVMR 470
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
46-129 |
3.32e-10 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 60.20 E-value: 3.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 46 FNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDR-----AVVFQEHRLFPWLtveqnieLG 120
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAyrqlfSAVFSDFHLFDRL-------LG 423
|
....*....
gi 1956008863 121 LLNEALTSR 129
Cdd:COG4615 424 LDGEADPAR 432
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
42-229 |
5.87e-10 |
|
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: 58.38 E-value: 5.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 42 VIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIG-----GDRAVVFQEHRLFpwltvEQN 116
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPlhtlrSRLSIILQDPILF-----SGS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 117 IELGLLNEALTSRDKdilVQKAIELIGLNGFEKAYPHQL-----------SGGMSQRVAIARSLVVQPRIFLLDEPFGAL 185
Cdd:cd03288 111 IRFNLDPECKCTDDR---LWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEATASI 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1956008863 186 DALTRHQMQNELLRIQSQQkmTTVFITHDVEEAVTlADRVVILK 229
Cdd:cd03288 188 DMATENILQKVVMTAFADR--TVVTIAHRVSTILD-ADLVLVLS 228
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
42-231 |
7.70e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 58.75 E-value: 7.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 42 VIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAG-LDQDfDGRI-LIDGADVSGIGGDRAVVFQEHR-LFPWLTV----- 113
Cdd:PRK15064 334 LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGeLEPD-SGTVkWSENANIGYYAQDHAYDFENDLtLFDWMSQwrqeg 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 114 --EQNIElGLLNEALTSRDkDIlvQKAIELiglngfekayphqLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRH 191
Cdd:PRK15064 413 ddEQAVR-GTLGRLLFSQD-DI--KKSVKV-------------LSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIE 475
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1956008863 192 QMQNELlriqSQQKMTTVFITHDVEEAVTLADRVVILKPK 231
Cdd:PRK15064 476 SLNMAL----EKYEGTLIFVSHDREFVSSLATRIIEITPD 511
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
40-228 |
8.12e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 58.79 E-value: 8.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 40 VKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQD-FDGRILIDGADVS----------GIG---GDRavvfQEH 105
Cdd:PRK13549 275 IKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGrWEGEIFIDGKPVKirnpqqaiaqGIAmvpEDR----KRD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 106 RLFPWLTVEQNIELGLLNE-ALTSRDKDILVQKAI-ELIGLNGFEKAYPHQ----LSGGMSQRVAIARSLVVQPRIFLLD 179
Cdd:PRK13549 351 GIVPVMGVGKNITLAALDRfTGGSRIDDAAELKTIlESIQRLKVKTASPELaiarLSGGNQQKAVLAKCLLLNPKILILD 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1956008863 180 EPFGALDALTRH---QMQNELlriqSQQKMTTVFITHDVEEAVTLADRVVIL 228
Cdd:PRK13549 431 EPTRGIDVGAKYeiyKLINQL----VQQGVAIIVISSELPEVLGLSDRVLVM 478
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
43-228 |
9.05e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.86 E-value: 9.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 43 IHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVS----------GIggdraVVFQEHR----LF 108
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVtrspqdglanGI-----VYISEDRkrdgLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 109 PWLTVEQNIELGLLNE------ALTSRDKDILVQKAIEL-----------IGLngfekayphqLSGGMSQRVAIARSLVV 171
Cdd:PRK10762 343 LGMSVKENMSLTALRYfsraggSLKHADEQQAVSDFIRLfniktpsmeqaIGL----------LSGGNQQKVAIARGLMT 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 172 QPRIFLLDEPFGALDALTR---HQMQNELlriqSQQKMTTVFITHDVEEAVTLADRVVIL 228
Cdd:PRK10762 413 RPKVLILDEPTRGVDVGAKkeiYQLINQF----KAEGLSIILVSSEMPEVLGMSDRILVM 468
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
41-186 |
1.73e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 56.66 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 41 KVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGiggdraVVFQEHRLFPW--LTVEQNIE 118
Cdd:PRK09544 18 RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIG------YVPQKLYLDTTlpLTVNRFLR 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1956008863 119 LgllneALTSRDKDILvqKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALD 186
Cdd:PRK09544 92 L-----RPGTKKEDIL--PALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
29-229 |
2.14e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.43 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 29 VHKSFvvnqQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDRAV------VF 102
Cdd:PRK10982 4 ISKSF----PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALengismVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 103 QEHRLFPWLTVEQNIELGL--LNEALTSRDKDILVQKAI--EL-IGLNGFEKAypHQLSGGMSQRVAIARSLVVQPRIFL 177
Cdd:PRK10982 80 QELNLVLQRSVMDNMWLGRypTKGMFVDQDKMYRDTKAIfdELdIDIDPRAKV--ATLSVSQMQMIEIAKAFSYNAKIVI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1956008863 178 LDEPfgaLDALTRHQMqNELLRIQSQQK---MTTVFITHDVEEAVTLADRVVILK 229
Cdd:PRK10982 158 MDEP---TSSLTEKEV-NHLFTIIRKLKergCGIVYISHKMEEIFQLCDEITILR 208
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
41-239 |
2.86e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.10 E-value: 2.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 41 KVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVS------GIGGDRAVVFQEHR---LFPWL 111
Cdd:PRK09700 277 KKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISprspldAVKKGMAYITESRRdngFFPNF 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 112 TVEQNIE-------------LGLLNEaltsRDKDILVQKAIELIGL--NGFEKAYpHQLSGGMSQRVAIARSLVVQPRIF 176
Cdd:PRK09700 357 SIAQNMAisrslkdggykgaMGLFHE----VDEQRTAENQRELLALkcHSVNQNI-TELSGGNQQKVLISKWLCCCPEVI 431
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1956008863 177 LLDEPFGALDALTRHQMQnELLRIQSQQKMTTVFITHDVEEAVTLADRVVILkpKPGRVEQII 239
Cdd:PRK09700 432 IFDEPTRGIDVGAKAEIY-KVMRQLADDGKVILMVSSELPEIITVCDRIAVF--CEGRLTQIL 491
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
32-195 |
4.18e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 54.88 E-value: 4.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 32 SFVVNQqpvKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIgGDRAVVFQEHRLFPWL 111
Cdd:PRK13541 8 QFNIEQ---KNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNI-AKPYCTYIGHNLGLKL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 112 --TVEQNieLGLLNEALTSRDkdiLVQKAIELIGLNGF--EKAYphQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDA 187
Cdd:PRK13541 84 emTVFEN--LKFWSEIYNSAE---TLYAAIHYFKLHDLldEKCY--SLSSGMQKIVAIARLIACQSDLWLLDEVETNLSK 156
|
....*...
gi 1956008863 188 LTRHQMQN 195
Cdd:PRK13541 157 ENRDLLNN 164
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
33-207 |
1.33e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 53.80 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 33 FVVNQQPVkvIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADvsgIGGDRA-----VVFQEHR- 106
Cdd:PRK13540 9 FDYHDQPL--LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQS---IKKDLCtyqkqLCFVGHRs 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 107 -LFPWLTVEQNIelgLLNEALTSRDKDIlvqkaIELIGLNGFEKA--YP-HQLSGGMSQRVAIARSLVVQPRIFLLDEPF 182
Cdd:PRK13540 84 gINPYLTLRENC---LYDIHFSPGAVGI-----TELCRLFSLEHLidYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
170 180 190
....*....|....*....|....*....|....
gi 1956008863 183 GALDALT---------RHQMQNELLRIQSQQKMT 207
Cdd:PRK13540 156 VALDELSlltiitkiqEHRAKGGAVLLTSHQDLP 189
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
51-233 |
1.75e-08 |
|
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: 53.91 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 51 KEGEFIAIVGSSGCGKSTLLRLLAG------------------LD-------QDFDGRILIDGADVsgiggdrAVVFQEH 105
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGklkpnlgkfddppdwdeiLDefrgselQNYFTKLLEGDVKV-------IVKPQYV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 106 RLFPwLTVEQNIElgllnEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGAL 185
Cdd:cd03236 97 DLIP-KAVKGKVG-----ELLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1956008863 186 DALTRHQMQnELLRIQSQQKMTTVFITHDVEEAVTLADRVVILKPKPG 233
Cdd:cd03236 171 DIKQRLNAA-RLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCLYGEPG 217
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
42-216 |
1.87e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 54.92 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 42 VIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLdQDFDGRILIDGadvsgIGGDRAVVFQEHRLFPWLTVEQNIELGL 121
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDG-----VSWNSVTLQTWRKAFGVIPQKVFIFSGT 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 122 LNEALT--SRDKDILVQKAIELIGLNGFEKAYPHQL-----------SGGMSQRVAIARSLVVQPRIFLLDEPFGALDAL 188
Cdd:TIGR01271 1308 FRKNLDpyEQWSDEEIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKAKILLLDEPSAHLDPV 1387
|
170 180
....*....|....*....|....*...
gi 1956008863 189 TrHQMQNELLRiQSQQKMTTVFITHDVE 216
Cdd:TIGR01271 1388 T-LQIIRKTLK-QSFSNCTVILSEHRVE 1413
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
53-224 |
2.43e-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: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 53 GEFIAIVGSSGCGKSTLLRLLAG-LDQDFDGRILIDGADVSGIGGDRAVVFQEHRlfpwltveqnielgllnealtsrdk 131
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALAReLGPPGGGVIYIDGEDILEEVLDQLLLIIVGG------------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 132 dilvqkaieliglngfekaYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQMQ-----NELLRIQSQQKM 206
Cdd:smart00382 57 -------------------KKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelRLLLLLKSEKNL 117
|
170
....*....|....*...
gi 1956008863 207 TTVFITHDVEEAVTLADR 224
Cdd:smart00382 118 TVILTTNDEKDLGPALLR 135
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
50-228 |
2.50e-08 |
|
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: 54.63 E-value: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 50 IKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDG----ADVSGIGGDRAVVFQEHRLFPWLTVEQNIELGLLNEA 125
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGksilTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRG 2041
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 126 LTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQMQNELLRIQSQQK 205
Cdd:TIGR01257 2042 VPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGR 2121
|
170 180
....*....|....*....|...
gi 1956008863 206 mTTVFITHDVEEAVTLADRVVIL 228
Cdd:TIGR01257 2122 -AVVLTSHSMEECEALCTRLAIM 2143
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
34-187 |
2.54e-08 |
|
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: 52.63 E-value: 2.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 34 VVNQQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAG--LDQDFDGRILIDGADVsGIGGDRAVVFQEHR--LFP 109
Cdd:cd03232 14 PVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPL-DKNFQRSTGYVEQQdvHSP 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1956008863 110 WLTVEQNIELGLLNEALTSRDKdilvqkaieliglngfekayphqlsggmsQRVAIARSLVVQPRIFLLDEPFGALDA 187
Cdd:cd03232 93 NLTVREALRFSALLRGLSVEQR-----------------------------KRLTIGVELAAKPSILFLDEPTSGLDS 141
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
41-180 |
7.41e-08 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 53.21 E-value: 7.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 41 KVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDgadvsgiggdravvfQEHRLF-----PWLT--- 112
Cdd:TIGR00954 466 VLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKP---------------AKGKLFyvpqrPYMTlgt 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 113 ----------VEQNIELGLlnealtsRDKDIlvQKAIELIGLN-------GFE--KAYPHQLSGGMSQRVAIARSLVVQP 173
Cdd:TIGR00954 531 lrdqiiypdsSEDMKRRGL-------SDKDL--EQILDNVQLThileregGWSavQDWMDVLSGGEKQRIAMARLFYHKP 601
|
....*..
gi 1956008863 174 RIFLLDE 180
Cdd:TIGR00954 602 QFAILDE 608
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
24-228 |
8.84e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.06 E-value: 8.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 24 VAFHHVHKSFVVNQQPVkvIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIGGDR----- 98
Cdd:PLN03232 1235 IKFEDVHLRYRPGLPPV--LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDlrrvl 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 99 AVVFQEHRLFPWlTVEQNIE-------LGLLNEALTSRDKDILVQKAIeliGLNGFEKAYPHQLSGGMSQRVAIARSLVV 171
Cdd:PLN03232 1313 SIIPQSPVLFSG-TVRFNIDpfsehndADLWEALERAHIKDVIDRNPF---GLDAEVSEGGENFSVGQRQLLSLARALLR 1388
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1956008863 172 QPRIFLLDEPFGALDALTRHQMQNEllrIQSQQKMTTVFITHDVEEAVTLADRVVIL 228
Cdd:PLN03232 1389 RSKILVLDEATASVDVRTDSLIQRT---IREEFKSCTMLVIAHRLNTIIDCDKILVL 1442
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
21-218 |
9.18e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.71 E-value: 9.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 21 QTRVAFHHVHKSFvvNQQPVkvIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGlD--QDFDGRILIDGADV-SG---- 93
Cdd:PRK10938 258 EPRIVLNNGVVSY--NDRPI--LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DhpQGYSNDLTLFGRRRgSGetiw 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 94 -----IGGDRAVVFQEHRLFpwLTVEQNIELGLLN-----EALTSRDKdILVQKAIELIGLNGFEKAYP-HQLSGGMSQR 162
Cdd:PRK10938 333 dikkhIGYVSSSLHLDYRVS--TSVRNVILSGFFDsigiyQAVSDRQQ-KLAQQWLDILGIDKRTADAPfHSLSWGQQRL 409
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1956008863 163 VAIARSLVVQPRIFLLDEPFGALDALTRHQMQNELLRIQSQQKMTTVFITHDVEEA 218
Cdd:PRK10938 410 ALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
50-228 |
9.80e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.80 E-value: 9.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 50 IKEGEFIAIVGSSGCGKSTLLRLLAG-LDQ---DFDGRILIDGADVSGI----GGDRAVVFQEHRLFPWLTVEQNIELGL 121
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIASnTDGfhiGVEGVITYDGITPEEIkkhyRGDVVYNAETDVHFPHLTVGETLDFAA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 122 LNEALTSR----DKDILVQKAIELI----GL---------NGFEKAyphqLSGGMSQRVAIARSLVVQPRIFLLDEPFGA 184
Cdd:TIGR00956 164 RCKTPQNRpdgvSREEYAKHIADVYmatyGLshtrntkvgNDFVRG----VSGGERKRVSIAEASLGGAKIQCWDNATRG 239
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1956008863 185 LDALTRHQMQNeLLRIQSQQKMTTVFIT--HDVEEAVTLADRVVIL 228
Cdd:TIGR00956 240 LDSATALEFIR-ALKTSANILDTTPLVAiyQCSQDAYELFDKVIVL 284
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
43-217 |
1.60e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 51.36 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 43 IHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGaDVSGIGGDRAVVFQehrlfpwLTVEQNIELGLL 122
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-EVSVIAISAGLSGQ-------LTGIENIEFKML 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 123 NEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEpfgALDALTRHQMQNELLRIQS 202
Cdd:PRK13546 112 CMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDE---ALSVGDQTFAQKCLDKIYE 188
|
170
....*....|....*..
gi 1956008863 203 --QQKMTTVFITHDVEE 217
Cdd:PRK13546 189 fkEQNKTIFFVSHNLGQ 205
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
45-218 |
2.23e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 51.66 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 45 DFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSgiggDRAvvfqeHR-----------------L 107
Cdd:NF033858 19 DVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA----DAR-----HRravcpriaympqglgknL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 108 FPWLTVEQNIE----LGLLNEAltSRDKDILvqkaiELI---GLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDE 180
Cdd:NF033858 90 YPTLSVFENLDffgrLFGQDAA--ERRRRID-----ELLratGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDE 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1956008863 181 PFGALDALTRHQMQnELL-RIQSQQ-KMTTVFITHDVEEA 218
Cdd:NF033858 163 PTTGVDPLSRRQFW-ELIdRIRAERpGMSVLVATAYMEEA 201
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
24-214 |
2.23e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 51.47 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 24 VAFHHVHKSFVVNQqpvkVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIdGADVsgiggDRAVVFQ 103
Cdd:TIGR03719 323 IEAENLTKAFGDKL----LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV-----KLAYVDQ 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 104 EH-RLFPWLTVEQNIELGLlnealtsrdkDILVQKAIEL-----IGLNGFEKA----YPHQLSGGMSQRVAIARSLVVQP 173
Cdd:TIGR03719 393 SRdALDPNKTVWEEISGGL----------DIIKLGKREIpsrayVGRFNFKGSdqqkKVGQLSGGERNRVHLAKTLKSGG 462
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1956008863 174 RIFLLDEPFGALDALTRHQMQNELLRIQSqqkmTTVFITHD 214
Cdd:TIGR03719 463 NVLLLDEPTNDLDVETLRALEEALLNFAG----CAVVISHD 499
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
35-234 |
3.15e-07 |
|
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: 49.24 E-value: 3.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 35 VNQQPVKVIHDFNLEIKEGEFIAIVGSSGCGKSTLLrlLAGLDQDFDGRIlidgADVSGIGGDRAVVF--QEHRLfpwlt 112
Cdd:cd03238 3 VSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLV--NEGLYASGKARL----ISFLPKFSRNKLIFidQLQFL----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 113 veqnIELGL----LNEALTSrdkdilvqkaieliglngfekayphqLSGGMSQRVAIARSLVVQPR--IFLLDEPFGALD 186
Cdd:cd03238 72 ----IDVGLgyltLGQKLST--------------------------LSGGELQRVKLASELFSEPPgtLFILDEPSTGLH 121
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1956008863 187 ALTRHQMQNELLRIQsQQKMTTVFITHDvEEAVTLADRVVILKPKPGR 234
Cdd:cd03238 122 QQDINQLLEVIKGLI-DLGNTVILIEHN-LDVLSSADWIIDFGPGSGK 167
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
43-239 |
3.33e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.88 E-value: 3.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 43 IHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVS------GIGGDRAVVFQEHR---LFPWLTV 113
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINnhnaneAINHGFALVTEERRstgIYAYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 114 E-----QNIE-----LGLLNEALTSRDkdilVQKAIELIGLngfeKAYPHQ-----LSGGMSQRVAIARSLVVQPRIFLL 178
Cdd:PRK10982 344 GfnsliSNIRnyknkVGLLDNSRMKSD----TQWVIDSMRV----KTPGHRtqigsLSGGNQQKVIIGRWLLTQPEILML 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1956008863 179 DEPFGALDALTRHQMQNELLRIQSQQKmTTVFITHDVEEAVTLADRVVILkpKPGRVEQII 239
Cdd:PRK10982 416 DEPTRGIDVGAKFEIYQLIAELAKKDK-GIIIISSEMPELLGITDRILVM--SNGLVAGIV 473
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
42-216 |
8.84e-07 |
|
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: 49.08 E-value: 8.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 42 VIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLdQDFDGRILIDGADVSgiggdrAVVFQEHR-LFPWLTVEQNIELG 120
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGVSWN------SVPLQKWRkAFGVIPQKVFIFSG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 121 LLNEALTSRDK--DILVQKAIELIGLNGFEKAYPHQL-----------SGGMSQRVAIARSLVVQPRIFLLDEPFGALDA 187
Cdd:cd03289 92 TFRKNLDPYGKwsDEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP 171
|
170 180
....*....|....*....|....*....
gi 1956008863 188 LTrHQMQNELLRiQSQQKMTTVFITHDVE 216
Cdd:cd03289 172 IT-YQVIRKTLK-QAFADCTVILSEHRIE 198
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
40-235 |
1.60e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 48.58 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 40 VKVIHDFNLEIKEGEFIAIVGSSGCG--KSTLLRLLAGLDQD-----FDGRILIDGADVSGIGGDRAVVFQEHRLFpwlT 112
Cdd:NF000106 26 VKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGrrpwrF*TWCANRRALRRTIG*HRPVR*GRRESF---S 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 113 VEQNIELGLLNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQ 192
Cdd:NF000106 103 GRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNE 182
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1956008863 193 MQNElLRIQSQQKMTTVFITHDVEEAVTLADRVVILkpKPGRV 235
Cdd:NF000106 183 VWDE-VRSMVRDGATVLLTTQYMEEAEQLAHELTVI--DRGRV 222
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
41-213 |
1.94e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 47.71 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 41 KVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLD--QDFDGRILIDGADVSGIGGD-RAvvfqehRLFPWLTVEQNI 117
Cdd:CHL00131 21 EILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEeRA------HLGIFLAFQYPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 118 EL-GLLNE-----ALTSRDK-------------DILVQKaIELIGLN----------GFekayphqlSGGMSQRVAIARS 168
Cdd:CHL00131 95 EIpGVSNAdflrlAYNSKRKfqglpeldpleflEIINEK-LKLVGMDpsflsrnvneGF--------SGGEKKRNEILQM 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1956008863 169 LVVQPRIFLLDEPFGALDALTRHQMQNELLRIQSQQKmTTVFITH 213
Cdd:CHL00131 166 ALLDSELAILDETDSGLDIDALKIIAEGINKLMTSEN-SIILITH 209
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
42-252 |
2.00e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.97 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 42 VIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIDGADVSGIG-----GDRAVVFQEHRLFPWlTVEQN 116
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGlmdlrKVLGIIPQAPVLFSG-TVRFN 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 117 IEL------GLLNEALT-SRDKDILVQKAielIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALT 189
Cdd:PLN03130 1333 LDPfnehndADLWESLErAHLKDVIRRNS---LGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRT 1409
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1956008863 190 RHQMQNEllrIQSQQKMTTVFITHDVEEAVTLADRVVILkpKPGRV-EQIIPVNLpRPRNRSSF 252
Cdd:PLN03130 1410 DALIQKT---IREEFKSCTMLIIAHRLNTIIDCDRILVL--DAGRVvEFDTPENL-LSNEGSAF 1467
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
41-220 |
2.36e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.41 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 41 KVIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIdgadvsgigGDRAVV--FQEHR--LFPWLTVEQN 116
Cdd:PRK11147 333 QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC---------GTKLEVayFDQHRaeLDPEKTVMDN 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 117 IELGLLNEALTSRDKDILVQkaieligLNGF----------EKAyphqLSGGMSQRVAIARSLVVQPRIFLLDEPFGALD 186
Cdd:PRK11147 404 LAEGKQEVMVNGRPRHVLGY-------LQDFlfhpkramtpVKA----LSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
|
170 180 190
....*....|....*....|....*....|....*....
gi 1956008863 187 ALTRhqmqnELLR--IQSQQKmTTVFITHD---VEEAVT 220
Cdd:PRK11147 473 VETL-----ELLEelLDSYQG-TVLLVSHDrqfVDNTVT 505
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
45-234 |
4.55e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 46.48 E-value: 4.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 45 DFNLEIKEGEFIAIVGSSGCGKSTL----------LRLLAGLDQDFDGRI-LIDGADVSGIGGDRAVVFQEHRLF---PW 110
Cdd:cd03270 13 NVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqRRYVESLSAYARQFLgQMDKPDVDSIEGLSPAIAIDQKTTsrnPR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 111 LTV----EQNIELGLL--NEALTSRdKDILVQKAIELIGLngfEKAYPhQLSGGMSQRVAIARSL------VvqprIFLL 178
Cdd:cd03270 93 STVgtvtEIYDYLRLLfaRVGIRER-LGFLVDVGLGYLTL---SRSAP-TLSGGEAQRIRLATQIgsgltgV----LYVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1956008863 179 DEPFGALdaltrHQMQNELLrIQSQQKM-----TTVFITHDvEEAVTLADRVVILKPKPGR 234
Cdd:cd03270 164 DEPSIGL-----HPRDNDRL-IETLKRLrdlgnTVLVVEHD-EDTIRAADHVIDIGPGAGV 217
|
|
| PRK15177 |
PRK15177 |
Vi polysaccharide ABC transporter ATP-binding protein VexC; |
54-214 |
4.88e-06 |
|
Vi polysaccharide ABC transporter ATP-binding protein VexC;
Pssm-ID: 185099 [Multi-domain] Cd Length: 213 Bit Score: 46.21 E-value: 4.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 54 EFIAIVGSSGCGKSTLLRLLAGLDQDfdgriliDGADVSGIGGDRAVVFQEHRLFPWLTVEQNIElglLNEALTSRDKDI 133
Cdd:PRK15177 14 EHIGILAAPGSGKTTLTRLLCGLDAP-------DEGDFIGLRGDALPLGANSFILPGLTGEENAR---MMASLYGLDGDE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 134 LVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQMQnELLRIQSQQKMTTVfITH 213
Cdd:PRK15177 84 FSHFCYQLTQLEQCYTDRVSEYSVTMKTHLAFAINLLLPCRLYIADGKLYTGDNATQLRMQ-AALACQLQQKGLIV-LTH 161
|
.
gi 1956008863 214 D 214
Cdd:PRK15177 162 N 162
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
53-187 |
7.31e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.15 E-value: 7.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 53 GEFIAIVGSSGCGKSTLLRLLAGLDQD--FDGRILIDG--------ADVSGiggdraVVFQEHRLFPWLTVEQNIELGL- 121
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGRKTGgyIEGDIRISGfpkkqetfARISG------YCEQNDIHSPQVTVRESLIYSAf 979
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1956008863 122 --LNEALTSRDKDILVQKAIELIGLNGFEKA---YP--HQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALDA 187
Cdd:PLN03140 980 lrLPKEVSKEEKMMFVDEVMELVELDNLKDAivgLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA 1052
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
56-186 |
1.01e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.39 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 56 IAIVGSSGCGKSTLLRLLAGLDQDFDGRILiDGADVsgiggdRAVVFQEHRLfPWLTVEQNIEL-------GLLNEALTS 128
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTVF-RSAKV------RMAVFSQHHV-DGLDLSSNPLLymmrcfpGVPEQKLRA 609
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1956008863 129 RdkdilvqkaIELIGLNGFEKAYP-HQLSGGMSQRVAIARSLVVQPRIFLLDEPFGALD 186
Cdd:PLN03073 610 H---------LGSFGVTGNLALQPmYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
153-230 |
1.50e-05 |
|
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: 44.27 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 153 HQLSGGMSQRVAIA---RSLVVQPRIF-LLDEPFGALDALTRHQMQNELLRiQSQQKMTTVFITHDvEEAVTLADRVVIL 228
Cdd:cd03227 76 LQLSGGEKELSALAlilALASLKPRPLyILDEIDRGLDPRDGQALAEAILE-HLVKGAQVIVITHL-PELAELADKLIHI 153
|
..
gi 1956008863 229 KP 230
Cdd:cd03227 154 KK 155
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
50-189 |
1.80e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.87 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 50 IKEGEFIAIVGSSGCGKSTLLRLLAgldQDFDGRILIDGADVSGiGGDRAVVFQEHRLFpwltVEQN---IELGLLNEAL 126
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLLNVLA---ERVTTGVITGGDRLVN-GRPLDSSFQRSIGY----VQQQdlhLPTSTVRESL 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 127 ------------TSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMS----QRVAIARSLVVQPRIFL-LDEPFGALDALT 189
Cdd:TIGR00956 858 rfsaylrqpksvSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGLNveqrKRLTIGVELVAKPKLLLfLDEPTSGLDSQT 937
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
46-233 |
1.19e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 43.26 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 46 FNLEI-KEGEFIAIVGSSGCGKSTLLRLLAG------------------LDQdFDGRILIDG-ADVSGiGGDRAVvfqeH 105
Cdd:PRK13409 91 YGLPIpKEGKVTGILGPNGIGKTTAVKILSGelipnlgdyeeepswdevLKR-FRGTELQNYfKKLYN-GEIKVV----H 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 106 RLfpwltveQNIEL------GLLNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLD 179
Cdd:PRK13409 165 KP-------QYVDLipkvfkGKVRELLKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1956008863 180 EPFGALDALTRHQMQNeLLRIQSQQKmTTVFITHDVeeAVT--LADRVVILKPKPG 233
Cdd:PRK13409 238 EPTSYLDIRQRLNVAR-LIRELAEGK-YVLVVEHDL--AVLdyLADNVHIAYGEPG 289
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
46-233 |
1.27e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 42.85 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 46 FNLEI-KEGEFIAIVGSSGCGKSTLLRLLAGLDQ----DFDGrilidgadvsgiGGDRAVVFQEHR---LFPWLT--VE- 114
Cdd:COG1245 91 YGLPVpKKGKVTGILGPNGIGKSTALKILSGELKpnlgDYDE------------EPSWDEVLKRFRgteLQDYFKklANg 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 115 --------QNIEL------GLLNEALTSRDKDILVQKAIELIGLNGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDE 180
Cdd:COG1245 159 eikvahkpQYVDLipkvfkGTVRELLEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1956008863 181 PFGALDALTRHQMQnELLRIQSQQKMTTVFITHDVeeAV--TLADRVVILKPKPG 233
Cdd:COG1245 239 PSSYLDIYQRLNVA-RLIRELAEEGKYVLVVEHDL--AIldYLADYVHILYGEPG 290
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
57-226 |
1.81e-04 |
|
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: 41.44 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 57 AIVGSSGCGKSTLLR-LLAGL--DQDFDGRILIDGADVSGIGGDRAVVFQEHRLFPWLTVEQNIELGLLNEALTSRDKDI 133
Cdd:cd03240 26 LIVGQNGAGKTTIIEaLKYALtgELPPNSKGGAHDPKLIREGEVRAQVKLAFENANGKKYTITRSLAILENVIFCHQGES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 134 LVQKAIELIGLNGFEKAyphqlSGGMSQRVAIARSLVVQPRIFLLDEPFGALDALTRHQMQNELLRIQSQQK-MTTVFIT 212
Cdd:cd03240 106 NWPLLDMRGRCSGGEKV-----LASLIIRLALAETFGSNCGILALDEPTTNLDEENIEESLAEIIEERKSQKnFQLIVIT 180
|
170
....*....|....
gi 1956008863 213 HDvEEAVTLADRVV 226
Cdd:cd03240 181 HD-EELVDAADHIY 193
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
24-186 |
2.37e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.03 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 24 VAFHHVHKSF---VVnqqpvkvIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLDQDFDGRILIdGADVsgiggDRAV 100
Cdd:PRK11819 325 IEAENLSKSFgdrLL-------IDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV-----KLAY 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 101 VFQEH-RLFPWLTVEQNIELGLlnealtsrdkdilvqkaiELIGLNGFE---KAY--------PHQ------LSGGMSQR 162
Cdd:PRK11819 392 VDQSRdALDPNKTVWEEISGGL------------------DIIKVGNREipsRAYvgrfnfkgGDQqkkvgvLSGGERNR 453
|
170 180
....*....|....*....|....
gi 1956008863 163 VAIARSLVVQPRIFLLDEPFGALD 186
Cdd:PRK11819 454 LHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
42-186 |
4.59e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 40.54 E-value: 4.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 42 VIHDFNLEIKEGEFIAIVGSSGCGKSTLLRLLAGLD--QDFDGRILIDGADVSGIG-GDRA-----VVFQEHRLFPWLTV 113
Cdd:PRK09580 16 ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSpEDRAgegifMAFQYPVEIPGVSN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 114 EQNIELGlLNEALTSRDKDIL--------VQKAIELIGL--NGFEKAYPHQLSGGMSQRVAIARSLVVQPRIFLLDEPFG 183
Cdd:PRK09580 96 QFFLQTA-LNAVRSYRGQEPLdrfdfqdlMEEKIALLKMpeDLLTRSVNVGFSGGEKKRNDILQMAVLEPELCILDESDS 174
|
...
gi 1956008863 184 ALD 186
Cdd:PRK09580 175 GLD 177
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
154-186 |
8.10e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.61 E-value: 8.10e-04
10 20 30
....*....|....*....|....*....|...
gi 1956008863 154 QLSGGMSQRVAIARSLVVQPRIFLLDEPFGALD 186
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
155-264 |
8.87e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.58 E-value: 8.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 155 LSGGMSQRVAIARSLVVQPR--IFLLDEPFGALDALTRHQMQNELLRIQSQQKmTTVFITHDvEEAVTLADRVVILKPKP 232
Cdd:PRK00635 477 LSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGN-TVLLVEHD-EQMISLADRIIDIGPGA 554
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1956008863 233 G---------------------------RVEQIIPVNLPRPRNRSSFEL-----HQLKEQIFRI 264
Cdd:PRK00635 555 GifggevlfngspreflaksdsltakylRQELTIPIPEKRTNSLGTLTLskatkHNLKDLTISL 618
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
50-81 |
1.48e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 39.00 E-value: 1.48e-03
10 20 30
....*....|....*....|....*....|....
gi 1956008863 50 IKEGE-FIAIVGSSGCGKSTLLR-LLAGLDQDFD 81
Cdd:COG3267 39 LAQGGgFVVLTGEVGTGKTTLLRrLLERLPDDVK 72
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
155-234 |
1.82e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 39.61 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 155 LSGGMSQRVAIARSL------VvqprIFLLDEPFGALdaltrHQMQNE-----LLRIQSQQKmTTVFITHDvEEAVTLAD 223
Cdd:TIGR00630 489 LSGGEAQRIRLATQIgsgltgV----LYVLDEPSIGL-----HQRDNRrlintLKRLRDLGN-TLIVVEHD-EDTIRAAD 557
|
90
....*....|.
gi 1956008863 224 RVVILKPKPGR 234
Cdd:TIGR00630 558 YVIDIGPGAGE 568
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
56-214 |
2.48e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 38.07 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 56 IAIVGSSGCGKSTLLRLL-------AGLDQDFDGRILIDGADVSGI------GGDRAVV------FQEHRLFPWLTVEQN 116
Cdd:COG0419 26 NLIVGPNGAGKSTILEAIryalygkARSRSKLRSDLINVGSEEASVelefehGGKRYRIerrqgeFAEFLEAKPSERKEA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 117 IE--LGL------------LNEALTSRDKDILVQKAIE---LIGLNGFEKayPHQLSGGMSQRVAIARSLvvqpRIFlLD 179
Cdd:COG0419 106 LKrlLGLeiyeelkerlkeLEEALESALEELAELQKLKqeiLAQLSGLDP--IETLSGGERLRLALADLL----SLI-LD 178
|
170 180 190
....*....|....*....|....*....|....*
gi 1956008863 180 epFGALDALTRHQMQNELLRIQsqqkmttvFITHD 214
Cdd:COG0419 179 --FGSLDEERLERLLDALEELA--------IITHV 203
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
47-214 |
3.22e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 38.72 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 47 NLEIK--EGEFIAIVGSSGCGKSTLLRLLAG-------------------LDQD---FDGRILIDGAdvsgIGGDRAV-- 100
Cdd:PRK15064 19 NISVKfgGGNRYGLIGANGCGKSTFMKILGGdlepsagnvsldpnerlgkLRQDqfaFEEFTVLDTV----IMGHTELwe 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956008863 101 VFQEH-RLF--PWLTVEQNIELGLLNEALT--------SRDKDILVQKAIELiglngfekaypHQLSGGMSQ-------R 162
Cdd:PRK15064 95 VKQERdRIYalPEMSEEDGMKVADLEVKFAemdgytaeARAGELLLGVGIPE-----------EQHYGLMSEvapgwklR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1956008863 163 VAIARSLVVQPRIFLLDEPFGALDALTRHQMQNELlriqSQQKMTTVFITHD 214
Cdd:PRK15064 164 VLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVL----NERNSTMIIISHD 211
|
|
| |
