|
Name |
Accession |
Description |
Interval |
E-value |
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-262 |
2.87e-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: 392.53 E-value: 2.87e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 1 MEKALLDLTRLGMRFPTPDGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDR 80
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 81 AVVFQNHSLLPWLTVYQNVELAVKqiAGKKGKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVL 160
Cdd:COG1116 83 GVVFQEPALLPWLTVLDNVALGLE--LRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 161 LMDEPFGALDALTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPaATIGEVLEVNLPRPRERvALADD 240
Cdd:COG1116 161 LMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSARP-GRIVEEIDVDLPRPRDR-ELRTS 238
|
250 260
....*....|....*....|..
gi 491592515 241 AQYQKCRQAVLKFLYEKQSKVE 262
Cdd:COG1116 239 PEFAALRAEILDLLREEAERAA 260
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
25-254 |
4.81e-121 |
|
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: 345.22 E-value: 4.81e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDRAVVFQNHSLLPWLTVYQNVELAVK 104
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVFQNYSLLPWLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 105 QIAGKKGKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHLQDALMKI 184
Cdd:TIGR01184 81 RVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 185 QAELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIGEVLEVNLPRPRERVALADDAQYQKCRQAVLKFL 254
Cdd:TIGR01184 161 WEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVPFPRPRDRLEVVEDPSYYDLRNEALYFL 230
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-228 |
3.33e-112 |
|
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: 322.50 E-value: 3.33e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 6 LDLTRLGMRFPTPDGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDRAVVFQ 85
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 86 NHSLLPWLTVYQNVELAVKqIAGKKGKAwIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEP 165
Cdd:cd03293 81 QDALLPWLTVLDNVALGLE-LQGVPKAE-ARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491592515 166 FGALDALTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPaATIGEVLEVNL 228
Cdd:cd03293 159 FSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSARP-GRIVAEVEVDL 220
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-258 |
6.60e-90 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 267.50 E-value: 6.60e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 4 ALLDLTRLGMRFPTPDGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDRAVV 83
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADRGVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 84 FQNHSLLPWLTVYQNVELAVKqIAGKkGKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMD 163
Cdd:COG4525 82 FQKDALLPWLNVLDNVAFGLR-LRGV-PKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 164 EPFGALDALTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPaATIGEVLEvnLPRPRERVALAD---- 239
Cdd:COG4525 160 EPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPGP-GRIVERLE--LDFSRRFLAGEDarai 236
|
250 260
....*....|....*....|.
gi 491592515 240 --DAQYQKCRQAVLKFLYEKQ 258
Cdd:COG4525 237 ksDPAFIALREELLDIIFAQE 257
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-215 |
3.58e-83 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 253.48 E-value: 3.58e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 1 MEKALLDLTRLGMRFptpdGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDR 80
Cdd:COG3842 1 MAMPALELENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 81 ---AVVFQNHSLLPWLTVYQNVE--LAVKqiagKKGKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALAL 155
Cdd:COG3842 77 rnvGMVFQDYALFPHLTVAENVAfgLRMR----GVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 156 QPKVLLMDEPFGALDALTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:COG3842 153 EPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDG 212
|
|
| ABC_ATP_SaoA |
NF040729 |
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC ... |
25-254 |
8.57e-76 |
|
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: 231.17 E-value: 8.57e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDRAVVFQNHSLLPWLTVYQNVELAVK 104
Cdd:NF040729 21 LKDISFDVEEGEFVSLLGPSGCGKTTLLTIIAGFQNATSGEILVNGNEVTKPGPDRGFVFQNYALFPWMTVKENIEYPMK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 105 QIagKKGKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHLQDALMKI 184
Cdd:NF040729 101 QQ--KMPKQEREKRLNELLEMAQLTGKENLYPHQISGGMKQRTAVIRALACKPEVLLMDEPLGAVDFQMRQILQEELESI 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491592515 185 QAELNNTVIMITHDVDEAVLLSDK-IVMMTNGpaATIGEVLEVNLPRPRERvalaDDAQYQKCRQAVLKFL 254
Cdd:NF040729 179 WLKDKTTVLMVTHDVDEAVYLSDRvIVMSRDK--GKILEDLKIDLPRPRNR----ESEKYLEYKDHLTNIL 243
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
20-221 |
2.69e-75 |
|
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: 228.56 E-value: 2.69e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 20 GEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDR---AVVFQNHSLLPWLTVY 96
Cdd:cd03259 11 GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERrniGMVFQDYALFPHLTVA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 97 QNVELAVKqiAGKKGKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAH 176
Cdd:cd03259 91 ENIAFGLK--LRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREE 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 491592515 177 LQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIG 221
Cdd:cd03259 169 LREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
20-221 |
5.98e-72 |
|
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: 220.57 E-value: 5.98e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 20 GEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAG-PGPDRAV--VFQNHSLLPWLTVY 96
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNlPPHKRPVntVFQNYALFPHLTVF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 97 QNVELAVKQiaGKKGKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAH 176
Cdd:cd03300 91 ENIAFGLRL--KKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 491592515 177 LQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIG 221
Cdd:cd03300 169 MQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIG 213
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-215 |
4.40e-71 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 218.37 E-value: 4.40e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 1 MEkALLDLTRLGMRFPTPDGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAG-PGPD 79
Cdd:COG1136 1 MS-PLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSlSERE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 80 RAV--------VFQNHSLLPWLTVYQNVELAVkQIAGKKGKAwIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIAR 151
Cdd:COG1136 80 LARlrrrhigfVFQFFNLLPELTALENVALPL-LLAGVSRKE-RRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491592515 152 ALALQPKVLLMDEPFGALDALTRAHLQDALMKIQAELNNTVIMITHDvDEAVLLSDKIVMMTNG 215
Cdd:COG1136 158 ALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRLRDG 220
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-215 |
2.26e-70 |
|
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: 216.20 E-value: 2.26e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 6 LDLTRLGMRFPTPDGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDR----- 80
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKElaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 81 ----AVVFQNHSLLPWLTVYQNVELAVkQIAGKKGKAWIqEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQ 156
Cdd:cd03255 81 rrhiGFVFQSFNLLPDLTALENVELPL-LLAGVPKKERR-ERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491592515 157 PKVLLMDEPFGALDALTRAHLQDALMKIQAELNNTVIMITHDvDEAVLLSDKIVMMTNG 215
Cdd:cd03255 159 PKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHD-PELAEYADRIIELRDG 216
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
4-215 |
8.76e-70 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 219.17 E-value: 8.76e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 4 ALLDLTRLGMRFptpdGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGP-DR-- 80
Cdd:COG3839 2 ASLELENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPkDRni 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 81 AVVFQNHSLLPWLTVYQNVELAVKqIAGKKgKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVL 160
Cdd:COG3839 78 AMVFQSYALYPHMTVYENIAFPLK-LRKVP-KAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVF 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491592515 161 LMDEPFGALDALTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:COG3839 156 LLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDG 210
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
19-215 |
3.95e-69 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 216.11 E-value: 3.95e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 19 DGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPD---RAV--VFQNHSLLPWL 93
Cdd:COG1125 12 PDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVelrRRIgyVIQQIGLFPHM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 94 TVYQNVELaVKQIAGKKgKAWIQEQVNHYLELIQMQHA--AHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDA 171
Cdd:COG1125 92 TVAENIAT-VPRLLGWD-KERIRARVDELLELVGLDPEeyRDRYPHELSGGQQQRVGVARALAADPPILLMDEPFGALDP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491592515 172 LTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:COG1125 170 ITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREG 213
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
20-226 |
1.20e-67 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 213.47 E-value: 1.20e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 20 GEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAG--PGPDRAV--VFQNHSLLPWLTV 95
Cdd:COG1118 13 GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTnlPPRERRVgfVFQHYALFPHMTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 96 YQNVELAVKqiAGKKGKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRA 175
Cdd:COG1118 93 AENIAFGLR--VRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRK 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491592515 176 HLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIGEVLEV 226
Cdd:COG1118 171 ELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
6-226 |
7.01e-67 |
|
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: 211.82 E-value: 7.01e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 6 LDLTRLGMRFptpdGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGP---DRAV 82
Cdd:TIGR03265 5 LSIDNIRKRF----GAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPqkrDYGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 83 VFQNHSLLPWLTVYQNVELAVKQIagKKGKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLM 162
Cdd:TIGR03265 81 VFQSYALFPNLTVADNIAYGLKNR--GMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491592515 163 DEPFGALDALTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIGEVLEV 226
Cdd:TIGR03265 159 DEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEI 222
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-215 |
1.49e-65 |
|
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: 204.44 E-value: 1.49e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 1 MEKALLDLTRLGMRFptpdGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDR 80
Cdd:COG1127 1 MSEPMIEVRNLTKSF----GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 81 --------AVVFQNHSLLPWLTVYQNVELAVKQiAGKKGKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARA 152
Cdd:COG1127 77 lyelrrriGMLFQGGALFDSLTVFENVAFPLRE-HTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491592515 153 LALQPKVLLMDEPFGALDALTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:COG1127 156 LALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADG 218
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
5-225 |
3.53e-65 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 204.16 E-value: 3.53e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 5 LLDLTRLGMRFP-TPdgefiALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDRAVV 83
Cdd:PRK11248 1 MLQISHLYADYGgKP-----ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 84 FQNHSLLPWLTVYQNVELAVkQIAGKkGKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMD 163
Cdd:PRK11248 76 FQNEGLLPWRNVQDNVAFGL-QLAGV-EKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLD 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491592515 164 EPFGALDALTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPaatiGEVLE 225
Cdd:PRK11248 154 EPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPGP----GRVVE 211
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
20-226 |
4.38e-65 |
|
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: 203.69 E-value: 4.38e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 20 GEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDR-----AVVFQNHSLLPWLT 94
Cdd:cd03295 12 GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrrkiGYVIQQIGLFPHMT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 95 VYQNVELAVKQIagKKGKAWIQEQVNHYLELIQM--QHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDAL 172
Cdd:cd03295 92 VEENIALVPKLL--KWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPI 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491592515 173 TRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIGEVLEV 226
Cdd:cd03295 170 TRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
20-226 |
3.33e-64 |
|
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: 201.03 E-value: 3.33e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 20 GEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGP-DRAV--VFQNHSLLPWLTVY 96
Cdd:cd03296 13 GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVqERNVgfVFQHYALFRHMTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 97 QNVE--LAVKQIAGKKGKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTR 174
Cdd:cd03296 93 DNVAfgLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVR 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491592515 175 AHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIGEVLEV 226
Cdd:cd03296 173 KELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
20-215 |
4.01e-64 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 205.72 E-value: 4.01e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 20 GEFIALKNVDLQINKGE-FVsLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDR---------AVVFQNHSL 89
Cdd:COG4175 38 GQTVGVNDASFDVEEGEiFV-IMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKElrelrrkkmSMVFQHFAL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 90 LPWLTVYQNVELAVKqIAGKkGKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGAL 169
Cdd:COG4175 117 LPHRTVLENVAFGLE-IQGV-PKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSAL 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491592515 170 DALTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:COG4175 195 DPLIRREMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIMKDG 240
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-233 |
1.54e-63 |
|
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: 207.45 E-value: 1.54e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 1 MEKALLDLTRLGMRFPT-PDGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPD 79
Cdd:COG1123 256 AAEPLLEVRNLSKRYPVrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 80 R--------AVVFQN--HSLLPWLTVYQNVELAVKqIAGKKGKAWIQEQVNHYLELIQMQ-HAAHKKPDEISGGMKQRVG 148
Cdd:COG1123 336 SlrelrrrvQMVFQDpySSLNPRMTVGDIIAEPLR-LHGLLSRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVA 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 149 IARALALQPKVLLMDEPFGALDALTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIGEVLEVnL 228
Cdd:COG1123 415 IARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEV-F 493
|
....*
gi 491592515 229 PRPRE 233
Cdd:COG1123 494 ANPQH 498
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
20-221 |
1.61e-63 |
|
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: 198.63 E-value: 1.61e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 20 GEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGP-DR--AVVFQNHSLLPWLTVY 96
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPkDRdiAMVFQNYALYPHMTVY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 97 QNVELAVKQiaGKKGKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAH 176
Cdd:cd03301 91 DNIAFGLKL--RKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQ 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 491592515 177 LQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIG 221
Cdd:cd03301 169 MRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
20-221 |
9.48e-61 |
|
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: 193.24 E-value: 9.48e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 20 GEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDR---------AVVFQNHSLL 90
Cdd:cd03294 35 GQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrkkiSMVFQSFALL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 91 PWLTVYQNVELAVkQIAGKkGKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALD 170
Cdd:cd03294 115 PHRTVLENVAFGL-EVQGV-PRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491592515 171 ALTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIG 221
Cdd:cd03294 193 PLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVG 243
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
15-226 |
2.30e-60 |
|
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: 191.26 E-value: 2.30e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 15 FPTPDGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDR--------AVVFQN 86
Cdd:cd03258 11 FGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrkarrriGMIFQH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 87 HSLLPWLTVYQNVELAVkQIAGKKgKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPF 166
Cdd:cd03258 91 FNLLSSRTVFENVALPL-EIAGVP-KAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 167 GALDALTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIGEVLEV 226
Cdd:cd03258 169 SALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-215 |
3.00e-60 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 190.79 E-value: 3.00e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 5 LLDLTRLGMRFPTPDGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDR---- 80
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 81 ----AVVFQN--HSLLPWLTVYQNVELAVkQIAGKKGKAWIQEQVNhYLELIQMQHA---AHKKPDEISGGMKQRVGIAR 151
Cdd:cd03257 81 rkeiQMVFQDpmSSLNPRMTIGEQIAEPL-RIHGKLSKKEARKEAV-LLLLVGVGLPeevLNRYPHELSGGQRQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491592515 152 ALALQPKVLLMDEPFGALDALTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAG 222
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-221 |
4.90e-60 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 194.78 E-value: 4.90e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 1 MEKALLDLTRLGMRFptpdGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAG-PGPD 79
Cdd:PRK09452 10 SLSPLVELRGISKSF----DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHvPAEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 80 RAV--VFQNHSLLPWLTVYQNVELAVKQiaGKKGKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQP 157
Cdd:PRK09452 86 RHVntVFQSYALFPHMTVFENVAFGLRM--QKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491592515 158 KVLLMDEPFGALDALTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIG 221
Cdd:PRK09452 164 KVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDG 227
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
20-215 |
1.41e-59 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 189.25 E-value: 1.41e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 20 GEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDR--------AVVFQNHSLLP 91
Cdd:cd03261 11 GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrrrmGMLFQSGALFD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 92 WLTVYQNVELAVKQiAGKKGKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDA 171
Cdd:cd03261 91 SLTVFENVAFPLRE-HTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491592515 172 LTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:cd03261 170 IASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDG 213
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
20-215 |
5.16e-59 |
|
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: 185.85 E-value: 5.16e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 20 GEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDR-------AVVFQNHSLLPW 92
Cdd:cd03229 11 GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELpplrrriGMVFQDFALFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 93 LTVYQNVELAvkqiagkkgkawiqeqvnhyleliqmqhaahkkpdeISGGMKQRVGIARALALQPKVLLMDEPFGALDAL 172
Cdd:cd03229 91 LTVLENIALG------------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPI 134
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 491592515 173 TRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:cd03229 135 TRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
20-226 |
1.47e-58 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 186.54 E-value: 1.47e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 20 GEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAG-PGPDRAV--VFQNHSLLPWLTVY 96
Cdd:TIGR00968 11 GSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRvHARDRKIgfVFQHYALFKHLTVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 97 QNVELAVKqiAGKKGKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAH 176
Cdd:TIGR00968 91 DNIAFGLE--IRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGALDAKVRKE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491592515 177 LQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIGEVLEV 226
Cdd:TIGR00968 169 LRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEV 218
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
14-236 |
2.15e-58 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 189.52 E-value: 2.15e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 14 RFPTPDGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDR--------AVVFQ 85
Cdd:COG1135 10 TFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElraarrkiGMIFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 86 NHSLLPWLTVYQNVELAVKqIAGKKgKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEP 165
Cdd:COG1135 90 HFNLLSSRTVAENVALPLE-IAGVP-KAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491592515 166 FGALDALTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIGEVLEVnLPRPRERVA 236
Cdd:COG1135 168 TSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDV-FANPQSELT 237
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
20-236 |
6.67e-58 |
|
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: 184.85 E-value: 6.67e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 20 GEFiALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDR---AVVFQNHSLLPWLTVY 96
Cdd:cd03299 11 KEF-KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKrdiSYVPQNYALFPHMTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 97 QNVELAVKQIAGKKGKawIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAH 176
Cdd:cd03299 90 KNIAYGLKKRKVDKKE--IERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEK 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491592515 177 LQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIGEVLEVnLPRPR-ERVA 236
Cdd:cd03299 168 LREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEV-FKKPKnEFVA 227
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
20-221 |
5.84e-56 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes 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 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. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 183.90 E-value: 5.84e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 20 GEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDR---------AVVFQNHSLL 90
Cdd:TIGR01186 4 GGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVElrevrrkkiGMVFQQFALF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 91 PWLTVYQNVELAVKQIAGKKGKAwiQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALD 170
Cdd:TIGR01186 84 PHMTILQNTSLGPELLGWPEQER--KEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491592515 171 ALTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIG 221
Cdd:TIGR01186 162 PLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVG 212
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
19-200 |
7.12e-56 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 179.09 E-value: 7.12e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 19 DGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDR--------AVVFQNHSLL 90
Cdd:COG2884 12 PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrrriGVVFQDFRLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 91 PWLTVYQNVELAVkQIAGKKGKAwIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALD 170
Cdd:COG2884 92 PDRTVYENVALPL-RVTGKSRKE-IRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLD 169
|
170 180 190
....*....|....*....|....*....|...
gi 491592515 171 ALTRahlqDALMKIQAELNN---TVIMITHDVD 200
Cdd:COG2884 170 PETS----WEIMELLEEINRrgtTVLIATHDLE 198
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
20-215 |
1.42e-55 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 179.10 E-value: 1.42e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 20 GEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPD-RA---VVFQNHSLLPWLTV 95
Cdd:COG1131 11 GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEvRRrigYVPQEPALYPDLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 96 YQNVELaVKQIAGKKGKAwIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRA 175
Cdd:COG1131 91 RENLRF-FARLYGLPRKE-ARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARR 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 491592515 176 HLQDALMKIQAElNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:COG1131 169 ELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKG 207
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
19-215 |
1.75e-55 |
|
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: 178.29 E-value: 1.75e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 19 DGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDRA-----VVFQNhsllPWL 93
Cdd:COG1122 11 PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELrrkvgLVFQN----PDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 94 -----TVYQNVELAVKQIagKKGKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGA 168
Cdd:COG1122 87 qlfapTVEEDVAFGPENL--GLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAG 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491592515 169 LDALTRAHLQDALMKIQAElNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:COG1122 165 LDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDG 210
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
20-234 |
3.32e-55 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 178.72 E-value: 3.32e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 20 GEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIvdgrevAGPGP------DRAVVFQNHSLLPWL 93
Cdd:PRK11247 23 GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL------AGTAPlaeareDTRLMFQDARLLPWK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 94 TVYQNVELavkqiaGKKGKaWiQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALT 173
Cdd:PRK11247 97 KVIDNVGL------GLKGQ-W-RDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491592515 174 RAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGpaaTIGEVLEVNLPRPRER 234
Cdd:PRK11247 169 RIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEG---KIGLDLTVDLPRPRRR 226
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-230 |
2.62e-54 |
|
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: 176.15 E-value: 2.62e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 5 LLDLTRLGMRFPTPDGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDR---- 80
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 81 -AVVFQN--HSLLPWLTVYQNVELAVKQIagkkGKAWIQEQVNHYLELIQMQHA-AHKKPDEISGGMKQRVGIARALALQ 156
Cdd:COG1124 81 vQMVFQDpyASLHPRHTVDRILAEPLRIH----GLPDREERIAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARALILE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491592515 157 PKVLLMDEPFGALDALTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGpaaTIGEVLEVNLPR 230
Cdd:COG1124 157 PELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNG---RIVEELTVADLL 227
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
27-221 |
3.51e-54 |
|
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: 174.79 E-value: 3.51e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 27 NVDLQINkGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGR-------EVAGPGPDRAV--VFQNHSLLPWLTVYQ 97
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsrkKINLPPQQRKIglVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 98 NVELAVKQIAGKKgkawIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHL 177
Cdd:cd03297 95 NLAFGLKRKRNRE----DRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491592515 178 QDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIG 221
Cdd:cd03297 171 LPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
18-215 |
7.84e-54 |
|
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: 173.81 E-value: 7.84e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 18 PDGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDR-----AVVFQN--HSLL 90
Cdd:cd03225 10 PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrrkvGLVFQNpdDQFF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 91 PwLTVYQNVELAVKQIagKKGKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALD 170
Cdd:cd03225 90 G-PTVEEEVAFGLENL--GLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 491592515 171 ALTRAHLQDALMKIQAElNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:cd03225 167 PAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
40-222 |
2.89e-53 |
|
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: 175.76 E-value: 2.89e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 40 LIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDR---AVVFQNHSLLPWLTVYQNVELAVKQiaGKKGKAWIQ 116
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLrhiNMVFQSYALFPHMTVEENVAFGLKM--RKVPRAEIK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 117 EQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHLQDALMKIQAELNNTVIMIT 196
Cdd:TIGR01187 79 PRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVT 158
|
170 180
....*....|....*....|....*.
gi 491592515 197 HDVDEAVLLSDKIVMMTNGPAATIGE 222
Cdd:TIGR01187 159 HDQEEAMTMSDRIAIMRKGKIAQIGT 184
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-226 |
3.18e-53 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 177.33 E-value: 3.18e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 5 LLDLTRLGMRFptpDGEFiALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDRA--- 81
Cdd:PRK11607 19 LLEIRNLTKSF---DGQH-AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRpin 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 82 VVFQNHSLLPWLTVYQNVELAVKQiaGKKGKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLL 161
Cdd:PRK11607 95 MMFQSYALFPHMTVEQNIAFGLKQ--DKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491592515 162 MDEPFGALDALTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIGEVLEV 226
Cdd:PRK11607 173 LDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
20-225 |
4.09e-52 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 174.06 E-value: 4.09e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 20 GEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAG-PGPDRAV--VFQNHSLLPWLTVY 96
Cdd:PRK11000 14 GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDvPPAERGVgmVFQSYALYPHLSVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 97 QNVELAVKqIAGKKgKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAH 176
Cdd:PRK11000 94 ENMSFGLK-LAGAK-KEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQ 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491592515 177 LQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIGEVLE 225
Cdd:PRK11000 172 MRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLE 220
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-215 |
8.61e-52 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 169.47 E-value: 8.61e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 4 ALLDLTRLGMRFPtpdGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDR--- 80
Cdd:COG3638 1 PMLELRNLSKRYP---GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 81 -----AVVFQNHSLLPWLTVYQNVelavkqIAGKKG-----KAWIQ-------EQVNHYLELIQMQHAAHKKPDEISGGM 143
Cdd:COG3638 78 lrrriGMIFQQFNLVPRLSVLTNV------LAGRLGrtstwRSLLGlfppedrERALEALERVGLADKAYQRADQLSGGQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491592515 144 KQRVGIARALALQPKVLLMDEPFGALDALTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:COG3638 152 QQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDG 223
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
7-236 |
1.19e-51 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 172.29 E-value: 1.19e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 7 DLTRLGMRFPTPDGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPD--RA--- 81
Cdd:PRK11153 3 ELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKelRKarr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 82 ---VVFQNHSLLPWLTVYQNVELAVKqIAGKKgKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPK 158
Cdd:PRK11153 83 qigMIFQHFNLLSSRTVFDNVALPLE-LAGTP-KAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491592515 159 VLLMDEPFGALD-ALTRAHLqDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIGEVLEVNLpRPRERVA 236
Cdd:PRK11153 161 VLLCDEATSALDpATTRSIL-ELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFS-HPKHPLT 237
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-221 |
4.11e-51 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 171.06 E-value: 4.11e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 1 MEKALLDLTRLGMRFptpdGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAgpgpDR 80
Cdd:PRK11432 2 TQKNFVVLKNITKRF----GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT----HR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 81 AV-------VFQNHSLLPWLTVYQNVELAVKQIagKKGKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARAL 153
Cdd:PRK11432 74 SIqqrdicmVFQSYALFPHMSLGENVGYGLKML--GVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491592515 154 ALQPKVLLMDEPFGALDALTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIG 221
Cdd:PRK11432 152 ILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIG 219
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
4-215 |
6.92e-51 |
|
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: 167.52 E-value: 6.92e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 4 ALLDLTRLGMRFptpdGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDRAV- 82
Cdd:COG0411 3 PLLEVRGLTKRF----GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIAr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 83 -----VFQNHSLLPWLTVYQNVELAVKQIAG-------------KKGKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMK 144
Cdd:COG0411 79 lgiarTFQNPRLFPELTVLENVLVAAHARLGrgllaallrlpraRREEREARERAEELLERVGLADRADEPAGNLSYGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491592515 145 QRVGIARALALQPKVLLMDEPFGALDALTRAHLQDALMKIQAELNNTVIMITHDVDeAVL-LSDKIVMMTNG 215
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMD-LVMgLADRIVVLDFG 229
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
5-200 |
8.80e-51 |
|
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: 165.88 E-value: 8.80e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 5 LLDLTRLGMRFPTPdgeFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAgPGPDRA--- 81
Cdd:TIGR02673 1 MIEFHNVSKAYPGG---VAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVN-RLRGRQlpl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 82 ------VVFQNHSLLPWLTVYQNVELAVkQIAGKKGKAwIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALAL 155
Cdd:TIGR02673 77 lrrrigVVFQDFRLLPDRTVYENVALPL-EVRGKKERE-IQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVN 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491592515 156 QPKVLLMDEPFGALDaltrAHLQDALMKIQAELNN---TVIMITHDVD 200
Cdd:TIGR02673 155 SPPLLLADEPTGNLD----PDLSERILDLLKRLNKrgtTVIVATHDLS 198
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-215 |
1.08e-50 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 166.32 E-value: 1.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 5 LLDLTRLGMRFptpdGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDRA--- 81
Cdd:COG1126 1 MIEIENLHKSF----GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINklr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 82 ----VVFQNHSLLPWLTVYQNVELA---VKqiagKKGKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALA 154
Cdd:COG1126 77 rkvgMVFQQFNLFPHLTVLENVTLApikVK----KMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491592515 155 LQPKVLLMDEPFGALD-ALTRAHLQdaLMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:COG1126 153 MEPKVMLFDEPTSALDpELVGEVLD--VMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGG 212
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
25-226 |
3.66e-50 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 168.72 E-value: 3.66e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAG-PGPDRAV--VFQNHSLLPWLTVYQNVEL 101
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRlHARDRKVgfVFQHYALFRHMTVFDNIAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 102 AVKQIAGKK--GKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHLQD 179
Cdd:PRK10851 98 GLTVLPRRErpNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRR 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491592515 180 ALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIGEVLEV 226
Cdd:PRK10851 178 WLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-212 |
8.42e-50 |
|
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: 166.77 E-value: 8.42e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 5 LLDLTRLGMRFPTPDGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMP---TDGGVIVDGREVAGPGPDR- 80
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 81 --------AVVFQN--HSLLPWLTVYQNVELAVKqIAGKKGKAWIQEQVNHYLELIQMQHA---AHKKPDEISGGMKQRV 147
Cdd:COG0444 81 rkirgreiQMIFQDpmTSLNPVMTVGDQIAEPLR-IHGGLSKAEARERAIELLERVGLPDPerrLDRYPHELSGGMRQRV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491592515 148 GIARALALQPKVLLMDEPFGALDALTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMM 212
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVM 224
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-215 |
1.07e-49 |
|
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: 163.76 E-value: 1.07e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 6 LDLTRLGMRFptpdGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDRAV--- 82
Cdd:cd03219 1 LEVRGLTKRF----GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIArlg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 83 ---VFQNHSLLPWLTVYQNVELAVKQIAGKKGKAW--------IQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIAR 151
Cdd:cd03219 77 igrTFQIPRLFPELTVLENVMVAAQARTGSGLLLArarreereARERAEELLERVGLADLADRPAGELSYGQQRRLEIAR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491592515 152 ALALQPKVLLMDEPFGALDALTRAHLQDALMKIqAELNNTVIMITHDVDeAVL-LSDKIVMMTNG 215
Cdd:cd03219 157 ALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMD-VVMsLADRVTVLDQG 219
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-215 |
3.08e-49 |
|
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: 160.64 E-value: 3.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 6 LDLTRLGMRFptpdGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDR----A 81
Cdd:cd03230 1 IEVRNLSKRY----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVkrriG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 82 VVFQNHSLLPWLTVYQNVELavkqiagkkgkawiqeqvnhyleliqmqhaahkkpdeiSGGMKQRVGIARALALQPKVLL 161
Cdd:cd03230 77 YLPEEPSLYENLTVRENLKL--------------------------------------SGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491592515 162 MDEPFGALDALTRAHLQDALMKIQAElNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNG 171
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-233 |
5.91e-49 |
|
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: 169.31 E-value: 5.91e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 1 MEkALLDLTRLGMRFPtpDGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPT---DGGVIVDGREVAGP- 76
Cdd:COG1123 1 MT-PLLEVRDLSVRYP--GGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELs 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 77 ----GPDRAVVFQN--HSLLPwLTVYQNVELAVKqiAGKKGKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIA 150
Cdd:COG1123 78 ealrGRRIGMVFQDpmTQLNP-VTVGDQIAEALE--NLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 151 RALALQPKVLLMDEPFGALDALTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIGEVLEVnLPR 230
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI-LAA 233
|
...
gi 491592515 231 PRE 233
Cdd:COG1123 234 PQA 236
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
27-241 |
3.02e-48 |
|
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: 163.73 E-value: 3.02e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 27 NVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGR----EVAG---PGPDRAV--VFQNHSLLPWLTVYQ 97
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdSARGiflPPHRRRIgyVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 98 NVELAVKQIAGKKGKAwiqeQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHL 177
Cdd:COG4148 97 NLLYGRKRAPRAERRI----SFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEI 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491592515 178 QDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIGEVLEVnLPRPR-ERVALADDA 241
Cdd:COG4148 173 LPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEV-LSRPDlLPLAGGEEA 236
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
20-226 |
7.53e-48 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 159.82 E-value: 7.53e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 20 GEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAG-PGPDRA----VVFQNHSLLPWLT 94
Cdd:COG1120 12 GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASlSRRELArriaYVPQEPPAPFGLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 95 VYQNVEL---AVKQIAGKKGKAWiQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDA 171
Cdd:COG1120 92 VRELVALgryPHLGLFGRPSAED-REAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491592515 172 LTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIGEVLEV 226
Cdd:COG1120 171 AHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
20-215 |
1.54e-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: 1.54e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 20 GEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPD----R---AVVFQNHSLLPW 92
Cdd:cd03262 11 GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinelRqkvGMVFQQFNLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 93 LTVYQNVELAVKQIAGKKgKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDAL 172
Cdd:cd03262 91 LTVLENITLAPIKVKGMS-KAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 491592515 173 TRAHLQDaLMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:cd03262 170 LVGEVLD-VMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDG 211
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
29-223 |
5.57e-47 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 156.84 E-value: 5.57e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 29 DLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDR---AVVFQNHSLLPWLTVYQNVELAVKq 105
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAErpvSMLFQENNLFPHLTVAQNIGLGLR- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 106 iAGKKGKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHLQDALMKIQ 185
Cdd:COG3840 98 -PGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELC 176
|
170 180 190
....*....|....*....|....*....|....*...
gi 491592515 186 AELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIGEV 223
Cdd:COG3840 177 RERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPT 214
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-215 |
6.20e-47 |
|
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: 156.96 E-value: 6.20e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 6 LDLTRLGMRFPtpdGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDR----- 80
Cdd:cd03256 1 IEVENLSKTYP---NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 81 ---AVVFQNHSLLPWLTVYQNV---ELA----VKQIAGKKGKAWIQEQVnHYLELIQMQHAAHKKPDEISGGMKQRVGIA 150
Cdd:cd03256 78 rqiGMIFQQFNLIERLSVLENVlsgRLGrrstWRSLFGLFPKEEKQRAL-AALERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491592515 151 RALALQPKVLLMDEPFGALDALTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDG 221
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-215 |
6.65e-47 |
|
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: 156.44 E-value: 6.65e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 1 MEKALLDLTRLGMRFPTPDGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPD- 79
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDa 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 80 RA--------VVFQNHSLLPWLTVYQNV----ELAVKQIAGKKGKAWiqeqvnhyLELIQMQHAAHKKPDEISGGMKQRV 147
Cdd:COG4181 84 RArlrarhvgFVFQSFQLLPTLTALENVmlplELAGRRDARARARAL--------LERVGLGHRLDHYPAQLSGGEQQRV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491592515 148 GIARALALQPKVLLMDEPFGALDALTRAHLQDALMKIQAELNNTVIMITHDVDEAvLLSDKIVMMTNG 215
Cdd:COG4181 156 ALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLRLRAG 222
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
19-226 |
1.29e-46 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 159.24 E-value: 1.29e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 19 DGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGP-DR--AVVFQNHSLLPWLTV 95
Cdd:PRK11650 14 DGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPaDRdiAMVFQNYALYPHMSV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 96 YQNVELAVKqIAGKkGKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRA 175
Cdd:PRK11650 94 RENMAYGLK-IRGM-PKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491592515 176 HLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIGEVLEV 226
Cdd:PRK11650 172 QMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEV 222
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
29-221 |
4.79e-46 |
|
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: 153.80 E-value: 4.79e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 29 DLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREV-AGPGPDRAV--VFQNHSLLPWLTVYQNVELAVkq 105
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVtAAPPADRPVsmLFQENNLFAHLTVEQNVGLGL-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 106 IAGKKGKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHLQDALMKIQ 185
Cdd:cd03298 96 SPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLH 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 491592515 186 AELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIG 221
Cdd:cd03298 176 AETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
5-215 |
2.34e-45 |
|
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: 152.84 E-value: 2.34e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 5 LLDLTRLGMRFPTPDgefIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDR---- 80
Cdd:TIGR02315 1 MLEVENLSKVYPNGK---QALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrkl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 81 ----AVVFQNHSLLPWLTVYQNV-------ELAVKQIAGKKGKAWIQEQVNhYLELIQMQHAAHKKPDEISGGMKQRVGI 149
Cdd:TIGR02315 78 rrriGMIFQHYNLIERLTVLENVlhgrlgyKPTWRSLLGRFSEEDKERALS-ALERVGLADKAYQRADQLSGGQQQRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491592515 150 ARALALQPKVLLMDEPFGALDALTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAG 222
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
20-226 |
1.02e-44 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 150.79 E-value: 1.02e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 20 GEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHM-----PTDGGVIVDGREVAGPGPDR-------AVVFQNH 87
Cdd:cd03260 11 GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDVlelrrrvGMVFQKP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 88 SLLPwLTVYQNVELAVKqIAGKKGKAWIQEQVNHYLELIQMQHAAHKKPD--EISGGMKQRVGIARALALQPKVLLMDEP 165
Cdd:cd03260 91 NPFP-GSIYDNVAYGLR-LHGIKLKEELDERVEEALRKAALWDEVKDRLHalGLSGGQQQRLCLARALANEPEVLLLDEP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491592515 166 FGALDALTRAHLQDALMKIQAELnnTVIMITHDVDEAVLLSDKIVMMTNgpaatiGEVLEV 226
Cdd:cd03260 169 TSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLN------GRLVEF 221
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
5-215 |
3.08e-44 |
|
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: 149.42 E-value: 3.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 5 LLDLTRLGMRFPTPDGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREV-AGPGPDRA-- 81
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLsKLSSNERAkl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 82 ------VVFQNHSLLPWLTVYQNVelAVKQIAGKKGKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALAL 155
Cdd:TIGR02211 81 rnkklgFIYQFHHLLPDFTALENV--AMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 156 QPKVLLMDEPFGALDALTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLsDKIVMMTNG 215
Cdd:TIGR02211 159 QPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDG 217
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
18-215 |
5.27e-44 |
|
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: 150.27 E-value: 5.27e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 18 PDGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDG------------REVAGpgpdraVVFQ 85
Cdd:TIGR04520 11 PESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGldtldeenlweiRKKVG------MVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 86 NhsllPwltvyQN------VELAV------KQIAGKKgkawIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARAL 153
Cdd:TIGR04520 85 N----P-----DNqfvgatVEDDVafglenLGVPREE----MRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491592515 154 ALQPKVLLMDEPFGALDALTRAHLQDALMKIQAELNNTVIMITHDVDEAVlLSDKIVMMTNG 215
Cdd:TIGR04520 152 AMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNKG 212
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-211 |
5.53e-44 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 151.81 E-value: 5.53e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 1 MEKALLDLTRLGMRFPTPDGEFI-------ALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREV 73
Cdd:COG4608 3 MAEPLLEVRDLKKHFPVRGGLFGrtvgvvkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 74 AGPGPDRA--------VVFQN--HSLLPWLTVYQNVELAVKqIAGKKGKAWIQEQVNHYLELIQM-QHAAHKKPDEISGG 142
Cdd:COG4608 83 TGLSGRELrplrrrmqMVFQDpyASLNPRMTVGDIIAEPLR-IHGLASKAERRERVAELLELVGLrPEHADRYPHEFSGG 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491592515 143 MKQRVGIARALALQPKVLLMDEPFGALDALTRAHLQDALMKIQAELNNTVIMITHDVdeAVL--LSDKI-VM 211
Cdd:COG4608 162 QRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDL--SVVrhISDRVaVM 231
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
25-215 |
1.93e-43 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 146.88 E-value: 1.93e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAG-PGPD--RAV--VFQNHSLlpWL-TVYQN 98
Cdd:COG4619 16 LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAmPPPEwrRQVayVPQEPAL--WGgTVRDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 99 VELavkqIAGKKGKAWIQEQVNHYLELIQMQHAAHKKP-DEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHL 177
Cdd:COG4619 94 LPF----PFQLRERKFDRERALELLERLGLPPDILDKPvERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRV 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 491592515 178 QDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:COG4619 170 EELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAG 207
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
24-198 |
3.38e-43 |
|
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: 146.40 E-value: 3.38e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 24 ALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPgPDRA---------VVFQNHSLLPWLT 94
Cdd:cd03292 16 ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDL-RGRAipylrrkigVVFQDFRLLPDRN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 95 VYQNVELAVkQIAGKKGKAWiQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTR 174
Cdd:cd03292 95 VYENVAFAL-EVTGVPPREI-RKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTT 172
|
170 180
....*....|....*....|....
gi 491592515 175 AHLQDALMKIQAElNNTVIMITHD 198
Cdd:cd03292 173 WEIMNLLKKINKA-GTTVVVATHA 195
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
25-166 |
5.52e-43 |
|
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: 143.94 E-value: 5.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDR-----AVVFQNHSLLPWLTVYQNV 99
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlrkeiGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491592515 100 ELAVkqIAGKKGKAWIQEQVNHYLELIQMQHAAHKKPD----EISGGMKQRVGIARALALQPKVLLMDEPF 166
Cdd:pfam00005 81 RLGL--LLKGLSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
18-215 |
6.76e-43 |
|
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: 144.06 E-value: 6.76e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 18 PDGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDR-----AVVFQNhsllPW 92
Cdd:cd03228 11 PGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrkniAYVPQD----PF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 93 L---TVYQNVelavkqiagkkgkawiqeqvnhyleliqmqhaahkkpdeISGGMKQRVGIARALALQPKVLLMDEPFGAL 169
Cdd:cd03228 87 LfsgTIRENI---------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSAL 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491592515 170 DALTRAHLQDALMKIQAELnnTVIMITHDVdEAVLLSDKIVMMTNG 215
Cdd:cd03228 128 DPETEALILEALRALAKGK--TVIVIAHRL-STIRDADRIIVLDDG 170
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
21-226 |
1.21e-42 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 146.83 E-value: 1.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 21 EFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREV-AGPGPDR-------AVVFQN--HSLL 90
Cdd:TIGR04521 17 EKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDItAKKKKKLkdlrkkvGLVFQFpeHQLF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 91 PwLTVYQNVELAVKQIagKKGKAWIQEQVNHYLELIQMQHA-AHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGAL 169
Cdd:TIGR04521 97 E-ETVYKDIAFGPKNL--GLSEEEAEERVKEALELVGLDEEyLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491592515 170 DALTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIGEVLEV 226
Cdd:TIGR04521 174 DPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREV 230
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-225 |
1.41e-42 |
|
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: 144.96 E-value: 1.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 6 LDLTRLGMRFPTpdGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAgPGPDRA---- 81
Cdd:cd03263 1 LQIRNLTKTYKK--GTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR-TDRKAArqsl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 82 -VVFQNHSLLPWLTVYQNVELavkqIAGKKGKAW--IQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPK 158
Cdd:cd03263 78 gYCPQFDALFDELTVREHLRF----YARLKGLPKseIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491592515 159 VLLMDEPFGALDALTRAHLQDALMKIQAelNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIGEVLE 225
Cdd:cd03263 154 VLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
20-226 |
1.97e-42 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 149.80 E-value: 1.97e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 20 GEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDR---------AVVFQNHSLL 90
Cdd:PRK10070 39 GLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevrrkkiAMVFQSFALM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 91 PWLTVYQNVELAVkQIAGKKGkAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALD 170
Cdd:PRK10070 119 PHMTVLDNTAFGM-ELAGINA-EERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491592515 171 ALTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIGEVLEV 226
Cdd:PRK10070 197 PLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
25-215 |
2.60e-42 |
|
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: 144.39 E-value: 2.60e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDRAV--------VFQNHSLLPWLTVY 96
Cdd:TIGR02982 21 LFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVqlrrrigyIFQAHNLLGFLTAR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 97 QNVELAVKQIAGKKGKAwIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAH 176
Cdd:TIGR02982 101 QNVQMALELQPNLSYQE-ARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAALDSKSGRD 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 491592515 177 LQDALMKIQAELNNTVIMITHD---VDEAvllsDKIVMMTNG 215
Cdd:TIGR02982 180 VVELMQKLAKEQGCTILMVTHDnriLDVA----DRILQMEDG 217
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
25-215 |
7.50e-42 |
|
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: 141.80 E-value: 7.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAgpgpdravvfqnhsllpwltVYQNVELAvK 104
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLA--------------------SLSPKELA-R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 105 QIAgkkgkawIQEQVnhyLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHLQDALMKI 184
Cdd:cd03214 74 KIA-------YVPQA---LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRL 143
|
170 180 190
....*....|....*....|....*....|.
gi 491592515 185 QAELNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:cd03214 144 ARERGKTVVMVLHDLNLAARYADRVILLKDG 174
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-215 |
1.51e-41 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 143.07 E-value: 1.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 5 LLDLTRLGMRFptpdGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDR---- 80
Cdd:COG4555 1 MIEVENLSKKY----GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREArrqi 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 81 AVVFQNHSLLPWLTVYQNVEL--AVKQIAGKKGKAWIQEqvnhYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPK 158
Cdd:COG4555 77 GVLPDERGLYDRLTVRENIRYfaELYGLFDEELKKRIEE----LIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491592515 159 VLLMDEPFGALDALTRAHLQDALMKIqAELNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKG 208
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
20-218 |
2.00e-41 |
|
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: 141.90 E-value: 2.00e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 20 GEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDRAVVFQNHSL---LPwLTVY 96
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGYVPQRRSIdrdFP-ISVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 97 QNVELA------VKQIAGKKGKAWIQEQvnhyLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALD 170
Cdd:cd03235 89 DVVLMGlyghkgLFRRLSKADKAKVDEA----LERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491592515 171 ALTRAHLQDALMKIQAElNNTVIMITHDVDEAVLLSDKIVMMTNGPAA 218
Cdd:cd03235 165 PKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRTVVA 211
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
20-225 |
2.22e-41 |
|
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: 142.12 E-value: 2.22e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 20 GEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAG-PGPDRA---VVFQNHSLLPWLTV 95
Cdd:cd03265 11 GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVRePREVRRrigIVFQDLSVDDELTG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 96 YQNVELAVKqIAGKKGKAWiQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRA 175
Cdd:cd03265 91 WENLYIHAR-LYGVPGAER-RERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491592515 176 HLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIGEVLE 225
Cdd:cd03265 169 HVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
20-215 |
3.31e-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: 139.30 E-value: 3.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 20 GEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDR-----AVVFQnhsllpwlt 94
Cdd:cd00267 10 GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEElrrriGYVPQ--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 95 vyqnvelavkqiagkkgkawiqeqvnhyleliqmqhaahkkpdeISGGMKQRVGIARALALQPKVLLMDEPFGALDALTR 174
Cdd:cd00267 81 --------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASR 116
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 491592515 175 AHLQDALMKIQAElNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:cd00267 117 ERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
24-224 |
2.86e-40 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 139.84 E-value: 2.86e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 24 ALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDRAVVFQNHSL---LPwLTVYQNVE 100
Cdd:COG1121 21 VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIGYVPQRAEVdwdFP-ITVRDVVL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 101 LAVKQIAG--KKGKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHLQ 178
Cdd:COG1121 100 MGRYGRRGlfRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALY 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491592515 179 DALMKIQAElNNTVIMITHDVDEAVLLSDKIVMMTNGPAA--TIGEVL 224
Cdd:COG1121 180 ELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVAhgPPEEVL 226
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
20-234 |
8.46e-40 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 138.69 E-value: 8.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 20 GEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPD-RAV------VFQNHSLLPW 92
Cdd:PRK09493 12 GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDeRLIrqeagmVFQQFYLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 93 LTVYQNVELAVKQIAGKkGKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDAL 172
Cdd:PRK09493 92 LTALENVMFGPLRVRGA-SKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491592515 173 TRaHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIG--EVLEVNLPRPRER 234
Cdd:PRK09493 171 LR-HEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGdpQVLIKNPPSQRLQ 233
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
20-198 |
1.85e-39 |
|
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: 136.59 E-value: 1.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 20 GEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDRAV---------VFQNHSLL 90
Cdd:TIGR03608 9 GDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASkfrreklgyLFQNFALI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 91 PWLTVYQNVELAVKQIAGKKGKawIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALD 170
Cdd:TIGR03608 89 ENETVEENLDLGLKYKKLSKKE--KREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLD 166
|
170 180 190
....*....|....*....|....*....|.
gi 491592515 171 ALTRahlqDALMKIQAELNN---TVIMITHD 198
Cdd:TIGR03608 167 PKNR----DEVLDLLLELNDegkTIIIVTHD 193
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
18-215 |
1.17e-38 |
|
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: 143.44 E-value: 1.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 18 PDGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPD--R---AVVFQNHSLLPw 92
Cdd:COG2274 484 PGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPAslRrqiGVVLQDVFLFS- 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 93 LTVYQNVELAVKQIAgkkgkawiQEQVNHYLELIQMQHAAHKKPD-----------EISGGMKQRVGIARALALQPKVLL 161
Cdd:COG2274 563 GTIRENITLGDPDAT--------DEEIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIARALLRNPRILI 634
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491592515 162 MDEPFGALDALTRAHLQDALMKIQAelNNTVIMITHDvDEAVLLSDKIVMMTNG 215
Cdd:COG2274 635 LDEATSALDAETEAIILENLRRLLK--GRTVIIIAHR-LSTIRLADRIIVLDKG 685
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
20-226 |
5.01e-38 |
|
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: 136.78 E-value: 5.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 20 GEFiALKnVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAG-------PGPDRAV--VFQNHSLL 90
Cdd:TIGR02142 10 GDF-SLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgiflPPEKRRIgyVFQEARLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 91 PWLTVYQNVELAVKQIAGKKGKAWIQEqvnhYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALD 170
Cdd:TIGR02142 88 PHLSVRGNLRYGMKRARPSERRISFER----VIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491592515 171 ALTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIGEVLEV 226
Cdd:TIGR02142 164 DPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
20-227 |
5.44e-38 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 134.39 E-value: 5.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 20 GEFIALKNVDLQINKGEFVSLIGHSGCGKSTVL---N----LVAGLHMptDGGVIVDGREVAGPGPD-----RAV--VFQ 85
Cdd:COG1117 22 GDKQALKDINLDIPENKVTALIGPSGCGKSTLLrclNrmndLIPGARV--EGEILLDGEDIYDPDVDvvelrRRVgmVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 86 NHSLLPwLTVYQNVELAVKqIAGKKGKAWIQEQVNHYLeliqmQHAA---------HKKPDEISGGMKQRVGIARALALQ 156
Cdd:COG1117 100 KPNPFP-KSIYDNVAYGLR-LHGIKSKSELDEIVEESL-----RKAAlwdevkdrlKKSALGLSGGQQQRLCIARALAVE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491592515 157 PKVLLMDEPFGALDALTRAHLQDALMKIQAELnnTVIMITHDVDEAVLLSDKIVMMTNgpaatiGEVLEVN 227
Cdd:COG1117 173 PEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTHNMQQAARVSDYTAFFYL------GELVEFG 235
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-215 |
2.48e-37 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 133.22 E-value: 2.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 1 MEKALLDLTRLGMRFPtpDGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAgpgpDR 80
Cdd:PRK13635 1 MKEEIIRVEHISFRYP--DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLS----EE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 81 AV---------VFQNhsllP-----WLTVYQNVELAVKQIAGKKGKawIQEQVNHYLELIQMQHAAHKKPDEISGGMKQR 146
Cdd:PRK13635 75 TVwdvrrqvgmVFQN----PdnqfvGATVQDDVAFGLENIGVPREE--MVERVDQALRQVGMEDFLNREPHRLSGGQKQR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491592515 147 VGIARALALQPKVLLMDEPFGALDALTRAHLQDALMKIQAELNNTVIMITHDVDEAvLLSDKIVMMTNG 215
Cdd:PRK13635 149 VAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKG 216
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
25-202 |
3.72e-37 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 130.68 E-value: 3.72e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMP---TDGGVIVDGREV-AGPGPDRAV--VFQNHSLLPWLTVYQN 98
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLtALPAEQRRIgiLFQDDLLFPHLSVGEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 99 VELAvkqIAGKKGKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAH-L 177
Cdd:COG4136 97 LAFA---LPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQfR 173
|
170 180
....*....|....*....|....*
gi 491592515 178 QDALMKIQaELNNTVIMITHDVDEA 202
Cdd:COG4136 174 EFVFEQIR-QRGIPALLVTHDEEDA 197
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
15-226 |
9.90e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 131.27 E-value: 9.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 15 FPTPDGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDRA-----VVFQNhsl 89
Cdd:PRK13632 15 FSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIrkkigIIFQN--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 90 lP-----WLTVYQNVE--LAVKQIAGKKgkawIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLM 162
Cdd:PRK13632 92 -PdnqfiGATVEDDIAfgLENKKVPPKK----MKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIF 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491592515 163 DEPFGALDALTRAHLQDALMKIQAELNNTVIMITHDVDEAvLLSDKIVMMTNGPAATIGEVLEV 226
Cdd:PRK13632 167 DESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEI 229
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-215 |
4.61e-36 |
|
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: 126.39 E-value: 4.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 6 LDLTRLGMRFptpdGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDRAvvfQ 85
Cdd:cd03216 1 LELRGITKRF----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDA---R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 86 NHSLlpwLTVYQnvelavkqiagkkgkawiqeqvnhyleliqmqhaahkkpdeISGGMKQRVGIARALALQPKVLLMDEP 165
Cdd:cd03216 74 RAGI---AMVYQ-----------------------------------------LSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491592515 166 FGALDALTRAHLQDALMKIQAElNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:cd03216 110 TAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDG 158
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
21-226 |
2.10e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 128.24 E-value: 2.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 21 EFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDRA-------VVFQ--NHSLLP 91
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSdirkkvgLVFQypEYQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 92 WlTVYQNVELAVKQIAGKKGKawIQEQVNHYLELIQMQHA--AHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGAL 169
Cdd:PRK13637 99 E-TIEKDIAFGPINLGLSEEE--IENRVKRAMNIVGLDYEdyKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491592515 170 DALTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIGEVLEV 226
Cdd:PRK13637 176 DPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREV 232
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
18-215 |
3.72e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 127.54 E-value: 3.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 18 PDGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAgpgPDR--------AVVFQN-HS 88
Cdd:PRK13650 16 EDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLT---EENvwdirhkiGMVFQNpDN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 89 LLPWLTVYQNVE--LAVKQIAGKKgkawIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPF 166
Cdd:PRK13650 93 QFVGATVEDDVAfgLENKGIPHEE----MKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEAT 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491592515 167 GALDALTRAHLQDALMKIQAELNNTVIMITHDVDEaVLLSDKIVMMTNG 215
Cdd:PRK13650 169 SMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNG 216
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
20-221 |
6.74e-35 |
|
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: 127.51 E-value: 6.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 20 GEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDG----REVAGPGPDRAVVFQNHSLLPWLTV 95
Cdd:TIGR01188 4 GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGydvvREPRKVRRSIGIVPQYASVDEDLTG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 96 YQNVELavkqIAGKKG--KAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALT 173
Cdd:TIGR01188 84 RENLEM----MGRLYGlpKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRT 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491592515 174 RAHLQDALMKIQaELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIG 221
Cdd:TIGR01188 160 RRAIWDYIRALK-EEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEG 206
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-198 |
2.28e-34 |
|
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: 123.36 E-value: 2.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 4 ALLDLTRLGMRFptpdGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDR--- 80
Cdd:COG4133 1 MMLEAENLSCRR----GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYrrr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 81 -AVVFQNHSLLPWLTVYQNVELAVKQiagkKGKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKV 159
Cdd:COG4133 77 lAYLGHADGLKPELTVRENLRFWAAL----YGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 491592515 160 LLMDEPFGALDALTRAHLQDAlmkIQAELNN--TVIMITHD 198
Cdd:COG4133 153 WLLDEPFTALDAAGVALLAEL---IAAHLARggAVLLTTHQ 190
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
4-253 |
4.60e-34 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 130.23 E-value: 4.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 4 ALLDLTRLGMRFPTPDGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDR--- 80
Cdd:PRK10535 3 ALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAlaq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 81 ------AVVFQNHSLLPWLTVYQNVElaVKQIAGKKGKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALA 154
Cdd:PRK10535 83 lrrehfGFIFQRYHLLSHLTAAQNVE--VPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 155 LQPKVLLMDEPFGALDaltrAHLQDALMKIQAELN---NTVIMITHDVDEAVlLSDKIVMMTNgpaatiGEVLEVNLPRP 231
Cdd:PRK10535 161 NGGQVILADEPTGALD----SHSGEEVMAILHQLRdrgHTVIIVTHDPQVAA-QAERVIEIRD------GEIVRNPPAQE 229
|
250 260
....*....|....*....|....*
gi 491592515 232 RERVALADDAQYQK---CRQAVLKF 253
Cdd:PRK10535 230 KVNVAGGTEPVVNTasgWRQFVSGF 254
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
5-220 |
1.82e-33 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 127.49 E-value: 1.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 5 LLDLTRLGMRFPTPDG-------EFIALKNVDLQINKGEFVSLIGHSGCGKST----VLNLVaglhmPTDGGVIVDGREV 73
Cdd:COG4172 275 LLEARDLKVWFPIKRGlfrrtvgHVKAVDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLI-----PSEGEIRFDGQDL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 74 AG--PGPDRA------VVFQN--HSLLPWLTVYQNVE--LAVKQIagKKGKAWIQEQVNHYLELIQMQHAA-HKKPDEIS 140
Cdd:COG4172 350 DGlsRRALRPlrrrmqVVFQDpfGSLSPRMTVGQIIAegLRVHGP--GLSAAERRARVAEALEEVGLDPAArHRYPHEFS 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 141 GGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHLQDALMKIQAELNNTVIMITHDVdeAVL--LSDKIVMMTNG--- 215
Cdd:COG4172 428 GGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDL--AVVraLAHRVMVMKDGkvv 505
|
....*...
gi 491592515 216 ---PAATI 220
Cdd:COG4172 506 eqgPTEQV 513
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
19-215 |
1.84e-33 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 127.97 E-value: 1.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 19 DGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDR-----AVVFQNHSLLPwL 93
Cdd:COG1132 350 PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrrqiGVVPQDTFLFS-G 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 94 TVYQNVELAVKQIAgkkgkawiQEQVNHYLELIQMQHAAHKKPD-----------EISGGMKQRVGIARALALQPKVLLM 162
Cdd:COG1132 429 TIRENIRYGRPDAT--------DEEVEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIARALLKDPPILIL 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491592515 163 DEPFGALDALTRAHLQDALMKIQAelNNTVIMITHDVdEAVLLSDKIVMMTNG 215
Cdd:COG1132 501 DEATSALDTETEALIQEALERLMK--GRTTIVIAHRL-STIRNADRILVLDDG 550
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-211 |
1.91e-33 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 121.85 E-value: 1.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 1 MEKALLDLTRLGMRFPTPDGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAG-PGPD 79
Cdd:PRK11629 1 MNKILLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlSSAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 80 RA--------VVFQNHSLLPWLTVYQNVelAVKQIAGKKGKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIAR 151
Cdd:PRK11629 81 KAelrnqklgFIYQFHHLLPDFTALENV--AMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491592515 152 ALALQPKVLLMDEPFGALDALTrahlQDALMKIQAELN----NTVIMITHDVDEAVLLSDKIVM 211
Cdd:PRK11629 159 ALVNNPRLVLADEPTGNLDARN----ADSIFQLLGELNrlqgTAFLVVTHDLQLAKRMSRQLEM 218
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
18-215 |
6.71e-33 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 126.41 E-value: 6.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 18 PDGEFiALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDR-----AVVFQNhsllPW 92
Cdd:COG4988 347 PGGRP-ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwrrqiAWVPQN----PY 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 93 L---TVYQNVELAVKQIAgkkgkawiQEQVNHYLELIQMQHAAHKKPDEI-----------SGGMKQRVGIARALALQPK 158
Cdd:COG4988 422 LfagTIRENLRLGRPDAS--------DEELEAALEAAGLDEFVAALPDGLdtplgeggrglSGGQAQRLALARALLRDAP 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491592515 159 VLLMDEPFGALDALTRAHLQDALMKIQAelNNTVIMITHDvDEAVLLSDKIVMMTNG 215
Cdd:COG4988 494 LLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHR-LALLAQADRILVLDDG 547
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-215 |
1.23e-32 |
|
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: 119.39 E-value: 1.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 5 LLDLTRLGMRFPTPDGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVA-GPGPDRA-- 81
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVkEPAEARRrl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 82 -VVFQNHSLLPWLTVYQNVELaVKQIAGKKGKAwIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVL 160
Cdd:cd03266 81 gFVSDSTGLYDRLTARENLEY-FAGLYGLKGDE-LTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491592515 161 LMDEPFGALDALTRAHLQDALmKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:cd03266 159 LLDEPTTGLDVMATRALREFI-RQLRALGKCILFSTHIMQEVERLCDRVVVLHRG 212
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
20-215 |
1.62e-32 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 119.08 E-value: 1.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 20 GEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDRAV------VFQNHSLLPWL 93
Cdd:cd03224 11 GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERAragigyVPEGRRIFPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 94 TVYQNVELAVkQIAGKKGKAWIQEQVNHYL-ELIQMQHAahkKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDAL 172
Cdd:cd03224 91 TVEENLLLGA-YARRRAKRKARLERVYELFpRLKERRKQ---LAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPK 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 491592515 173 TRAHLQDALMKIQAElNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:cd03224 167 IVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERG 208
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-215 |
2.23e-32 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 124.41 E-value: 2.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 1 MEKALLDLTRLGMRFPTPDGEFIALKNVDLQINKGEFVSLIGHSGCGKS----TVLNLVAGLHMPTDGGVIVDGREVAGP 76
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 77 GPDR---------AVVFQN--HSLLPWLTVyqnvelaVKQIA-------GKKGKAwIQEQVNHYLELIQMQHAAHK---K 135
Cdd:COG4172 82 SERElrrirgnriAMIFQEpmTSLNPLHTI-------GKQIAevlrlhrGLSGAA-ARARALELLERVGIPDPERRldaY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 136 PDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHLQDALMKIQAELNNTVIMITHD---VDEavlLSDKIVMM 212
Cdd:COG4172 154 PHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDlgvVRR---FADRVAVM 230
|
...
gi 491592515 213 TNG 215
Cdd:COG4172 231 RQG 233
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
25-226 |
3.76e-32 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 119.06 E-value: 3.76e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPD-----RAVVFQNHSL-LPWlTVYQN 98
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWelarrRAVLPQHSSLaFPF-TVEEV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 99 VELAVkqIAGKKGKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALA-------LQPKVLLMDEPFGALDA 171
Cdd:COG4559 96 VALGR--APHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491592515 172 ltrAHlQDALMKIQAEL---NNTVIMITHDVDEAVLLSDKIVMMTNGPAATIGEVLEV 226
Cdd:COG4559 174 ---AH-QHAVLRLARQLarrGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEV 227
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
21-215 |
4.07e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 119.42 E-value: 4.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 21 EFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDG------------REVAGpgpdraVVFQN-H 87
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtsdeenlwdiRNKAG------MVFQNpD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 88 SLLPWLTVYQNVELAVKQIAGKKGKawIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFG 167
Cdd:PRK13633 96 NQIVATIVEEDVAFGPENLGIPPEE--IRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491592515 168 ALDALTRAHLQDALMKIQAELNNTVIMITHDVDEAVlLSDKIVMMTNG 215
Cdd:PRK13633 174 MLDPSGRREVVNTIKELNKKYGITIILITHYMEEAV-EADRIIVMDSG 220
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
25-215 |
5.94e-32 |
|
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: 117.64 E-value: 5.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAG-PGPDRA---VVF--QNHSLLPWLTVYQN 98
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKlPMHKRArlgIGYlpQEASIFRKLTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 99 VeLAVKQIAGKKGKAWIQEqVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHLQ 178
Cdd:cd03218 96 I-LAVLEIRGLSKKEREEK-LEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQ 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 491592515 179 dalmKIQAELN--NTVIMIT-HDVDEAVLLSDKIVMMTNG 215
Cdd:cd03218 174 ----KIIKILKdrGIGVLITdHNVRETLSITDRAYIIYEG 209
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-215 |
6.51e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 118.65 E-value: 6.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 17 TPDgEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAG-PGPDRAV----VFQNHSL-- 89
Cdd:COG1101 15 TVN-EKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKlPEYKRAKyigrVFQDPMMgt 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 90 LPWLTVYQNVELAVKQiaGKK---GKAWIQEQVNHYLELIQ-----MQHAAHKKPDEISGGmkQRvgiaRALAL------ 155
Cdd:COG1101 94 APSMTIEENLALAYRR--GKRrglRRGLTKKRRELFRELLAtlglgLENRLDTKVGLLSGG--QR----QALSLlmatlt 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 156 QPKVLLMDEPFGALDALTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:COG1101 166 KPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEG 225
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-215 |
8.30e-32 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 122.43 E-value: 8.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 2 EKALLDLTRLGMRFPTpdgeFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDRA 81
Cdd:COG1129 1 AEPLLEMRGISKSFGG----VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 82 ------VVFQNHSLLPWLTVYQNVELAvkQIAGKKG----KAwIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIAR 151
Cdd:COG1129 77 qaagiaIIHQELNLVPNLSVAENIFLG--REPRRGGlidwRA-MRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491592515 152 ALALQPKVLLMDEPFGALDALTRAHLQDALMKIQAElNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:COG1129 154 ALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDG 216
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
4-215 |
1.26e-31 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 116.99 E-value: 1.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 4 ALLDLT----RLGMRFptpdgefialknvDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPD 79
Cdd:PRK10771 3 KLTDITwlyhHLPMRF-------------DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 80 R---AVVFQNHSLLPWLTVYQNVELAVKqiAGKKGKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQ 156
Cdd:PRK10771 70 RrpvSMLFQENNLFSHLTVAQNIGLGLN--PGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVRE 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491592515 157 PKVLLMDEPFGALDALTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:PRK10771 148 QPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADG 206
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
4-226 |
1.87e-31 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 117.25 E-value: 1.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 4 ALLDLTRLGMRFPTPDG-----EFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVA-GPG 77
Cdd:COG4167 3 ALLEVRNLSKTFKYRTGlfrrqQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEyGDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 78 PDRA----VVFQ--NHSLLPWLTVYQ--------NVELAVKQIagkkgkawiQEQVNHYLELIQM--QHAaHKKPDEISG 141
Cdd:COG4167 83 KYRCkhirMIFQdpNTSLNPRLNIGQileeplrlNTDLTAEER---------EERIFATLRLVGLlpEHA-NFYPHMLSS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 142 GMKQRVGIARALALQPKVLLMDEPFGALDALTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIG 221
Cdd:COG4167 153 GQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYG 232
|
....*
gi 491592515 222 EVLEV 226
Cdd:COG4167 233 KTAEV 237
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
24-215 |
2.03e-31 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 116.65 E-value: 2.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 24 ALKNVDLQINKGEFVSLIGHSGCGKST---VLNLvagLHMPTDGGVIVDGREV---AGPGP--------DRAVVFQNHSL 89
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSllrVLNL---LEMPRSGTLNIAGNHFdfsKTPSDkairelrrNVGMVFQQYNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 90 LPWLTVYQNVELAVKQIAGKkGKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGAL 169
Cdd:PRK11124 94 WPHLTVQQNLIEAPCRVLGL-SKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491592515 170 DALTRAHlqdaLMKIQAELNNTVI---MITHDVDEAVLLSDKIVMMTNG 215
Cdd:PRK11124 173 DPEITAQ----IVSIIRELAETGItqvIVTHEVEVARKTASRVVYMENG 217
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-223 |
2.44e-31 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 121.29 E-value: 2.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 1 MEKALLDLTRLGMRFPTpdgeFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDR 80
Cdd:COG3845 1 MMPPALELRGITKRFGG----VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 81 AV------VFQNHSLLPWLTVYQNVELAVKQIAG-----KKGKAWIQEQVNHY-LELiqmqhAAHKKPDEISGGMKQRVG 148
Cdd:COG3845 77 AIalgigmVHQHFMLVPNLTVAENIVLGLEPTKGgrldrKAARARIRELSERYgLDV-----DPDAKVEDLSVGEQQRVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 149 IARALALQPKVLLMDEP------------FGALDALTRAHLqdalmkiqaelnnTVIMITHDVDEAVLLSDKIVMMTNGp 216
Cdd:COG3845 152 ILKALYRGARILILDEPtavltpqeadelFEILRRLAAEGK-------------SIIFITHKLREVMAIADRVTVLRRG- 217
|
....*..
gi 491592515 217 aATIGEV 223
Cdd:COG3845 218 -KVVGTV 223
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
20-215 |
4.67e-31 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 115.88 E-value: 4.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 20 GEFIALKNVDLQINKGEFVSLIGHSGCGKST---VLNLvagLHMPTDGGVIVDGREV---AGPGPDRA--------VVFQ 85
Cdd:COG4161 13 GSHQALFDINLECPSGETLVLLGPSGAGKSSllrVLNL---LETPDSGQLNIAGHQFdfsQKPSEKAIrllrqkvgMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 86 NHSLLPWLTVYQN-VELAVKQIAGKKGKAwiQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDE 164
Cdd:COG4161 90 QYNLWPHLTVMENlIEAPCKVLGLSKEQA--REKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491592515 165 PFGALDALTRAHlqdaLMKIQAELNNTVI---MITHDVDEAVLLSDKIVMMTNG 215
Cdd:COG4161 168 PTAALDPEITAQ----VVEIIRELSQTGItqvIVTHEVEFARKVASQVVYMEKG 217
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
24-199 |
6.89e-31 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 114.97 E-value: 6.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 24 ALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAG------PGPDRAV--VFQNHSLLPWLTV 95
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRlknrevPFLRRQIgmIFQDHHLLMDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 96 YQNVELAVKqIAGKKGKAwIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDaltrA 175
Cdd:PRK10908 97 YDNVAIPLI-IAGASGDD-IRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD----D 170
|
170 180
....*....|....*....|....*..
gi 491592515 176 HLQDALMKIQAELNN---TVIMITHDV 199
Cdd:PRK10908 171 ALSEGILRLFEEFNRvgvTVLMATHDI 197
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-230 |
6.91e-31 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 115.47 E-value: 6.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 1 MEKALLDLTRLGMRFptpdGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAG-PGPD 79
Cdd:PRK11300 1 MSQPLLSVSGLMMRF----GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGlPGHQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 80 RA---VV--FQNHSLLPWLTVYQNVELAVKQ------IAG-------KKGKAWIQEQVNHYLELIQMQHAAHKKPDEISG 141
Cdd:PRK11300 77 IArmgVVrtFQHVRLFREMTVIENLLVAQHQqlktglFSGllktpafRRAESEALDRAATWLERVGLLEHANRQAGNLAY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 142 GMKQRVGIARALALQPKVLLMDEPFGALDALTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIG 221
Cdd:PRK11300 157 GQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANG 236
|
250
....*....|
gi 491592515 222 EVLEV-NLPR 230
Cdd:PRK11300 237 TPEEIrNNPD 246
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-215 |
1.72e-30 |
|
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: 119.49 E-value: 1.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 4 ALLDLTRLGMRFPtpDGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDR--- 80
Cdd:COG4987 332 PSLELEDVSFRYP--GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrr 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 81 --AVVFQNhsllPWL---TVYQNVELAVKQIAgkkgkawiQEQVNHYLELIQMQHAAHKKPD-----------EISGGMK 144
Cdd:COG4987 410 riAVVPQR----PHLfdtTLRENLRLARPDAT--------DEELWAALERVGLGDWLAALPDgldtwlgeggrRLSGGER 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491592515 145 QRVGIARALALQPKVLLMDEPFGALDALTRAHLQDALMKIQAelNNTVIMITHDvDEAVLLSDKIVMMTNG 215
Cdd:COG4987 478 RRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHR-LAGLERMDRILVLEDG 545
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
3-226 |
1.78e-30 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 116.36 E-value: 1.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 3 KALLDLTRLGMRFPTPDGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMP---TDGGVIVDGREVAGPgPD 79
Cdd:PRK09473 10 DALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNL-PE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 80 R----------AVVFQN--HSLLPWLTVYQNVeLAVKQIAGKKGKAWIQEQVNHYLELIQMQHAaHKK----PDEISGGM 143
Cdd:PRK09473 89 KelnklraeqiSMIFQDpmTSLNPYMRVGEQL-MEVLMLHKGMSKAEAFEESVRMLDAVKMPEA-RKRmkmyPHEFSGGM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 144 KQRVGIARALALQPKVLLMDEPFGALDALTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIGEV 223
Cdd:PRK09473 167 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNA 246
|
...
gi 491592515 224 LEV 226
Cdd:PRK09473 247 RDV 249
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
13-226 |
4.00e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 114.02 E-value: 4.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 13 MRFPTPDGEfIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDR-------AVVFQ 85
Cdd:PRK13639 7 LKYSYPDGT-EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLlevrktvGIVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 86 N---HSLLPwlTVYQNVelAVKQIAGKKGKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLM 162
Cdd:PRK13639 86 NpddQLFAP--TVEEDV--AFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491592515 163 DEPFGALDALTRAhlqdALMKIQAELNN---TVIMITHDVDEAVLLSDKIVMMTNGPAATIGEVLEV 226
Cdd:PRK13639 162 DEPTSGLDPMGAS----QIMKLLYDLNKegiTIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-215 |
8.06e-30 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 111.52 E-value: 8.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 6 LDLTRLGMRFPTPdgefIALKNVDLQINKGEFVsLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREV-AGPGPDRAVVF 84
Cdd:cd03264 1 LQLENLTKRYGKK----RALDGVSLTLGPGMYG-LLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVlKQPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 85 ---QNHSLLPWLTVYQNVE-LAV-KQIAGKKGKAwiqeQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKV 159
Cdd:cd03264 76 ylpQEFGVYPNFTVREFLDyIAWlKGIPSKEVKA----RVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491592515 160 LLMDEPFGALDALTRAHLQDALMKIQAelNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:cd03264 152 LIVDEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKG 205
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
25-215 |
1.05e-29 |
|
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: 112.98 E-value: 1.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDRAVVFQNHSLLpwltVYQ------N 98
Cdd:TIGR02769 27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAFRRDVQL----VFQdspsavN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 99 VELAVKQIAGKK-------GKAWIQEQVNHYLELIQMQ-HAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALD 170
Cdd:TIGR02769 103 PRMTVRQIIGEPlrhltslDESEQKARIAELLDMVGLRsEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 491592515 171 ALTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:TIGR02769 183 MVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKG 227
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
25-215 |
1.13e-29 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 112.10 E-value: 1.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVI-VDGREVAGpgpdrAVVFQ--------NHSLLPWLTV 95
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrLFGERRGG-----EDVWElrkriglvSPALQLRFPR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 96 YQNVELAVkqIAGKKG--------KAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFG 167
Cdd:COG1119 94 DETVLDVV--LSGFFDsiglyrepTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491592515 168 ALDALTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:COG1119 172 GLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDG 219
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
20-215 |
2.90e-29 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 110.84 E-value: 2.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 20 GEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDRAV------VFQNHSLLPWL 93
Cdd:COG0410 14 GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIArlgigyVPEGRRIFPSL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 94 TVYQNVELAVKQIAGKKGKAWIQEQVNHY---LELIQMQHAAhkkpdEISGGMKQRVGIARALALQPKVLLMDEPFGALD 170
Cdd:COG0410 94 TVEENLLLGAYARRDRAEVRADLERVYELfprLKERRRQRAG-----TLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 491592515 171 ALTRAHLQDALMKIQAElNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:COG0410 169 PLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERG 212
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
24-215 |
3.16e-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: 3.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 24 ALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDRAVV---FQNHSLLPWLTVYQNVE 100
Cdd:cd03268 15 VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIgalIEAPGFYPNLTARENLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 101 LAVKQIAGKKgkawiqEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHLQDA 180
Cdd:cd03268 95 LLARLLGIRK------KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELREL 168
|
170 180 190
....*....|....*....|....*....|....*
gi 491592515 181 LMKIQAElNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:cd03268 169 ILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKG 202
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
12-215 |
3.96e-29 |
|
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: 108.84 E-value: 3.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 12 GMRFPTPDGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPD--RAVVFqnhsl 89
Cdd:cd03246 5 NVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNelGDHVG----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 90 lpwlTVYQNVELAVKQIAgkkgkawiqeqvnhyleliqmqhaahkkpDEI-SGGMKQRVGIARALALQPKVLLMDEPFGA 168
Cdd:cd03246 80 ----YLPQDDELFSGSIA-----------------------------ENIlSGGQRQRLGLARALYGNPRILVLDEPNSH 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491592515 169 LDALTRAHLQDALMKIQAElNNTVIMITHDVdEAVLLSDKIVMMTNG 215
Cdd:cd03246 127 LDVEGERALNQAIAALKAA-GATRIVIAHRP-ETLASADRILVLEDG 171
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
15-211 |
4.71e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 111.43 E-value: 4.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 15 FPTPDGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGG---VIVDG-----------REVAGpgpdr 80
Cdd:PRK13640 13 FTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGitltaktvwdiREKVG----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 81 aVVFQN-HSLLPWLTVYQNVELAVKQIAGKKGKawIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKV 159
Cdd:PRK13640 88 -IVFQNpDNQFVGATVGDDVAFGLENRAVPRPE--MIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491592515 160 LLMDEPFGALDALTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVM 211
Cdd:PRK13640 165 IILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVL 216
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-215 |
5.13e-29 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 110.83 E-value: 5.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 1 MEKALLDLTRLGMRFptpdGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGRE-------- 72
Cdd:PRK10619 1 MSENKLNVIDLHKRY----GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTinlvrdkd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 73 ----VAGPGPDR------AVVFQNHSLLPWLTVYQNVELAVKQIAGKKgKAWIQEQVNHYLELIQMQHAAHKK-PDEISG 141
Cdd:PRK10619 77 gqlkVADKNQLRllrtrlTMVFQHFNLWSHMTVLENVMEAPIQVLGLS-KQEARERAVKYLAKVGIDERAQGKyPVHLSG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491592515 142 GMKQRVGIARALALQPKVLLMDEPFGALDA-LTRAHLQdaLMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:PRK10619 156 GQQQRVSIARALAMEPEVLLFDEPTSALDPeLVGEVLR--IMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQG 228
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
6-212 |
1.03e-28 |
|
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: 114.31 E-value: 1.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 6 LDLTRLGMRFPtpdGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDR----- 80
Cdd:TIGR02857 322 LEFSGVSVAYP---GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSwrdqi 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 81 AVVFQNhsllPWL---TVYQNVELAVK-----QIAGKKGKAWIQEQVNhylELIQMQHA-AHKKPDEISGGMKQRVGIAR 151
Cdd:TIGR02857 399 AWVPQH----PFLfagTIAENIRLARPdasdaEIREALERAGLDEFVA---ALPQGLDTpIGEGGAGLSGGQAQRLALAR 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491592515 152 ALALQPKVLLMDEPFGALDALTRAHLQDALMKIQAelNNTVIMITHDvDEAVLLSDKIVMM 212
Cdd:TIGR02857 472 AFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHR-LALAALADRIVVL 529
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
15-215 |
1.17e-28 |
|
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: 108.50 E-value: 1.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 15 FPTPDGEFIaLKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDRAV--VFQN-HSLLP 91
Cdd:cd03226 7 FSYKKGTEI-LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSIgyVMQDvDYQLF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 92 WLTVYQNVELAVKQIAGKkgkawiQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDa 171
Cdd:cd03226 86 TDSVREELLLGLKELDAG------NEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD- 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491592515 172 ltRAHLQD--ALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:cd03226 159 --YKNMERvgELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
21-215 |
2.41e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 109.46 E-value: 2.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 21 EFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVI-----VDGREVAGPGPDRAVVFQN-HSLLPWLT 94
Cdd:PRK13648 21 ASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFynnqaITDDNFEKLRKHIGIVFQNpDNQFVGSI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 95 VYQNVELAVKQIAGKKGKawIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTR 174
Cdd:PRK13648 101 VKYDVAFGLENHAVPYDE--MHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDAR 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 491592515 175 AHLQDALMKIQAELNNTVIMITHDVDEAvLLSDKIVMMTNG 215
Cdd:PRK13648 179 QNLLDLVRKVKSEHNITIISITHDLSEA-MEADHVIVMNKG 218
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
24-215 |
3.85e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 108.67 E-value: 3.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 24 ALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAgPGPDRAV------VFQN-HSLLPWLTVY 96
Cdd:PRK13647 20 ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVN-AENEKWVrskvglVFQDpDDQVFSSTVW 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 97 QNVelAVKQIAGKKGKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTrah 176
Cdd:PRK13647 99 DDV--AFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRG--- 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 491592515 177 lQDALMKIQAELNN---TVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:PRK13647 174 -QETLMEILDRLHNqgkTVIVATHDVDLAAEWADQVIVLKEG 214
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-215 |
4.62e-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: 107.23 E-value: 4.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 2 EKALLDLTRLGMRFPTPDGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGRevagpgpDRA 81
Cdd:cd03220 15 GGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR-------VSS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 82 VVFQNHSLLPWLTVYQNVELaVKQIAGKKGKAwIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLL 161
Cdd:cd03220 88 LLGLGGGFNPELTGRENIYL-NGRLLGLSRKE-IDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491592515 162 MDEPFGALDALTRAHLQDALMKIQAElNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:cd03220 166 IDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKG 218
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
24-227 |
4.89e-28 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 107.94 E-value: 4.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 24 ALKNVDLQINKGEFVSLIGHSGCGKSTVL---NLVAGL--HMPTDGGVIVDGREVAGPGPDR-------AVVFQNHSLLP 91
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLrsiNRMNDLnpEVTITGSIVYNGHNIYSPRTDTvdlrkeiGMVFQQPNPFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 92 wLTVYQNVELAVKqIAGKKGKAWIQEQVNHYLELI----QMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFG 167
Cdd:PRK14239 100 -MSIYENVVYGLR-LKGIKDKQVLDEAVEKSLKGAsiwdEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTS 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 168 ALDALTRAHLQDALMKIQAELnnTVIMITHDVDEAVLLSDKIVMMTNgpaatiGEVLEVN 227
Cdd:PRK14239 178 ALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLD------GDLIEYN 229
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-226 |
5.05e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 108.78 E-value: 5.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 1 MEKALLDLTRLGMRFPtpDGEFiALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREV--AGPG- 77
Cdd:PRK13636 1 MEDYILKVEELNYNYS--DGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdySRKGl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 78 ----PDRAVVFQ--NHSLLPwLTVYQNVELAVKQIagKKGKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIAR 151
Cdd:PRK13636 78 mklrESVGMVFQdpDNQLFS-ASVYQDVSFGAVNL--KLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491592515 152 ALALQPKVLLMDEPFGALDALTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIGEVLEV 226
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
21-240 |
6.51e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 108.57 E-value: 6.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 21 EFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVdGREVAGPG-------PDR---AVVFQ--NHS 88
Cdd:PRK13634 19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGkknkklkPLRkkvGIVFQfpEHQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 89 LLPwLTVYQNVELAVKQIAGKKGKAwiQEQVNHYLELIQMQHAA-HKKPDEISGGMKQRVGIARALALQPKVLLMDEPFG 167
Cdd:PRK13634 98 LFE-ETVEKDICFGPMNFGVSEEDA--KQKAREMIELVGLPEELlARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491592515 168 ALDALTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIGevlevnlpRPRERVALADD 240
Cdd:PRK13634 175 GLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQG--------TPREIFADPDE 239
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
25-201 |
6.54e-28 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 107.42 E-value: 6.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREV----------AGPG--PDRAVVFQNhsllpw 92
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIthlpmhkrarLGIGylPQEASIFRK------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 93 LTVYQNVeLAVKQIAGKKGKAwIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDAL 172
Cdd:COG1137 93 LTVEDNI-LAVLELRKLSKKE-REERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDPI 170
|
170 180 190
....*....|....*....|....*....|..
gi 491592515 173 TRAHLQdalmKIQAEL--NNTVIMIT-HDVDE 201
Cdd:COG1137 171 AVADIQ----KIIRHLkeRGIGVLITdHNVRE 198
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
24-226 |
1.85e-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: 110.66 E-value: 1.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 24 ALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIV----DGREVAGPGPD---RA-----VVFQNHSLLP 91
Cdd:TIGR03269 299 AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPDgrgRAkryigILHQEYDLYP 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 92 WLTVYQNV----------ELAV-KQIAGKKGKAWIQEQVNHYLEliqmqhaahKKPDEISGGMKQRVGIARALALQPKVL 160
Cdd:TIGR03269 379 HRTVLDNLteaiglelpdELARmKAVITLKMVGFDEEKAEEILD---------KYPDELSEGERHRVALAQVLIKEPRIV 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491592515 161 LMDEPFGALDALTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIGEVLEV 226
Cdd:TIGR03269 450 ILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
25-226 |
2.82e-27 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 105.94 E-value: 2.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAG-PGPDRA----VVFQNHSLLPWLTVYQNV 99
Cdd:COG4604 17 LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATtPSRELAkrlaILRQENHINSRLTVRELV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 100 ELavkqiaGK----KGK--AWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDAlt 173
Cdd:COG4604 97 AF------GRfpysKGRltAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDM-- 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491592515 174 rAHLQdALMKI--QA--ELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIGEVLEV 226
Cdd:COG4604 169 -KHSV-QMMKLlrRLadELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
24-212 |
2.94e-27 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 104.24 E-value: 2.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 24 ALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVivdgreVAGPGPDRAVVFQnHSLLPW---LTVYQNVE 100
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV------RRAGGARVAYVPQ-RSEVPDslpLTVRDLVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 101 LAVKQIAGKKGKAWIQEQ--VNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHLQ 178
Cdd:NF040873 80 MGRWARRGLWRRLTRDDRaaVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERII 159
|
170 180 190
....*....|....*....|....*....|....
gi 491592515 179 DALMKIQAElNNTVIMITHDvDEAVLLSDKIVMM 212
Cdd:NF040873 160 ALLAEEHAR-GATVVVVTHD-LELVRRADPCVLL 191
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
3-226 |
3.06e-27 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 107.48 E-value: 3.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 3 KALLDLTRLGMRFPTPDGE---------FIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREV 73
Cdd:PRK15079 6 KVLLEVADLKVHFDIKDGKqwfwqppktLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 74 AGPGPD--RAV------VFQN--HSLLPWLTV----------------YQNVELAVKQIAGKKGkaWIQEQVNHYleliq 127
Cdd:PRK15079 86 LGMKDDewRAVrsdiqmIFQDplASLNPRMTIgeiiaeplrtyhpklsRQEVKDRVKAMMLKVG--LLPNLINRY----- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 128 mqhaahkkPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSD 207
Cdd:PRK15079 159 --------PHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISD 230
|
250
....*....|....*....
gi 491592515 208 KIVMMTNGPAATIGEVLEV 226
Cdd:PRK15079 231 RVLVMYLGHAVELGTYDEV 249
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-215 |
3.61e-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: 104.67 E-value: 3.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 6 LDLTRLGMRFptpdGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDR-AVVF 84
Cdd:cd03269 1 LEVENVTKRF----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRiGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 85 QNHSLLPWLTVyQNVELAVKQIAGKKgKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDE 164
Cdd:cd03269 77 EERGLYPKMKV-IDQLVYLAQLKGLK-KEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491592515 165 PFGALDALTRAHLQDALMKIQAElNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:cd03269 155 PFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKG 204
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-226 |
3.94e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 105.69 E-value: 3.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGL-----HMPTDGGVIVDGREVAGPGPDR-------AVVFQNHSLLPW 92
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVDPievrrevGMVFQYPNPFPH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 93 LTVYQNVELAVKQIAGKKGKAWIQEQVNHYLELI----QMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGA 168
Cdd:PRK14267 100 LTIYDNVAIGVKLNGLVKSKKELDERVEWALKKAalwdEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTAN 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491592515 169 LDALTRAHLQDALMKIQAELnnTVIMITHDVDEAVLLSDKIVMMTNGPAATIGEVLEV 226
Cdd:PRK14267 180 IDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKV 235
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
12-215 |
4.39e-27 |
|
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: 104.59 E-value: 4.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 12 GMRFPTPDGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDG---REVagpgpDRAVVFQNHS 88
Cdd:cd03245 7 NVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdiRQL-----DPADLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 89 LLP---WL---TVYQNVELA-----------VKQIAGkkgkawIQEQVNHYLELIQMQHAAHKkpDEISGGMKQRVGIAR 151
Cdd:cd03245 82 YVPqdvTLfygTLRDNITLGapladderilrAAELAG------VTDFVNKHPNGLDLQIGERG--RGLSGGQRQAVALAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491592515 152 ALALQPKVLLMDEPFGALDALTRAHLQDALMKIQAElnNTVIMITHdvdEAVLLS--DKIVMMTNG 215
Cdd:cd03245 154 ALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGD--KTLIIITH---RPSLLDlvDRIIVMDSG 214
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
21-226 |
5.58e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 106.25 E-value: 5.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 21 EFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDG----------REVAGPGPDRAVVFQnhslL 90
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlkkiKEVKRLRKEIGLVFQ----F 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 91 PWLTVYQNV---ELAVKQIAGKKGKAWIQEQVNHYLELIQM-QHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPF 166
Cdd:PRK13645 99 PEYQLFQETiekDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPT 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 167 GALDALTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIGEVLEV 226
Cdd:PRK13645 179 GGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEI 238
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
25-224 |
9.50e-27 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 104.85 E-value: 9.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAG-PGPD----RAVVFQNHSL-LPWlTVYQN 98
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwSPAElarrRAVLPQHSSLsFPF-TVEEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 99 VELAVkqIAGKKGKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALA------LQPKVLLMDEPFGALDAl 172
Cdd:PRK13548 97 VAMGR--APHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDL- 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491592515 173 trAHlQDALMKIQAEL----NNTVIMITHDVDEAVLLSDKIVMMTNGPAA---TIGEVL 224
Cdd:PRK13548 174 --AH-QHHVLRLARQLaherGLAVIVVLHDLNLAARYADRIVLLHQGRLVadgTPAEVL 229
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
17-215 |
1.09e-26 |
|
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: 103.85 E-value: 1.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 17 TPDGEFIaLKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDR-----AVVFQNhSLLP 91
Cdd:cd03251 11 PGDGPPV-LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlrrqiGLVSQD-VFLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 92 WLTVYQNvelavkqIA-GKKGKAwiQEQVNHYLELIQMQHAAHKKPD-----------EISGGMKQRVGIARALALQPKV 159
Cdd:cd03251 89 NDTVAEN-------IAyGRPGAT--REEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491592515 160 LLMDEPFGALDALTRAHLQDALMKIQAelNNTVIMITHDvdeavlLS-----DKIVMMTNG 215
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMK--NRTTFVIAHR------LStienaDRIVVLEDG 212
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
10-226 |
1.63e-26 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 103.62 E-value: 1.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 10 RLGMRFPTPDGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGReVAgpgpdravvfqnhSL 89
Cdd:COG1134 27 LLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR-VS-------------AL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 90 L-------PWLTVYQNVEL-------AVKQIAGKK---------GKAwIQEQVNHYleliqmqhaahkkpdeiSGGMKQR 146
Cdd:COG1134 93 LelgagfhPELTGRENIYLngrllglSRKEIDEKFdeivefaelGDF-IDQPVKTY-----------------SSGMRAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 147 VGIARALALQPKVLLMDEPFGALDALTRAHLQDALMKIQAElNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIGEVLEV 226
Cdd:COG1134 155 LAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEV 233
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
18-215 |
2.53e-26 |
|
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: 102.95 E-value: 2.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 18 PDGEFIaLKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPD--RA---VVFQNHSLLPw 92
Cdd:cd03252 12 PDGPVI-LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlRRqvgVVLQENVLFN- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 93 LTVYQNVELA-----------VKQIAGkkGKAWIQEQVNHYLELIQMQHAAhkkpdeISGGMKQRVGIARALALQPKVLL 161
Cdd:cd03252 90 RSIRDNIALAdpgmsmervieAAKLAG--AHDFISELPEGYDTIVGEQGAG------LSGGQRQRIAIARALIHNPRILI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491592515 162 MDEPFGALDALTRAHLQDALMKIQAelNNTVIMITHDVdEAVLLSDKIVMMTNG 215
Cdd:cd03252 162 FDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRL-STVKNADRIIVMEKG 212
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-232 |
3.01e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 103.45 E-value: 3.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 20 GEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGL-----HMPTDGGVIVDGREVAGPGP---DRAV--VFQNHSL 89
Cdd:PRK14247 14 GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVielRRRVqmVFQIPNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 90 LPWLTVYQNVELAVKQIAGKKGKAWIQEQVNHYLELIQMQHAAHKKPD----EISGGMKQRVGIARALALQPKVLLMDEP 165
Cdd:PRK14247 94 IPNLSIFENVALGLKLNRLVKSKKELQERVRWALEKAQLWDEVKDRLDapagKLSGGQQQRLCIARALAFQPEVLLADEP 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491592515 166 FGALDALTRAHLQDALMKIQAELnnTVIMITHDVDEAVLLSDKIVMMTNGPAATIGEVLEVnLPRPR 232
Cdd:PRK14247 174 TANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREV-FTNPR 237
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
24-220 |
3.02e-26 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 105.05 E-value: 3.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 24 ALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPD------RAV--VFQN--HSLLPWL 93
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEaqkllrQKIqiVFQNpyGSLNPRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 94 TVYQNVELAVkQIAGKKGKAWIQEQVNHYLELIQM--QHAaHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDA 171
Cdd:PRK11308 110 KVGQILEEPL-LINTSLSAAERREKALAMMAKVGLrpEHY-DRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDV 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491592515 172 LTRAHLQDALMKIQAELNNTVIMITHD--VDEAVlLSDKIVM-----MTNGPAATI 220
Cdd:PRK11308 188 SVQAQVLNLMMDLQQELGLSYVFISHDlsVVEHI-ADEVMVMylgrcVEKGTKEQI 242
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
7-215 |
4.20e-26 |
|
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: 101.47 E-value: 4.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 7 DLTRLGMRFPTPDGEFIaLKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMP--TDGGVIVDGRevagPGPDRAV-- 82
Cdd:cd03213 8 NLTVTVKSSPSKSGKQL-LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGR----PLDKRSFrk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 83 ----VFQNHSLLPWLTVYQNvelavkqiagkkgkawiqeqvnhyleliqMQHAAHKKpdEISGGMKQRVGIARALALQPK 158
Cdd:cd03213 83 iigyVPQDDILHPTLTVRET-----------------------------LMFAAKLR--GLSGGERKRVSIALELVSNPS 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491592515 159 VLLMDEPFGALDALTRAHLQDALMKIqAELNNTVIMITHDV-DEAVLLSDKIVMMTNG 215
Cdd:cd03213 132 LLFLDEPTSGLDSSSALQVMSLLRRL-ADTGRTIICSIHQPsSEIFELFDKLLLLSQG 188
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
19-215 |
5.91e-26 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 101.92 E-value: 5.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 19 DGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDR-----AVVFQNhsllPWL 93
Cdd:cd03254 13 DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlrsmiGVVLQD----TFL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 94 ---TVYQNVELAvKQIAGkkgkawiQEQVNHYLELIQMQHAAHKKPD-----------EISGGMKQRVGIARALALQPKV 159
Cdd:cd03254 89 fsgTIMENIRLG-RPNAT-------DEEVIEAAKEAGAHDFIMKLPNgydtvlgenggNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491592515 160 LLMDEPFGALDALTRAHLQDALMKIQAelNNTVIMITHDVDeAVLLSDKIVMMTNG 215
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLS-TIKNADKILVLDDG 213
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
20-208 |
6.01e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 102.94 E-value: 6.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 20 GEFIALKNVDLQINKGEFVSLIGHSGCGKSTVL-------NLVAGLHMptDGGVIVDGREVAGPGPDRA-------VVFQ 85
Cdd:PRK14243 21 GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlnDLIPGFRV--EGKVTFHGKNLYAPDVDPVevrrrigMVFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 86 NHSLLPwLTVYQNVELAVKqIAGKKGKawIQEQVNHYLELIQMQHAAHKKPDE----ISGGMKQRVGIARALALQPKVLL 161
Cdd:PRK14243 99 KPNPFP-KSIYDNIAYGAR-INGYKGD--MDELVERSLRQAALWDEVKDKLKQsglsLSGGQQQRLCIARAIAVQPEVIL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491592515 162 MDEPFGALDALTRAHLQDaLMKIQAElNNTVIMITHDVDEAVLLSDK 208
Cdd:PRK14243 175 MDEPCSALDPISTLRIEE-LMHELKE-QYTIIIVTHNMQQAARVSDM 219
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
14-215 |
1.02e-25 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 101.46 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 14 RFPT-PDgeFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDR-----AVVFQNH 87
Cdd:cd03249 9 RYPSrPD--VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWlrsqiGLVSQEP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 88 SLLPwLTVYQNVELavkqiaGKKGKawIQEQVnhylELIQMQHAAH----KKPD-----------EISGGMKQRVGIARA 152
Cdd:cd03249 87 VLFD-GTIAENIRY------GKPDA--TDEEV----EEAAKKANIHdfimSLPDgydtlvgergsQLSGGQKQRIAIARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491592515 153 LALQPKVLLMDEPFGALDALTRAHLQDALMKiqAELNNTVIMITHDVdEAVLLSDKIVMMTNG 215
Cdd:cd03249 154 LLRNPKILLLDEATSALDAESEKLVQEALDR--AMKGRTTIVIAHRL-STIRNADLIAVLQNG 213
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
24-215 |
1.71e-25 |
|
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: 99.43 E-value: 1.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 24 ALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDRA----VVF-----QNHSLLPWLT 94
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAiragIAYvpedrKREGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 95 VYQNVELAvkqiagkkgkawiqeqvnHYLeliqmqhaahkkpdeiSGGMKQRVGIARALALQPKVLLMDEPFGALDALTR 174
Cdd:cd03215 95 VAENIALS------------------SLL----------------SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAK 140
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 491592515 175 AHLQDaLMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:cd03215 141 AEIYR-LIRELADAGKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
19-221 |
1.74e-25 |
|
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: 100.77 E-value: 1.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 19 DGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDG-----------REVAGPGPDRAVVFQNh 87
Cdd:cd03253 11 DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdirevtldslRRAIGVVPQDTVLFND- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 88 sllpwlTVYQNVELA------VKQIAGKKgKAWIQEQVnhylelIQMQHAAHKKPDE----ISGGMKQRVGIARALALQP 157
Cdd:cd03253 90 ------TIGYNIRYGrpdatdEEVIEAAK-AAQIHDKI------MRFPDGYDTIVGErglkLSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491592515 158 KVLLMDEPFGALDALTRAHLQDALMKIQAelNNTVIMITHDVDEaVLLSDKIVMMTNGPAATIG 221
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLST-IVNADKIIVLKDGRIVERG 217
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
24-215 |
2.41e-25 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 101.24 E-value: 2.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 24 ALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGL---------HMPTDGGVI-VDGREVAGPGPDRA---VVFQNHSLL 90
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdksagsHIELLGRTVqREGRLARDIRKSRAntgYIFQQFNLV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 91 PWLTVYQNVelavkqIAGKKGKA--------WI-QEQVNHYLELIQ---MQHAAHKKPDEISGGMKQRVGIARALALQPK 158
Cdd:PRK09984 99 NRLSVLENV------LIGALGSTpfwrtcfsWFtREQKQRALQALTrvgMVHFAHQRVSTLSGGQQQRVAIARALMQQAK 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491592515 159 VLLMDEPFGALDALTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:PRK09984 173 VILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQG 229
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-215 |
2.89e-25 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 100.77 E-value: 2.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 1 MEKALLDLTRLGMRFptpdGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGRE------VA 74
Cdd:PRK11701 2 MDQPLLSVRGLTKLY----GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlrdlYA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 75 GPGPDRAVVFQNHsllpWLTVYQN----VELAVKqiAGkkgkAWIQEQ-----VNHYLELiqMQHAAH------------ 133
Cdd:PRK11701 78 LSEAERRRLLRTE----WGFVHQHprdgLRMQVS--AG----GNIGERlmavgARHYGDI--RATAGDwlerveidaari 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 134 -KKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMM 212
Cdd:PRK11701 146 dDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVM 225
|
...
gi 491592515 213 TNG 215
Cdd:PRK11701 226 KQG 228
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
12-207 |
3.34e-25 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 100.99 E-value: 3.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 12 GMRFPTpdGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVagPGPDR----------A 81
Cdd:PRK11831 12 GVSFTR--GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENI--PAMSRsrlytvrkrmS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 82 VVFQNHSLLPWLTVYQNVELAVKQiAGKKGKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLL 161
Cdd:PRK11831 88 MLFQSGALFTDMNVFDNVAYPLRE-HTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIM 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491592515 162 MDEPFGALDALTRAhlqdALMKIQAELNN----TVIMITHDVDEAVLLSD 207
Cdd:PRK11831 167 FDEPFVGQDPITMG----VLVKLISELNSalgvTCVVVSHDVPEVLSIAD 212
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
27-215 |
4.41e-25 |
|
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: 99.75 E-value: 4.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 27 NVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMP----TDGGVIVDGREVAGP---GPDRAVVFQN--HSLLPWLTVYQ 97
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGRPLLPLsirGRHIATIMQNprTAFNPLFTMGN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 98 NVELAVKQIAGKKGKAwiQEQVNHYLELIQMQHAA---HKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTR 174
Cdd:TIGR02770 84 HAIETLRSLGKLSKQA--RALILEALEAVGLPDPEevlKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQ 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 491592515 175 AHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:TIGR02770 162 ARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDG 202
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
3-201 |
7.42e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 99.02 E-value: 7.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 3 KALLDLTRLGMRFptpdGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDR-- 80
Cdd:PRK10247 5 SPLLQLQNVGYLA----GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 81 ---AVVFQNHSLLPwLTVYQNVELAVkQIAGKkgkawiQEQVNHYL-ELIQM---QHAAHKKPDEISGGMKQRVGIARAL 153
Cdd:PRK10247 81 qqvSYCAQTPTLFG-DTVYDNLIFPW-QIRNQ------QPDPAIFLdDLERFalpDTILTKNIAELSGGEKQRISLIRNL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491592515 154 ALQPKVLLMDEPFGALDALTRAHLQDALMKIQAELNNTVIMITHDVDE 201
Cdd:PRK10247 153 QFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE 200
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
24-215 |
1.01e-24 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 98.94 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 24 ALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREvagPGPDR-------AVVFQNHSLLPW-LTV 95
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLV---PWKRRkkflrriGVVFGQKTQLWWdLPV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 96 YQNVELaVKQIAGKKgKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRA 175
Cdd:cd03267 113 IDSFYL-LAAIYDLP-PARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQE 190
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 491592515 176 HLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:cd03267 191 NIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKG 230
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
16-215 |
1.05e-24 |
|
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: 97.93 E-value: 1.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 16 PTPDGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAG-LHmPTDGGVIVDGREvagpgpdrAVVFQNhsllPWL- 93
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGeLE-KLSGSVSVPGSI--------AYVSQE----PWIq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 94 --TVYQNVelavkqIAGKK-GKAWiqeqvnhYLELIqmqHAAHKKPD----------EI-------SGGMKQRVGIARAL 153
Cdd:cd03250 79 ngTIRENI------LFGKPfDEER-------YEKVI---KACALEPDleilpdgdltEIgekginlSGGQKQRISLARAV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491592515 154 ALQPKVLLMDEPFGALDALTRAHL-QDALMKIQAElNNTVIMITHDVdEAVLLSDKIVMMTNG 215
Cdd:cd03250 143 YSDADIYLLDDPLSAVDAHVGRHIfENCILGLLLN-NKTRILVTHQL-QLLPHADQIVVLDNG 203
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
24-215 |
1.34e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 99.43 E-value: 1.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 24 ALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDRAV---------VFQ-NHSLLPWL 93
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIkqirkkvglVFQfPESQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 94 TVYQNVELAVKQIAGKKGKAwiQEQVNHYLELIQM-QHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDAL 172
Cdd:PRK13649 102 TVLKDVAFGPQNFGVSQEEA--EALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPK 179
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 491592515 173 TRAHLQDaLMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:PRK13649 180 GRKELMT-LFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKG 221
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
6-215 |
1.96e-24 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 97.73 E-value: 1.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 6 LDLTRLGMRFPTPDGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGL---HMPTDGGVIVDGREV-AGPGPDR- 80
Cdd:cd03234 4 LPWWDVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRvegGGTTSGQILFNGQPRkPDQFQKCv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 81 AVVFQNHSLLPWLTVYQNVELAVKQIAGKKGKAWIQEQVNHYLELIQM--QHAAHKKPDEISGGMKQRVGIARALALQPK 158
Cdd:cd03234 84 AYVRQDDILLPGLTVRETLTYTAILRLPRKSSDAIRKKRVEDVLLRDLalTRIGGNLVKGISGGERRRVSIAVQLLWDPK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491592515 159 VLLMDEPFGALDALTrAHLqdaLMKIQAEL---NNTVIMITH----DVDEavlLSDKIVMMTNG 215
Cdd:cd03234 164 VLILDEPTSGLDSFT-ALN---LVSTLSQLarrNRIVILTIHqprsDLFR---LFDRILLLSSG 220
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
3-215 |
2.01e-24 |
|
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: 98.36 E-value: 2.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 3 KALLDLTRLGMRFptpdGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGlHMPTDGGVIV----DGREV---AG 75
Cdd:TIGR02323 1 KPLLQVSGLSKSY----GGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAG-RLAPDHGTATyimrSGAELelyQL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 76 PGPDRAVVFQNHsllpWLTVYQN----VELAVKQIA---------GKKGKAWIQEQVNHYLELIQMQHA-AHKKPDEISG 141
Cdd:TIGR02323 76 SEAERRRLMRTE----WGFVHQNprdgLRMRVSAGAnigerlmaiGARHYGNIRATAQDWLEEVEIDPTrIDDLPRAFSG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491592515 142 GMKQRVGIARALALQPKVLLMDEPFGALDALTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:TIGR02323 152 GMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQG 225
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
25-254 |
2.22e-24 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 98.28 E-value: 2.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDRA-------------VVFQNHSLLP 91
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQqkglirqlrqhvgFVFQNFNLFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 92 WLTVYQNV-ELAVkqIAGKKGKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALD 170
Cdd:PRK11264 99 HRTVLENIiEGPV--IVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 171 AltrAHLQDALMKIQ--AELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIGEVlevnlprprerVALADDAQYQKCRQ 248
Cdd:PRK11264 177 P---ELVGEVLNTIRqlAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPA-----------KALFADPQQPRTRQ 242
|
....*.
gi 491592515 249 AVLKFL 254
Cdd:PRK11264 243 FLEKFL 248
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
24-215 |
2.48e-24 |
|
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: 102.40 E-value: 2.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 24 ALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVA----------GPGPDRAVVFQNhsllpwL 93
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIEtnldavrqslGMCPQHNILFHH------L 1018
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 94 TVYQNVeLAVKQIagkKGKAWIQEQVNH--YLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDA 171
Cdd:TIGR01257 1019 TVAEHI-LFYAQL---KGRSWEEAQLEMeaMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDP 1094
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491592515 172 LTRAHLQDALMKIQAelNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:TIGR01257 1095 YSRRSIWDLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIISQG 1136
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
20-215 |
2.52e-24 |
|
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: 97.60 E-value: 2.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 20 GEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDR------AVVFQNHSLLPWL 93
Cdd:TIGR03410 11 GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHEraragiAYVPQGREIFPRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 94 TVYQNVELaVKQIAGKKGKAWIQEQVNHYLELIQMQHaahKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALT 173
Cdd:TIGR03410 91 TVEENLLT-GLAALPRRSRKIPDEIYELFPVLKEMLG---RRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSI 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 491592515 174 RAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:TIGR03410 167 IKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERG 208
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
25-202 |
2.56e-24 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 97.54 E-value: 2.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVA-----GPGPDRA----VVFQNHSLLPWLTV 95
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHqmdeeARAKLRAkhvgFVFQSFMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 96 YQNVELAvkqiAGKKGKAWIQ--EQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALT 173
Cdd:PRK10584 106 LENVELP----ALLRGESSRQsrNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQT 181
|
170 180
....*....|....*....|....*....
gi 491592515 174 RAHLQDALMKIQAELNNTVIMITHDVDEA 202
Cdd:PRK10584 182 GDKIADLLFSLNREHGTTLILVTHDLQLA 210
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
25-199 |
2.71e-24 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 98.61 E-value: 2.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDRAVVFQNHSLLpwltVYQNVELAVK 104
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRDIQM----VFQDSISAVN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 105 qiAGKKGKAWIQEQVNHYLELIQMQHAAH----------------KKPDEISGGMKQRVGIARALALQPKVLLMDEPFGA 168
Cdd:PRK10419 104 --PRKTVREIIREPLRHLLSLDKAERLARasemlravdlddsvldKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSN 181
|
170 180 190
....*....|....*....|....*....|.
gi 491592515 169 LDALTRAHLQDALMKIQAELNNTVIMITHDV 199
Cdd:PRK10419 182 LDLVLQAGVIRLLKKLQQQFGTACLFITHDL 212
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
27-226 |
3.26e-24 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 99.56 E-value: 3.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 27 NVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGR-------EVAGPGPDRAV--VFQNHSLLPWLTVYQ 97
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfdaekGICLPPEKRRIgyVFQDARLFPHYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 98 NVELAVKQIagkkgkawIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHL 177
Cdd:PRK11144 96 NLRYGMAKS--------MVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKREL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491592515 178 QDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIGEVLEV 226
Cdd:PRK11144 168 LPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-198 |
3.68e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 101.29 E-value: 3.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 8 LTRLGMRFptpdGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGpgpdraVVFQNH 87
Cdd:COG0488 1 LENLSKSF----GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIG------YLPQEP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 88 SLLPWLTVYQNVELAVKQI-AGKKGKAWIQEQVNHYLELIQMQHAAH------------------------------KKP 136
Cdd:COG0488 71 PLDDDLTVLDTVLDGDAELrALEAELEELEAKLAEPDEDLERLAELQeefealggweaearaeeilsglgfpeedldRPV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491592515 137 DEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHLQDALmkiqAELNNTVIMITHD 198
Cdd:COG0488 151 SELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFL----KNYPGTVLVVSHD 208
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-241 |
4.78e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 98.26 E-value: 4.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 6 LDLTRLGMRFptpdGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVagpgpDRAVVfq 85
Cdd:COG4152 2 LELKGLTKRF----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL-----DPEDR-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 86 NH--------SLLPWLTVY-QNVELAvkQIAGKKGKAwIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQ 156
Cdd:COG4152 71 RRigylpeerGLYPKMKVGeQLVYLA--RLKGLSKAE-AKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 157 PKVLLMDEPFGALDALTRAHLQDALMkiqaELNN---TVIMITHDVDEAVLLSDKIVMMTNGPAATIGEVLEVN--LPRP 231
Cdd:COG4152 148 PELLILDEPFSGLDPVNVELLKDVIR----ELAAkgtTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRrqFGRN 223
|
250
....*....|
gi 491592515 232 RERVALADDA 241
Cdd:COG4152 224 TLRLEADGDA 233
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
21-215 |
7.29e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 97.54 E-value: 7.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 21 EFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDR---------AVVFQnhslLP 91
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKyirpvrkriGMVFQ----FP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 92 WLTVYQ-NVELAVkqIAGKKGKAWIQEQVNHY-----LELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEP 165
Cdd:PRK13646 95 ESQLFEdTVEREI--IFGPKNFKMNLDEVKNYahrllMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491592515 166 FGALDALTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:PRK13646 173 TAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEG 222
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
4-226 |
1.45e-23 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 97.50 E-value: 1.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 4 ALLDLTRLGMRFPTPDGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLhMPTDGGVIVDGREVAGP------- 76
Cdd:PRK11022 2 ALLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGL-IDYPGRVMAEKLEFNGQdlqrise 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 77 -------GPDRAVVFQN--HSLLPWLTV-YQNVE-LAVKQIAGKKgkaWIQEQVNHYLELIQMQHAAHK---KPDEISGG 142
Cdd:PRK11022 81 kerrnlvGAEVAMIFQDpmTSLNPCYTVgFQIMEaIKVHQGGNKK---TRRQRAIDLLNQVGIPDPASRldvYPHQLSGG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 143 MKQRVGIARALALQPKVLLMDEPFGALDALTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIGE 222
Cdd:PRK11022 158 MSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGK 237
|
....
gi 491592515 223 VLEV 226
Cdd:PRK11022 238 AHDI 241
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-228 |
2.14e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 95.87 E-value: 2.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHmPTDGGVIVDGR-EVAGPGP-DRAV-----------VFQNHSLLP 91
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMN-ELESEVRVEGRvEFFNQNIyERRVnlnrlrrqvsmVHPKPNLFP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 92 wLTVYQNVELAVKqIAGKKGKAWIQEQVNHYLELIQM----QHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFG 167
Cdd:PRK14258 102 -MSVYDNVAYGVK-IVGWRPKLEIDDIVESALKDADLwdeiKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCF 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491592515 168 ALDALTRAHLQDAL--MKIQAELnnTVIMITHDVDEAVLLSDkIVMMTNGPAATIGEVLEVNL 228
Cdd:PRK14258 180 GLDPIASMKVESLIqsLRLRSEL--TMVIVSHNLHQVSRLSD-FTAFFKGNENRIGQLVEFGL 239
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
24-221 |
4.34e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 95.57 E-value: 4.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 24 ALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIV---------DGREVAGPGPDRAVVFQ-NHSLLPWL 93
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivvsstsKQKEIKPVRKKVGVVFQfPESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 94 TVYQNVELAVKQIAGKKGKAwiQEQVNHYLELIQM-QHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDAL 172
Cdd:PRK13643 101 TVLKDVAFGPQNFGIPKEKA--EKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPK 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491592515 173 TRAHLQDALMKIQaELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIG 221
Cdd:PRK13643 179 ARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCG 226
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
21-215 |
6.74e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 94.90 E-value: 6.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 21 EFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDRAV---------VFQ-NHSLL 90
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLkklrkkvslVFQfPEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 91 PWLTVYQNVELAVKQIAGKKGKAwiQEQVNHYLELIQM-QHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGAL 169
Cdd:PRK13641 99 FENTVLKDVEFGPKNFGFSEDEA--KEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491592515 170 DALTRAHLQDALMKIQAElNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:PRK13641 177 DPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHG 221
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
6-226 |
8.15e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 96.45 E-value: 8.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 6 LDLTRLGMRFptpdGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGP-----GPDR 80
Cdd:PRK09536 4 IDVSDLSVEF----GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALsaraaSRRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 81 AVVFQNHSLLPWLTVYQNVELAVKQIAGKKGKAWIQEQ--VNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPK 158
Cdd:PRK09536 80 ASVPQDTSLSFEFDVRQVVEMGRTPHRSRFDTWTETDRaaVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491592515 159 VLLMDEPFGALDaLTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIGEVLEV 226
Cdd:PRK09536 160 VLLLDEPTASLD-INHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV 226
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
25-215 |
1.10e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 94.39 E-value: 1.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPG-----PDRAVVFQN-HSLLPWLTVYQN 98
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENvwnlrRKIGMVFQNpDNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 99 VELAVKQIAGKKGKawIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHLQ 178
Cdd:PRK13642 103 VAFGMENQGIPREE--MIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIM 180
|
170 180 190
....*....|....*....|....*....|....*..
gi 491592515 179 DALMKIQAELNNTVIMITHDVDEAVlLSDKIVMMTNG 215
Cdd:PRK13642 181 RVIHEIKEKYQLTVLSITHDLDEAA-SSDRILVMKAG 216
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-215 |
1.56e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 94.49 E-value: 1.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 1 MEKALLDLTRLGMRFptpdGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGRevagPGPDR 80
Cdd:PRK13537 3 MSVAPIDFRNVEKRY----GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGE----PVPSR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 81 A--------VVFQNHSLLPWLTVYQNVelavkQIAGKK---GKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGI 149
Cdd:PRK13537 75 ArharqrvgVVPQFDNLDPDFTVRENL-----LVFGRYfglSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491592515 150 ARALALQPKVLLMDEPFGALDALTRAHLQDALMKIQAElNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:PRK13537 150 ARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
20-235 |
2.16e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 93.15 E-value: 2.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 20 GEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDRavVFQNHSLLPW-LTVYQN 98
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQ--LARRLALLPQhHLTPEG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 99 VelAVKQIAGKKGKAWI----------QEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGA 168
Cdd:PRK11231 91 I--TVRELVAYGRSPWLslwgrlsaedNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTY 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 169 LDAltrAHlQDALMKIQAELNN---TVIMITHDVDEAVLLSDKIVMMTNGPAATIGEVLEVNLPRPRERV 235
Cdd:PRK11231 169 LDI---NH-QVELMRLMRELNTqgkTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTV 234
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-226 |
3.37e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 92.80 E-value: 3.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGReVAGPGPD------------RAVVFQNHSLLPW 92
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGK-VLYFGKDifqidaiklrkeVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 93 LTVYQNVELAVKQiAGKKGKAWIQEQVNHYLELIQMQHAAHKK----PDEISGGMKQRVGIARALALQPKVLLMDEPFGA 168
Cdd:PRK14246 105 LSIYDNIAYPLKS-HGIKEKREIKKIVEECLRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491592515 169 LDALTRAHLQDALMKIQAELnnTVIMITHDVDEAVLLSDKIVMMTNGPAATIGEVLEV 226
Cdd:PRK14246 184 IDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
20-226 |
5.98e-22 |
|
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: 94.87 E-value: 5.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 20 GEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGL--HMPTDGGVI-----------VDGREVAGP---------- 76
Cdd:TIGR03269 11 DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyVERPSKVGEpcpvcggtle 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 77 -------GPDR----------AVVFQ-NHSLLPWLTVYQNVELAVKQIaGKKGKAWIQEQVNhYLELIQMQHAAHKKPDE 138
Cdd:TIGR03269 91 peevdfwNLSDklrrrirkriAIMLQrTFALYGDDTVLDNVLEALEEI-GYEGKEAVGRAVD-LIEMVQLSHRITHIARD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 139 ISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPAA 218
Cdd:TIGR03269 169 LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEIK 248
|
....*...
gi 491592515 219 TIGEVLEV 226
Cdd:TIGR03269 249 EEGTPDEV 256
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
20-215 |
6.41e-22 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 90.92 E-value: 6.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 20 GEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPG-PDRAVVFQNHSLLPWLTVYQN 98
Cdd:TIGR03740 11 GKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRKDlHKIGSLIESPPLYENLTAREN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 99 VELAVKQIAGKKGKawiqeqVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHLQ 178
Cdd:TIGR03740 91 LKVHTTLLGLPDSR------IDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGLDPIGIQELR 164
|
170 180 190
....*....|....*....|....*....|....*..
gi 491592515 179 DaLMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:TIGR03740 165 E-LIRSFPEQGITVILSSHILSEVQQLADHIGIISEG 200
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
25-226 |
6.55e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 91.99 E-value: 6.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDG-------REVAGPGPDRAVVFQNHSLLPWLT-VY 96
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpldyskRGLLALRQQVATVFQDPEQQIFYTdID 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 97 QNVELAVKQIAgkKGKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAH 176
Cdd:PRK13638 97 SDIAFSLRNLG--VPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491592515 177 LQDALMKIQAElNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIGEVLEV 226
Cdd:PRK13638 175 MIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEV 223
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
24-226 |
7.26e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 94.47 E-value: 7.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 24 ALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDRA------VVFQNHSLLPWLTVYQ 97
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAaqlgigIIYQELSVIDELTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 98 NV---ELAVKQIAGKKGKAW--IQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPfgaLDAL 172
Cdd:PRK09700 100 NLyigRHLTKKVCGVNIIDWreMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEP---TSSL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491592515 173 TRAHLqDALMKIQAELNN---TVIMITHDVDEAVLLSDKIVMMTNGPAATIGEVLEV 226
Cdd:PRK09700 177 TNKEV-DYLFLIMNQLRKegtAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-221 |
8.71e-22 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 94.54 E-value: 8.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 3 KALLDLTRLGMRFPTPDG-------EFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAG 75
Cdd:PRK10261 311 EPILQVRNLVTRFPLRSGllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDT 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 76 PGP--------DRAVVFQN--HSLLPWLTV-YQNVE-LAVKQI----AGKKGKAWIQEQVNhylelIQMQHAAhKKPDEI 139
Cdd:PRK10261 391 LSPgklqalrrDIQFIFQDpyASLDPRQTVgDSIMEpLRVHGLlpgkAAAARVAWLLERVG-----LLPEHAW-RYPHEF 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 140 SGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPAAT 219
Cdd:PRK10261 465 SGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVE 544
|
..
gi 491592515 220 IG 221
Cdd:PRK10261 545 IG 546
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-215 |
1.43e-21 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 90.32 E-value: 1.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 1 MEKALLDLTRLGMRFptpdGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDR 80
Cdd:PRK11614 1 MEKVMLSFDKVSAHY----GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 81 ------AVVFQNHSLLPWLTVYQNveLAVKQIAGKKGKawIQEQVNHYLELI-QMQHAAHKKPDEISGGMKQRVGIARAL 153
Cdd:PRK11614 77 imreavAIVPEGRRVFSRMTVEEN--LAMGGFFAERDQ--FQERIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491592515 154 ALQPKVLLMDEPFGALDALTRAHLQDALMKIQAElNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:PRK11614 153 MSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENG 213
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
17-215 |
1.72e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 93.76 E-value: 1.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 17 TPDGEfIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLhMPTDGGVIVDGREVAGPGPDR-----AVVFQNhSLLP 91
Cdd:PRK11174 359 SPDGK-TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELDPESwrkhlSWVGQN-PQLP 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 92 WLTVYQNVELAVKQIAgkkgkawiQEQVNHYLELIQMQHAAHKKPD-----------EISGGMKQRVGIARALALQPKVL 160
Cdd:PRK11174 436 HGTLRDNVLLGNPDAS--------DEQLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLL 507
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491592515 161 LMDEPFGALDALTRAHLQDALMkiQAELNNTVIMITHDVDEavLLS-DKIVMMTNG 215
Cdd:PRK11174 508 LLDEPTASLDAHSEQLVMQALN--AASRRQTTLMVTHQLED--LAQwDQIWVMQDG 559
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
3-225 |
2.72e-21 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 92.89 E-value: 2.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 3 KALLDLTRLGMRfpTPDGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDRav 82
Cdd:COG4618 328 KGRLSVENLTVV--PPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREE-- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 83 vFQNH--------SLLPWlTVYQNV--------ELAVK--QIAGkkgkawiqeqVnHylELIQmqhaahKKPD----EI- 139
Cdd:COG4618 404 -LGRHigylpqdvELFDG-TIAENIarfgdadpEKVVAaaKLAG----------V-H--EMIL------RLPDgydtRIg 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 140 ------SGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHLQDALMKIQAElNNTVIMITHDVdeAVL-LSDKIVMM 212
Cdd:COG4618 463 eggarlSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRP--SLLaAVDKLLVL 539
|
250
....*....|....*.
gi 491592515 213 TNGPAATIG---EVLE 225
Cdd:COG4618 540 RDGRVQAFGprdEVLA 555
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
5-198 |
3.52e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 92.85 E-value: 3.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 5 LLDLTRLGMRFPTPDGEF-------IALKNVDLQINKGEFVSLIGHSGCGKST----VLNLVAglhmpTDGGVIVDGREV 73
Cdd:PRK15134 275 LLDVEQLQVAFPIRKGILkrtvdhnVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 74 AGPGPDR--------AVVFQ--NHSLLPWLTVYQNVE--LAVKQiaGKKGKAWIQEQVNHYLELIQMQHAA-HKKPDEIS 140
Cdd:PRK15134 350 HNLNRRQllpvrhriQVVFQdpNSSLNPRLNVLQIIEegLRVHQ--PTLSAAQREQQVIAVMEEVGLDPETrHRYPAEFS 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491592515 141 GGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHLQDALMKIQAELNNTVIMITHD 198
Cdd:PRK15134 428 GGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHD 485
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
7-198 |
4.25e-21 |
|
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: 92.42 E-value: 4.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 7 DLTRLGMRFPTPDGEfIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPD----RAV 82
Cdd:TIGR02868 334 TLELRDLSAGYPGAP-PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDevrrRVS 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 83 VFQNHSLLPWLTVYQNVELAVKQIAGKKGKA---------WIQEqVNHYLELIQMQHAAhkkpdEISGGMKQRVGIARAL 153
Cdd:TIGR02868 413 VCAQDAHLFDTTVRENLRLARPDATDEELWAalervgladWLRA-LPDGLDTVLGEGGA-----RLSGGERQRLALARAL 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 491592515 154 ALQPKVLLMDEPFGALDALTRAHLQDALMKIQAELnnTVIMITHD 198
Cdd:TIGR02868 487 LADAPILLLDEPTEHLDAETADELLEDLLAALSGR--TVVLITHH 529
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
12-215 |
5.22e-21 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 92.34 E-value: 5.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 12 GMRFPTPDGEFiALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDRavvFQNHsllp 91
Cdd:PRK10522 327 NVTFAYQDNGF-SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPED---YRKL---- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 92 WLTVYQNVELaVKQIAGKKGKAWIQEQVNHYLELIQMQHAAHKKPDEI-----SGGMKQRVGIARALALQPKVLLMDEPF 166
Cdd:PRK10522 399 FSAVFTDFHL-FDQLLGPEGKPANPALVEKWLERLKMAHKLELEDGRIsnlklSKGQKKRLALLLALAEERDILLLDEWA 477
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491592515 167 GALDALTRAHLQDALMKIQAELNNTVIMITHDvDEAVLLSDKIVMMTNG 215
Cdd:PRK10522 478 ADQDPHFRREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNG 525
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
24-215 |
5.35e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 92.00 E-value: 5.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 24 ALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDRA----VVF-----QNHSLLPWLT 94
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAiragIAYvpedrKGEGLVLDLS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 95 VYQNVELAVKQIAGKKG---KAWIQEQVNHYLELIQMQHAAHKKP-DEISGGMKQRVGIARALALQPKVLLMDEPFGALD 170
Cdd:COG1129 347 IRENITLASLDRLSRGGlldRRRERALAEEYIKRLRIKTPSPEQPvGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGID 426
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 491592515 171 ALTRAHLQDaLMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:COG1129 427 VGAKAEIYR-LIRELAAEGKAVIVISSELPELLGLSDRILVMREG 470
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
15-215 |
6.71e-21 |
|
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: 86.98 E-value: 6.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 15 FPTPDGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDR----AVVFQNhsll 90
Cdd:cd03247 8 FSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALssliSVLNQR---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 91 PWL---TVYQNVelavkqiaGKKgkawiqeqvnhyleliqmqhaahkkpdeISGGMKQRVGIARALALQPKVLLMDEPFG 167
Cdd:cd03247 84 PYLfdtTLRNNL--------GRR----------------------------FSGGERQRLALARILLQDAPIVLLDEPTV 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491592515 168 ALDALTRAHLQDALMKiQAElNNTVIMITHDVdEAVLLSDKIVMMTNG 215
Cdd:cd03247 128 GLDPITERQLLSLIFE-VLK-DKTLIWITHHL-TGIEHMDKILFLENG 172
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
18-222 |
9.75e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 88.89 E-value: 9.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 18 PDGEfIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDRAV------VFQN-HSLL 90
Cdd:PRK13644 12 PDGT-PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIrklvgiVFQNpETQF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 91 PWLTVYQNVELAVKQIAGKKGKawIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALD 170
Cdd:PRK13644 91 VGRTVEEDLAFGPENLCLPPIE--IRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491592515 171 ALTRAHLQDALMKIQaELNNTVIMITHDVDEaVLLSDKIVMMTNGPAATIGE 222
Cdd:PRK13644 169 PDSGIAVLERIKKLH-EKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGE 218
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
25-240 |
1.58e-20 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 87.64 E-value: 1.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLhMPTDGG-VIVDGREVA-GPGPDRA-----VVFQNHSLLPWLTVYQ 97
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGI-VPRDAGnIIIDDEDISlLPLHARArrgigYLPQEASIFRRLSVYD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 98 NVeLAVKQIAGKKGKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHL 177
Cdd:PRK10895 98 NL-MAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDI 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491592515 178 QdalmKIQAELNNT---VIMITHDVDEAVLLSDKIVMMTNGPAATIGEVLEVNLPRPRERVALADD 240
Cdd:PRK10895 177 K----RIIEHLRDSglgVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYLGED 238
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
5-226 |
2.38e-20 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 90.30 E-value: 2.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 5 LLDLTRLGMRFPTPDGEFIALKNVDLQINKGEFVSLIGHSGCGKS-TVLNLV-----AGLHMPTDGGV-------IVDGR 71
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMrlleqAGGLVQCDKMLlrrrsrqVIELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 72 EVAGP------GPDRAVVFQN--HSLLPWLTVYQNVELAVKQIAGKKGKAWIQEqVNHYLELIQM---QHAAHKKPDEIS 140
Cdd:PRK10261 92 EQSAAqmrhvrGADMAMIFQEpmTSLNPVFTVGEQIAESIRLHQGASREEAMVE-AKRMLDQVRIpeaQTILSRYPHQLS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 141 GGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATI 220
Cdd:PRK10261 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVET 250
|
....*.
gi 491592515 221 GEVLEV 226
Cdd:PRK10261 251 GSVEQI 256
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
24-226 |
3.11e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 87.55 E-value: 3.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 24 ALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDR-----AVVFQN---HSLLPwlTV 95
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREvrkfvGLVFQNpddQIFSP--TV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 96 YQNVelAVKQIAGKKGKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRA 175
Cdd:PRK13652 97 EQDI--AFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVK 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491592515 176 HLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIGEVLEV 226
Cdd:PRK13652 175 ELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
24-215 |
3.47e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 88.22 E-value: 3.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 24 ALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREvagPGPDR-------AVVFQNHSLLPW-LTV 95
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYV---PFKRRkefarriGVVFGQRSQLWWdLPA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 96 YQNVEL--AVKQIagkkGKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALT 173
Cdd:COG4586 114 IDSFRLlkAIYRI----PDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVS 189
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 491592515 174 RAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:COG4586 190 KEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHG 231
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
20-237 |
3.50e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 88.35 E-value: 3.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 20 GEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVagpgPDRA--------VVFQNHSLLP 91
Cdd:PRK13536 52 GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV----PARArlararigVVPQFDNLDL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 92 WLTVYQNVeLAVKQIAGKKGKAwIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDA 171
Cdd:PRK13536 128 EFTVRENL-LVFGRYFGMSTRE-IEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDP 205
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491592515 172 LTRAHLQDALMKIQAeLNNTVIMITHDVDEAVLLSDKIVMMTNG-------PAATIGE-----VLEVNLPRPRERVAL 237
Cdd:PRK13536 206 HARHLIWERLRSLLA-RGKTILLTTHFMEEAERLCDRLCVLEAGrkiaegrPHALIDEhigcqVIEIYGGDPHELSSL 282
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
24-215 |
3.98e-20 |
|
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: 86.33 E-value: 3.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 24 ALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIV--DGREV----AGPgpdRAV----------VFQNH 87
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVdlaqASP---REIlalrrrtigyVSQFL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 88 SLLPWLTVYQNV-----ELAV-KQIAGKKGKAWIqeqvnHYLELiqMQHAAHKKPDEISGGMKQRVGIARALALQPKVLL 161
Cdd:COG4778 103 RVIPRVSALDVVaepllERGVdREEARARARELL-----ARLNL--PERLWDLPPATFSGGEQQRVNIARGFIADPPLLL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491592515 162 MDEPFGALDALTRAHLQDALMKIQAElNNTVIMITHDVD--EAVllSDKIVMMTNG 215
Cdd:COG4778 176 LDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEvrEAV--ADRVVDVTPF 228
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
21-215 |
5.58e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 87.45 E-value: 5.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 21 EFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGV-----------------IVDGREVAGPGPDR--- 80
Cdd:PRK13651 19 ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekeKVLEKLVIQKTRFKkik 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 81 ---------AVVFQnhsllpwLTVYQNVELAV-KQIA------GKKgKAWIQEQVNHYLELIQM-QHAAHKKPDEISGGM 143
Cdd:PRK13651 99 kikeirrrvGVVFQ-------FAEYQLFEQTIeKDIIfgpvsmGVS-KEEAKKRAAKYIELVGLdESYLQRSPFELSGGQ 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491592515 144 KQRVGIARALALQPKVLLMDEPFGALDaltrAHLQDALMKIQAELNN---TVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:PRK13651 171 KRRVALAGILAMEPDFLVFDEPTAGLD----PQGVKEILEIFDNLNKqgkTIILVTHDLDNVLEWTKRTIFFKDG 241
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
20-197 |
6.39e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 85.31 E-value: 6.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 20 GEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDRAVVFQNHS--LLPWLTVYQ 97
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGHRnaMKPALTVAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 98 NVELAvkqiAGKKGKAwiQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHL 177
Cdd:PRK13539 93 NLEFW----AAFLGGE--ELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALF 166
|
170 180
....*....|....*....|
gi 491592515 178 QDaLMKIQAELNNTVIMITH 197
Cdd:PRK13539 167 AE-LIRAHLAQGGIVIAATH 185
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
4-212 |
2.11e-19 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 86.11 E-value: 2.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 4 ALLDLTRLGMRFPTPDGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPT-----D----GGV------IV 68
Cdd:COG4170 2 PLLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtaDrfrwNGIdllklsPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 69 DGREVAGPgpDRAVVFQN--HSLLPWLTVYQNVELAVKQIAGKkGKAWiQEQVNHYLELIQMQHAA----HKK-----PD 137
Cdd:COG4170 82 ERRKIIGR--EIAMIFQEpsSCLDPSAKIGDQLIEAIPSWTFK-GKWW-QRFKWRKKRAIELLHRVgikdHKDimnsyPH 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491592515 138 EISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHLQDALMKIqAELNNTVIM-ITHDVDEAVLLSDKIVMM 212
Cdd:COG4170 158 ELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARL-NQLQGTSILlISHDLESISQWADTITVL 232
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
21-226 |
2.66e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 85.67 E-value: 2.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 21 EFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGV----------IVDGREVAGPGPDR---------- 80
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiyigdkKNNHELITNPYSKKiknfkelrrr 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 81 -AVVFQnhslLPWLTVYQNV---ELAVKQIAGKKGKAWIQEQVNHYLELIQMQHA-AHKKPDEISGGMKQRVGIARALAL 155
Cdd:PRK13631 118 vSMVFQ----FPEYQLFKDTiekDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSyLERSPFGLSGGQKRRVAIAGILAI 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491592515 156 QPKVLLMDEPFGALDALTRAHLQDALMKIQAElNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIGEVLEV 226
Cdd:PRK13631 194 QPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEI 263
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-215 |
4.04e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 86.68 E-value: 4.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 1 MEKALLDLTRLGMRFPTPDGEFIALKNVDLQINKGEFVSLIGHSGCGKS-TVLNLVAGLHMP----TDGGVIVDG----- 70
Cdd:PRK15134 1 MTQPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGesllh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 71 ---REVAGPGPDR-AVVFQNH--SLLPwltvYQNVElavKQIA-------GKKGKAWIQEQVNhYLELIQMQHAAHKK-- 135
Cdd:PRK15134 81 aseQTLRGVRGNKiAMIFQEPmvSLNP----LHTLE---KQLYevlslhrGMRREAARGEILN-CLDRVGIRQAAKRLtd 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 136 -PDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTN 214
Cdd:PRK15134 153 yPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQN 232
|
.
gi 491592515 215 G 215
Cdd:PRK15134 233 G 233
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
24-226 |
5.98e-19 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 84.07 E-value: 5.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 24 ALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVA-GPGPDRA----VVFQN--HSLLPWLTVY 96
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfGDYSYRSqrirMIFQDpsTSLNPRQRIS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 97 QNVELAVKQIAGKKGKAWiQEQVNHYLELIQM--QHAAHKkPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTR 174
Cdd:PRK15112 108 QILDFPLRLNTDLEPEQR-EKQIIETLRQVGLlpDHASYY-PHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMR 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491592515 175 AHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIGEVLEV 226
Cdd:PRK15112 186 SQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADV 237
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
20-178 |
8.68e-19 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 82.02 E-value: 8.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 20 GEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVA--GPGPDRAVVFQNHS--LLPWLTV 95
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAeqRDEPHENILYLGHLpgLKPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 96 YQNVELAVKQIAGKKGKAWiqeqvnHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALD----- 170
Cdd:TIGR01189 91 LENLHFWAAIHGGAQRTIE------DALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDkagva 164
|
170
....*....|.
gi 491592515 171 ---ALTRAHLQ 178
Cdd:TIGR01189 165 llaGLLRAHLA 175
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
25-197 |
1.06e-18 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 85.54 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPG-----PDRAVVFQNHSLLPwLTVYQNV 99
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLShsvlrQGVAMVQQDPVVLA-DTFLANV 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 100 ELavkqiagkkGKAWIQEQVNHYLELIQMQHAAHKKPDEI-----------SGGMKQRVGIARALALQPKVLLMDEPFGA 168
Cdd:PRK10790 436 TL---------GRDISEEQVWQALETVQLAELARSLPDGLytplgeqgnnlSVGQKQLLALARVLVQTPQILILDEATAN 506
|
170 180
....*....|....*....|....*....
gi 491592515 169 LDALTRAHLQDALMKIQAelNNTVIMITH 197
Cdd:PRK10790 507 IDSGTEQAIQQALAAVRE--HTTLVVIAH 533
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-215 |
1.10e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 85.26 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 2 EKALLDLTRLgmRFPTPDGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPD-- 79
Cdd:PRK11160 335 DQVSLTLNNV--SFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAal 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 80 RA---VVFQ-----NHSL-------LP------WLTVYQNVELAvKQIAGKKG-KAWIQE---Qvnhyleliqmqhaahk 134
Cdd:PRK11160 413 RQaisVVSQrvhlfSATLrdnlllaAPnasdeaLIEVLQQVGLE-KLLEDDKGlNAWLGEggrQ---------------- 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 135 kpdeISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHLQDALMKIQAelNNTVIMITHdvdEAVLLS--DKIVMM 212
Cdd:PRK11160 476 ----LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITH---RLTGLEqfDRICVM 546
|
...
gi 491592515 213 TNG 215
Cdd:PRK11160 547 DNG 549
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
25-198 |
2.52e-18 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 79.41 E-value: 2.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGgvivdgrevagpgpdravvfqnhsllpWLTVYQNVELAvk 104
Cdd:cd03221 16 LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEG---------------------------IVTWGSTVKIG-- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 105 qiagkkgkawiqeqvnhYLEliQMqhaahkkpdeiSGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHLQDALmki 184
Cdd:cd03221 67 -----------------YFE--QL-----------SGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEAL--- 113
|
170
....*....|....
gi 491592515 185 qAELNNTVIMITHD 198
Cdd:cd03221 114 -KEYPGTVILVSHD 126
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
24-215 |
2.66e-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: 81.00 E-value: 2.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 24 ALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDR-----AVVFQNhsllPWL---TV 95
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDlrsriSIIPQD----PVLfsgTI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 96 YQNVELavkqiagkkGKAWIQEQVNHYLELIQMQHAAHKKPDEI-----------SGGMKQRVGIARALALQPKVLLMDE 164
Cdd:cd03244 95 RSNLDP---------FGEYSDEELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARALLRKSKILVLDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491592515 165 PFGALDALTRAHLQDALMKIQAelNNTVIMITHDVDeAVLLSDKIVMMTNG 215
Cdd:cd03244 166 ATASVDPETDALIQKTIREAFK--DCTVLTIAHRLD-TIIDSDRILVLDKG 213
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
25-215 |
2.67e-18 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 81.36 E-value: 2.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGRevagPGPDR---------AVVFQNHSLLPwLTV 95
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGK----PISQYehkylhskvSLVGQEPVLFA-RSL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 96 YQNVELAVKQIAGKKGKAWIQEQVNHYLeLIQMQHA----AHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDA 171
Cdd:cd03248 105 QDNIAYGLQSCSFECVKEAAQKAHAHSF-ISELASGydteVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDA 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491592515 172 LTRAHLQDALMkiQAELNNTVIMITHDVdEAVLLSDKIVMMTNG 215
Cdd:cd03248 184 ESEQQVQQALY--DWPERRTVLVIAHRL-STVERADQILVLDGG 224
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
15-197 |
6.34e-18 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 83.14 E-value: 6.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 15 FPTPDGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREV-----AGPGPDRAVVFQNHSL 89
Cdd:PRK11176 349 FTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLrdytlASLRNQVALVSQNVHL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 90 LPwLTVYQNVELAVKqiaGKKGKAWIQE--QVNHYLELI-QMQHAAHKKPDE----ISGGMKQRVGIARALALQPKVLLM 162
Cdd:PRK11176 429 FN-DTIANNIAYART---EQYSREQIEEaaRMAYAMDFInKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRDSPILIL 504
|
170 180 190
....*....|....*....|....*....|....*
gi 491592515 163 DEPFGALDALTRAHLQDALMKIQAelNNTVIMITH 197
Cdd:PRK11176 505 DEATSALDTESERAIQAALDELQK--NRTSLVIAH 537
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
20-235 |
6.58e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 81.19 E-value: 6.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 20 GEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREV---AGPGPDRAV--VFQNHSLLPWLT 94
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIqhyASKEVARRIglLAQNATTPGDIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 95 VYQNVELA--VKQIAGKKGKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDAL 172
Cdd:PRK10253 98 VQELVARGryPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIS 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491592515 173 TRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIGEVLEVNLPRPRERV 235
Cdd:PRK10253 178 HQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERI 240
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
26-236 |
8.14e-18 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 80.51 E-value: 8.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 26 KNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMP----TDGGVIVDGREVAG---PGPDRAVVFQN--HSLLPWLTVY 96
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPcalRGRKIATIMQNprSAFNPLHTMH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 97 QNVELAVKQIagkkGKAWIQEQVNHYLELIQMQHAA---HKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALT 173
Cdd:PRK10418 100 THARETCLAL----GKPADDATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVA 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491592515 174 RAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIGEVLEVnLPRPRERVA 236
Cdd:PRK10418 176 QARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL-FNAPKHAVT 237
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
35-225 |
1.06e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 80.60 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 35 GEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPD---RAVVFQNHSLLP--WLTVYQNVELAVKQIAGK 109
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKafaRKVAYLPQQLPAaeGMTVRELVAIGRYPWHGA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 110 KGK--AWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDAltrAHLQDALMKIQ-- 185
Cdd:PRK10575 117 LGRfgAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDI---AHQVDVLALVHrl 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491592515 186 -AELNNTVIMITHDVDEAVLLSDKIV------MMTNGPAATI--GEVLE 225
Cdd:PRK10575 194 sQERGLTVIAVLHDINMAARYCDYLValrggeMIAQGTPAELmrGETLE 242
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
17-197 |
1.10e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 82.55 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 17 TPDGEFIaLKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVdgrevagPGPDRAVVFQNHSLLPWLT-- 94
Cdd:COG4178 372 TPDGRPL-LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR-------PAGARVLFLPQRPYLPLGTlr 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 95 ---VYQNVELAVKQiagkkgkawiqEQVNHYLELIQMQHAAHKkPDEI-------SGGMKQRVGIARALALQPKVLLMDE 164
Cdd:COG4178 444 ealLYPATAEAFSD-----------AELREALEAVGLGHLAER-LDEEadwdqvlSLGEQQRLAFARLLLHKPDWLFLDE 511
|
170 180 190
....*....|....*....|....*....|....
gi 491592515 165 PFGALDALTRAHLqdaLMKIQAELNN-TVIMITH 197
Cdd:COG4178 512 ATSALDEENEAAL---YQLLREELPGtTVISVGH 542
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
25-226 |
1.34e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 79.88 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHmPTDGGVIVDGREVAG-PGPD----RAVVFQNHSLLPWLTVYQNV 99
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDwSAAElarhRAYLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 100 ELAVkqiAGKKGKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALaLQ--------PKVLLMDEPFGALDA 171
Cdd:COG4138 91 ALHQ---PAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVL-LQvwptinpeGQLLLLDEPMNSLDV 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491592515 172 LTRAHLQDALMKIqAELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIGEVLEV 226
Cdd:COG4138 167 AQQAALDRLLREL-CQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEV 220
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
12-215 |
3.98e-17 |
|
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: 80.92 E-value: 3.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 12 GMRFPTPDGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAgpgpD-RAVVFQNHSLL 90
Cdd:TIGR02203 335 NVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLA----DyTLASLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 91 pwltVYQNVEL----AVKQIAGKKGKAWIQEQVNHYLELIQMQHAAHKKPDEI-----------SGGMKQRVGIARALAL 155
Cdd:TIGR02203 411 ----VSQDVVLfndtIANNIAYGRTEQADRAEIERALAAAYAQDFVDKLPLGLdtpigengvllSGGQRQRLAIARALLK 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 156 QPKVLLMDEPFGALDALTRAHLQDALMKIQAelNNTVIMITHDVdEAVLLSDKIVMMTNG 215
Cdd:TIGR02203 487 DAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRL-STIEKADRIVVMDDG 543
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
25-197 |
4.21e-17 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 80.92 E-value: 4.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDG------------REVAGPGPDrAVVFQ---NHSL 89
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGvplvqydhhylhRQVALVGQE-PVLFSgsvRENI 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 90 LPWLTVYQNVE-LAVKQIAGkkGKAWIQEQVNHYLELIQmqhaahKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGA 168
Cdd:TIGR00958 576 AYGLTDTPDEEiMAAAKAAN--AHDFIMEFPNGYDTEVG------EKGSQLSGGQKQRIAIARALVRKPRVLILDEATSA 647
|
170 180
....*....|....*....|....*....
gi 491592515 169 LDALTRAHLQDAlmKIQAELnnTVIMITH 197
Cdd:TIGR00958 648 LDAECEQLLQES--RSRASR--TVLLIAH 672
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-215 |
5.57e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 80.49 E-value: 5.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 5 LLDLTRLGMRFptpDGEFIaLKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVdgrevaGPGPDRAVVF 84
Cdd:COG0488 315 VLELEGLSKSY---GDKTL-LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL------GETVKIGYFD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 85 QNHSLL-PWLTVYQNvelaVKQIAGKKGkawiQEQVNHYLEliQM---QHAAHKKPDEISGGMKQRVGIARALALQPKVL 160
Cdd:COG0488 385 QHQEELdPDKTVLDE----LRDGAPGGT----EQEVRGYLG--RFlfsGDDAFKPVGVLSGGEKARLALAKLLLSPPNVL 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491592515 161 LMDEPFGALDALTRAHLQDALmkiqAELNNTVIMITHD---VDEavlLSDKIVMMTNG 215
Cdd:COG0488 455 LLDEPTNHLDIETLEALEEAL----DDFPGTVLLVSHDryfLDR---VATRILEFEDG 505
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-222 |
1.03e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 79.59 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 1 MEKALLDLTRLGMRFPTpdgeFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGL--HMPTDGGVIVDGREVAGPG- 77
Cdd:PRK13549 1 MMEYLLEMKNITKTFGG----VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEELQASNi 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 78 --PDRA---VVFQNHSLLPWLTVYQNVELavkqiagkkGKAWIQEQVNHY----------LELIQMQHAAHKKPDEISGG 142
Cdd:PRK13549 77 rdTERAgiaIIHQELALVKELSVLENIFL---------GNEITPGGIMDYdamylraqklLAQLKLDINPATPVGNLGLG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 143 MKQRVGIARALALQPKVLLMDEPFGALDALTRAHLQDALMKIQAElNNTVIMITHDVDEAVLLSDKIVMMTNG------P 216
Cdd:PRK13549 148 QQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGrhigtrP 226
|
....*.
gi 491592515 217 AATIGE 222
Cdd:PRK13549 227 AAGMTE 232
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
11-215 |
2.03e-16 |
|
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: 78.71 E-value: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 11 LGMRFPTPD-GEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGL--HMPTDGGVIVDGREVAGPG---PDRA--- 81
Cdd:TIGR02633 2 LEMKGIVKTfGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASNirdTERAgiv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 82 VVFQNHSLLPWLTVYQNVELAvKQIAGKKGKAWIQEQVNHYLELIQmQHAAHKKPD-----EISGGMKQRVGIARALALQ 156
Cdd:TIGR02633 82 IIHQELTLVPELSVAENIFLG-NEITLPGGRMAYNAMYLRAKNLLR-ELQLDADNVtrpvgDYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491592515 157 PKVLLMDEPFGALDALTRAHLQDALMKIQAElNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:TIGR02633 160 ARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
25-211 |
2.08e-16 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 76.26 E-value: 2.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGL--HMPTDGGVIVDGREVAGPGPD-RA-----VVFQNHSLLPWLTVY 96
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSPDeRAragifLAFQYPVEIPGVSVS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 97 QNVELAVKQIAGKKGKAWI-QEQVNHYLELIQMQHAAHKKP--DEISGGMKQRVGIARALALQPKVLLMDEPFGALDAlt 173
Cdd:COG0396 96 NFLRTALNARRGEELSAREfLKLLKEKMKELGLDEDFLDRYvnEGFSGGEKKRNEILQMLLLEPKLAILDETDSGLDI-- 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491592515 174 rahlqDALmKIQAEL-------NNTVIMITH--------DVDEAVLLSD-KIVM 211
Cdd:COG0396 174 -----DAL-RIVAEGvnklrspDRGILIITHyqrildyiKPDFVHVLVDgRIVK 221
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
4-215 |
3.37e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 78.03 E-value: 3.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 4 ALLDLTRLGMRFPTpdgeFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREV---------- 73
Cdd:PRK11288 3 PYLSFDGIGKTFPG----VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfasttaala 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 74 AGPgpdrAVVFQNHSLLPWLTVYQNVELAvkQIAGKKG---KAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIA 150
Cdd:PRK11288 79 AGV----AIIYQELHLVPEMTVAENLYLG--QLPHKGGivnRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491592515 151 RALALQPKVLLMDEPFGALDAltRAhlQDALMKIQAEL--NNTVIM-ITHDVDEAVLLSDKIVMMTNG 215
Cdd:PRK11288 153 KALARNARVIAFDEPTSSLSA--RE--IEQLFRVIRELraEGRVILyVSHRMEEIFALCDAITVFKDG 216
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
25-215 |
3.88e-16 |
|
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: 75.45 E-value: 3.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDRAVVFQNHSLL-----PWL---TVY 96
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAyaaqkPWLlnaTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 97 QNVELAvKQIAGKKGKAWIQE-QVNHYLELIQM--QHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALT 173
Cdd:cd03290 97 ENITFG-SPFNKQRYKAVTDAcSLQPDIDLLPFgdQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 491592515 174 RAHL-QDALMKIQAELNNTVIMITHDVdEAVLLSDKIVMMTNG 215
Cdd:cd03290 176 SDHLmQEGILKFLQDDKRTLVLVTHKL-QYLPHADWIIAMKDG 217
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
15-226 |
4.36e-16 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 77.62 E-value: 4.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 15 FPTPDGEF-IALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREvagpgpdrAVVFQNHSLLPWL 93
Cdd:PRK13545 29 FRSKDGEYhYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA--------ALIAISSGLNGQL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 94 TVYQNVELAVKQIAGKKGKawIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALD-AL 172
Cdd:PRK13545 101 TGIENIELKGLMMGLTKEK--IKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDqTF 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491592515 173 TRAHLQDalMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIGEVLEV 226
Cdd:PRK13545 179 TKKCLDK--MNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEV 230
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
25-210 |
4.37e-16 |
|
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: 77.94 E-value: 4.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDG---REVA--------GPGPDRAVVFQNhsllpwl 93
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGqdiRDVTqaslraaiGIVPQDTVLFND------- 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 94 TVYQNvelavkqIA-GKKGKAwiQEQVNHYLELIQMQHAAHKKPD-----------EISGGMKQRVGIARALALQPKVLL 161
Cdd:COG5265 447 TIAYN-------IAyGRPDAS--EEEVEAAARAAQIHDFIESLPDgydtrvgerglKLSGGEKQRVAIARTLLKNPPILI 517
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491592515 162 MDEPFGALDALTRAHLQDALMKIQAelNNTVIMITH------DVDEAVLLSD-KIV 210
Cdd:COG5265 518 FDEATSALDSRTERAIQAALREVAR--GRTTLVIAHrlstivDADEILVLEAgRIV 571
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
24-215 |
4.63e-16 |
|
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: 77.86 E-value: 4.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 24 ALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPgpDRAVVFQNHSLLPWL------TVYQ 97
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDI--DRHTLRQFINYLPQEpyifsgSILE 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 98 NVELAVKQIAGkkgkawiQEQVNHYLELIQMQHAAHKKP-----------DEISGGMKQRVGIARALALQPKVLLMDEPF 166
Cdd:TIGR01193 567 NLLLGAKENVS-------QDEIWAACEIAEIKDDIENMPlgyqtelseegSSISGGQKQRIALARALLTDSKVLILDEST 639
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491592515 167 GALDALTRAHLQDALMKIQaelNNTVIMITHDVDEAVlLSDKIVMMTNG 215
Cdd:TIGR01193 640 SNLDTITEKKIVNNLLNLQ---DKTIIFVAHRLSVAK-QSDKIIVLDHG 684
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
24-219 |
7.16e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 75.30 E-value: 7.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 24 ALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGRevagpgPDRAVVFQNhsLLPWLTVYQNVELA- 102
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQ------PTRQALQKN--LVAYVPQSEEVDWSf 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 103 ---VKQIA--GKKG--------KAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGAL 169
Cdd:PRK15056 94 pvlVEDVVmmGRYGhmgwlrraKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491592515 170 DALTRAHLQDALMKIQAElNNTVIMITHDVDEAVLLSDKIVM-----MTNGPAAT 219
Cdd:PRK15056 174 DVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCDYTVMvkgtvLASGPTET 227
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
7-229 |
7.96e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 77.09 E-value: 7.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 7 DLTrlgMRFptpdGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAgPGpDRA----V 82
Cdd:NF033858 271 GLT---MRF----GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD-AG-DIAtrrrV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 83 VF--QNHSLLPWLTVYQNVELAVK--QIAGKKGKAWIQEQVNHYleliQMQHAAHKKPDEISGGMKQRVGIARALALQPK 158
Cdd:NF033858 342 GYmsQAFSLYGELTVRQNLELHARlfHLPAAEIAARVAEMLERF----DLADVADALPDSLPLGIRQRLSLAVAVIHKPE 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491592515 159 VLLMDEPFGALDALTRahlqDALMKIQAEL--NNTV-IMI-THDVDEAvLLSDKIVMMTNgpaatiGEVLEVNLP 229
Cdd:NF033858 418 LLILDEPTSGVDPVAR----DMFWRLLIELsrEDGVtIFIsTHFMNEA-ERCDRISLMHA------GRVLASDTP 481
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
19-211 |
9.30e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 74.22 E-value: 9.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 19 DGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAgPGPDRAVVfqnHSLLPWLTVYQN 98
Cdd:COG2401 40 VVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQ-FGREASLI---DAIGRKGDFKDA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 99 VELAvkQIAGKkGKAWIqeqvnhYLeliqmqhaahKKPDEISGGMKQRVGIARALALQPKVLLMDEpFGA-LDALTRAHL 177
Cdd:COG2401 116 VELL--NAVGL-SDAVL------WL----------RRFKELSTGQKFRFRLALLLAERPKLLVIDE-FCShLDRQTAKRV 175
|
170 180 190
....*....|....*....|....*....|....*
gi 491592515 178 QDALMKIQAELNNTVIMITHDVD-EAVLLSDKIVM 211
Cdd:COG2401 176 ARNLQKLARRAGITLVVATHHYDvIDDLQPDLLIF 210
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
25-223 |
1.21e-15 |
|
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: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMP---TDGGVIVDGREVAGPGPDR--AVVFQNHSLLPWLTVYQNV 99
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKEMRAisAYVQQDDLFIPTLTVREHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 100 ----ELAVKQIAGKKGKawiQEQVNHYLELIQMQHAAHKK---PDE---ISGGMKQRVGIARALALQPKVLLMDEPFGAL 169
Cdd:TIGR00955 121 mfqaHLRMPRRVTKKEK---RERVDEVLQALGLRKCANTRigvPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGL 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491592515 170 DALTRAHLQDALMKIqAELNNTVIMITHDVDEAVL-LSDKIVMMTNGPAATIGEV 223
Cdd:TIGR00955 198 DSFMAYSVVQVLKGL-AQKGKTIICTIHQPSSELFeLFDKIILMAEGRVAYLGSP 251
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
20-199 |
7.71e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 72.07 E-value: 7.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 20 GEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDRavvFQNHSLLPwLTVYQNV 99
Cdd:PRK09544 15 GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQK---LYLDTTLP-LTVNRFL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 100 EL--AVKqiagkkgkawiQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHL 177
Cdd:PRK09544 91 RLrpGTK-----------KEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVAL 159
|
170 180
....*....|....*....|..
gi 491592515 178 QDALMKIQAELNNTVIMITHDV 199
Cdd:PRK09544 160 YDLIDQLRRELDCAVLMVSHDL 181
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
18-198 |
8.54e-15 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 73.82 E-value: 8.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 18 PDGEFIaLKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGgvivdgreVAGPGPDRAVVF--QNHSLLPWLTV 95
Cdd:TIGR03719 15 PPKKEI-LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG--------EARPQPGIKVGYlpQEPQLDPTKTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 96 YQNVELAVKQIAGK----------------------KGKAWIQEQVN----HYLELiQMQHAAH--KKPD------EISG 141
Cdd:TIGR03719 86 RENVEEGVAEIKDAldrfneisakyaepdadfdklaAEQAELQEIIDaadaWDLDS-QLEIAMDalRCPPwdadvtKLSG 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491592515 142 GMKQRVGIARALALQPKVLLMDEPFGALDALTRAHLQDALmkiqAELNNTVIMITHD 198
Cdd:TIGR03719 165 GERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL----QEYPGTVVAVTHD 217
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
19-215 |
1.28e-14 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 73.46 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 19 DGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDG---REVAGPGPDR--AVVFQNHSLLPwL 93
Cdd:PRK13657 345 DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtdiRTVTRASLRRniAVVFQDAGLFN-R 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 94 TVYQNVELavkqiaGKKGKAwiQEQVNHYLELIQMQHAAHKKPD-----------EISGGMKQRVGIARALALQPKVLLM 162
Cdd:PRK13657 424 SIEDNIRV------GRPDAT--DEEMRAAAERAQAHDFIERKPDgydtvvgergrQLSGGERQRLAIARALLKDPPILIL 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491592515 163 DEPFGALDALTRAHLQDAL---MKiqaelNNTVIMITH---DVDEAvllsDKIVMMTNG 215
Cdd:PRK13657 496 DEATSALDVETEAKVKAALdelMK-----GRTTFIIAHrlsTVRNA----DRILVFDNG 545
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
25-215 |
1.29e-14 |
|
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: 70.75 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPT---DGGVIVDGREV--AGPGPDRAVVF--QNHSLLPWLTVYQ 97
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYkeFAEKYPGEIIYvsEEDVHFPTLTVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 98 NVELAVKQiagkKGKAWIQEqvnhyleliqmqhaahkkpdeISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHL 177
Cdd:cd03233 103 TLDFALRC----KGNEFVRG---------------------ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEI 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 491592515 178 QDALMKIQAELNNTVIM-ITHDVDEAVLLSDKIVMMTNG 215
Cdd:cd03233 158 LKCIRTMADVLKTTTFVsLYQASDEIYDLFDKVLVLYEG 196
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
5-215 |
1.31e-14 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 72.53 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 5 LLDLTRLGMRFPTPDGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGlhmptdggVIVDGREVAG--------- 75
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICG--------VTKDNWRVTAdrmrfddid 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 76 -----PGPDRAVVFQNHSLL-----PWLTVYQNVELAVKQ-IAG--KKGKAWiqeQVNHYLE--LIQMQH----AAHKK- 135
Cdd:PRK15093 75 llrlsPRERRKLVGHNVSMIfqepqSCLDPSERVGRQLMQnIPGwtYKGRWW---QRFGWRKrrAIELLHrvgiKDHKDa 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 136 ----PDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVM 211
Cdd:PRK15093 152 mrsfPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINV 231
|
....
gi 491592515 212 MTNG 215
Cdd:PRK15093 232 LYCG 235
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
6-215 |
1.38e-14 |
|
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: 73.29 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 6 LDLTRLGMRFPTPDGE--FiALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDR--- 80
Cdd:COG4615 328 LELRGVTYRYPGEDGDegF-TLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAyrq 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 81 --AVVFQNHSLLpwltvyqnvelavKQIAGKKGKAwIQEQVNHYLELIQMQHAAHKKPDEI-----SGGMKQRVGIARAL 153
Cdd:COG4615 407 lfSAVFSDFHLF-------------DRLLGLDGEA-DPARARELLERLELDHKVSVEDGRFsttdlSQGQRKRLALLVAL 472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491592515 154 ALQPKVLLMDEpfGALDaltrahlQDA----------LMKIQAElNNTVIMITHDvDEAVLLSDKIVMMTNG 215
Cdd:COG4615 473 LEDRPILVFDE--WAAD-------QDPefrrvfytelLPELKAR-GKTVIAISHD-DRYFDLADRVLKMDYG 533
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
17-197 |
1.49e-14 |
|
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: 69.49 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 17 TPDGEFIaLKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGL--------HMPTDGGVI-VDGREVAGPGPDRAVVfqnh 87
Cdd:cd03223 10 TPDGRVL-LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLwpwgsgriGMPEGEDLLfLPQRPYLPLGTLREQL---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 88 sLLPWLtvyqnvelavkqiagkkgkawiqeqvnhyleliqmqhaahkkpDEISGGMKQRVGIARALALQPKVLLMDEPFG 167
Cdd:cd03223 85 -IYPWD-------------------------------------------DVLSGGEQQRLAFARLLLHKPKFVFLDEATS 120
|
170 180 190
....*....|....*....|....*....|
gi 491592515 168 ALDALTrahlQDALMKIQAELNNTVIMITH 197
Cdd:cd03223 121 ALDEES----EDRLYQLLKELGITVISVGH 146
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-222 |
2.25e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 72.73 E-value: 2.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 3 KALLDLTRLGMRFPTPDgefiALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDRA- 81
Cdd:PRK10762 2 QALLQLKGIDKAFPGVK----ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 82 -----VVFQNHSLLPWLTVYQNVELAvKQIAGKKGKA-W--IQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARAL 153
Cdd:PRK10762 78 eagigIIHQELNLIPQLTIAENIFLG-REFVNRFGRIdWkkMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491592515 154 ALQPKVLLMDEPfgaLDALTRAHLQdALMKIQAELNNT---VIMITHDVDEAVLLSDKIVMMTNGpaATIGE 222
Cdd:PRK10762 157 SFESKVIIMDEP---TDALTDTETE-SLFRVIRELKSQgrgIVYISHRLKEIFEICDDVTVFRDG--QFIAE 222
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
25-234 |
3.48e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 70.63 E-value: 3.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAG-LHMPTD-------GGVIVDGREVAGPGPD-----RAVVFQNHSLLP 91
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGAprgarvtGDVTLNGEPLAAIDAPrlarlRAVLPQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 92 WLTVYQNVELAVKQIAGKKGKAWIQEQ--VNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALA---------LQPKVL 160
Cdd:PRK13547 97 AFSAREIVLLGRYPHARRAGALTHRDGeiAWQALALAGATALVGRDVTTLSGGELARVQFARVLAqlwpphdaaQPPRYL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491592515 161 LMDEPFGALDALTRAHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIGEVLEVNLPRPRER 234
Cdd:PRK13547 177 LLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLTPAHIAR 250
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
31-227 |
9.59e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 69.19 E-value: 9.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 31 QINKGEFVSLIGHSGCGKSTVLNLVAGLhMPTDGGVIVDGREVAG-PGPD----RAVVFQNHSLLPWLTVYQnvELAVKQ 105
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAwSAAElarhRAYLSQQQTPPFAMPVFQ--YLTLHQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 106 IAGKKgKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIA-------RALALQPKVLLMDEPFGALDALTRAHLq 178
Cdd:PRK03695 95 PDKTR-TEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMNSLDVAQQAAL- 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491592515 179 DALMKIQAELNNTVIMITHDV-------DEAVLLSDKiVMMTNGPAAtigEVLEVN 227
Cdd:PRK03695 173 DRLLSELCQQGIAVVMSSHDLnhtlrhaDRVWLLKQG-KLLASGRRD---EVLTPE 224
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
25-231 |
9.83e-14 |
|
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: 69.50 E-value: 9.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPgpdravvfQNHSLLPWlTVYQNVELAVk 104
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSS--------QFSWIMPG-TIKENIIFGV- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 105 qiagkkgkAWIQEQVNHYLELIQMQHAAHKKPDE-----------ISGGMKQRVGIARALALQPKVLLMDEPFGALDALT 173
Cdd:cd03291 123 --------SYDEYRYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491592515 174 RAHLQDA-LMKIQAelNNTVIMITHDVdEAVLLSDKIVMMTNGPAATIGEVLEVNLPRP 231
Cdd:cd03291 195 EKEIFEScVCKLMA--NKTRILVTSKM-EHLKKADKILILHEGSSYFYGTFSELQSLRP 250
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
25-227 |
1.07e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 70.46 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDRA------VVFQNHSLLPWLTVYQN 98
Cdd:PRK15439 27 LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAhqlgiyLVPQEPLLFPNLSVKEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 99 V--ELAVKQIAGKKGKAWIQeQVNHYLELiQMQHAAHKKPDeisggmKQRVGIARALALQPKVLLMDEPFGaldALTRAH 176
Cdd:PRK15439 107 IlfGLPKRQASMQKMKQLLA-ALGCQLDL-DSSAGSLEVAD------RQIVEILRGLMRDSRILILDEPTA---SLTPAE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491592515 177 LQDALMKIQAELNNTV--IMITHDVDEAVLLSDKIVMMTNGPAATIGEVLEVN 227
Cdd:PRK15439 176 TERLFSRIRELLAQGVgiVFISHKLPEIRQLADRISVMRDGTIALSGKTADLS 228
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-215 |
2.01e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 69.67 E-value: 2.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 3 KALLDLTRLGMRfptPDGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGP---- 78
Cdd:COG3845 255 EVVLEVENLSVR---DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPrerr 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 79 ---------DRavvfQNHSLLPWLTVYQNveLAVKQIAGKK--GKAWIQEQVNHyleliqmQHAAH-------KKPDE-- 138
Cdd:COG3845 332 rlgvayipeDR----LGRGLVPDMSVAEN--LILGRYRRPPfsRGGFLDRKAIR-------AFAEElieefdvRTPGPdt 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 139 ----ISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHLQDALMKiQAELNNTVIMITHDVDEAVLLSDKIVMMTN 214
Cdd:COG3845 399 parsLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLE-LRDAGAAVLLISEDLDEILALSDRIAVMYE 477
|
.
gi 491592515 215 G 215
Cdd:COG3845 478 G 478
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
19-217 |
2.52e-13 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 67.82 E-value: 2.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 19 DGEFiALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVA-GP---GPDRAVvfqnhsllpwlT 94
Cdd:cd03237 10 LGEF-TLEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSyKPqyiKADYEG-----------T 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 95 VYQnveLAVKQIAGKKGKAWIQEQVNHYLELIQMqhaAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTR 174
Cdd:cd03237 78 VRD---LLSSITKDFYTHPYFKTEIAKPLQIEQI---LDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 491592515 175 AHLQDALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPA 217
Cdd:cd03237 152 LMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFEGEPS 194
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
4-215 |
5.55e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 68.98 E-value: 5.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 4 ALLDLTRLGMRF---PTPDGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGlhmPTDGGVIVDGREVA--GPGP 78
Cdd:TIGR00956 53 ALLKILTRGFRKlkkFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAS---NTDGFHIGVEGVITydGITP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 79 D------RAVVF---QNHSLLPWLTVYQNVELAVK------QIAGKKGKAWIQEQVNHYLELIQMQHAAHKKPDE----- 138
Cdd:TIGR00956 130 EeikkhyRGDVVynaETDVHFPHLTVGETLDFAARcktpqnRPDGVSREEYAKHIADVYMATYGLSHTRNTKVGNdfvrg 209
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491592515 139 ISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHLQDALMKIQAELNNTVIM-ITHDVDEAVLLSDKIVMMTNG 215
Cdd:TIGR00956 210 VSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVaIYQCSQDAYELFDKVIVLYEG 287
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
25-231 |
6.75e-13 |
|
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: 68.78 E-value: 6.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGpdravvfqnhslLPWL---TVYQNVEL 101
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQ------------TSWImpgTIKDNIIF 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 102 avkqiagkkGKAWIQEQVNHYLELIQMQHAAHKKPDE-----------ISGGMKQRVGIARALALQPKVLLMDEPFGALD 170
Cdd:TIGR01271 510 ---------GLSYDEYRYTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491592515 171 ALTRAHL-QDALMKIQAelNNTVIMITHDVdEAVLLSDKIVMMTNGPAATIGEVLEVNLPRP 231
Cdd:TIGR01271 581 VVTEKEIfESCLCKLMS--NKTRILVTSKL-EHLKKADKILLLHEGVCYFYGTFSELQAKRP 639
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
26-215 |
7.58e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 68.15 E-value: 7.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 26 KNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGP----DRAVVF-----QNHSLLPWLTVY 96
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTaqrlARGLVYlpedrQSSGLYLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 97 QNV-ELAVKQ----IAGKKGKAwIQEQVNHYLElIQMQHAaHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDA 171
Cdd:PRK15439 360 WNVcALTHNRrgfwIKPARENA-VLERYRRALN-IKFNHA-EQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491592515 172 LTRAHLQDaLMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:PRK15439 437 SARNDIYQ-LIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQG 479
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
24-227 |
8.96e-13 |
|
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: 65.04 E-value: 8.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 24 ALKNVDLQINKGEFVSLIGHSGCGKSTVLNlvaglhmptDGGvivdgrevAGPGPDRAVvfqnhSLLPwlTVYQNVELAV 103
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLVN---------EGL--------YASGKARLI-----SFLP--KFSRNKLIFI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 104 KQIagkkgKAWIQEQVNhYLELIQmqhaahkKPDEISGGMKQRVGIARALALQPK--VLLMDEPFGALDALTRAHLQDAL 181
Cdd:cd03238 66 DQL-----QFLIDVGLG-YLTLGQ-------KLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVI 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491592515 182 MKIqAELNNTVIMITHDVDeaVL-LSDKIVMMTNGPAATIGEVLEVN 227
Cdd:cd03238 133 KGL-IDLGNTVILIEHNLD--VLsSADWIIDFGPGSGKSGGKVVFSG 176
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
22-230 |
9.61e-13 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 66.38 E-value: 9.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 22 FIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGrevagpgpDRAVVFQNHSLLPWLTVYQNVEL 101
Cdd:PRK13546 37 FFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG--------EVSVIAISAGLSGQLTGIENIEF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 102 AVKQIAGKKGKawIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEpfgALDALTRAHLQDAL 181
Cdd:PRK13546 109 KMLCMGFKRKE--IKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDE---ALSVGDQTFAQKCL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491592515 182 MKIQ--AELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIGEVLEVnLPR 230
Cdd:PRK13546 184 DKIYefKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDV-LPK 233
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
20-197 |
1.03e-12 |
|
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: 65.21 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 20 GEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPD--RAVVFQNHS--LLPWLTV 95
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiaRGLLYLGHApgIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 96 YQNVELAVKQIAgkkgkawiQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRA 175
Cdd:cd03231 91 LENLRFWHADHS--------DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVA 162
|
170 180
....*....|....*....|..
gi 491592515 176 HLQDAlMKIQAELNNTVIMITH 197
Cdd:cd03231 163 RFAEA-MAGHCARGGMVVLTTH 183
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
34-215 |
1.69e-12 |
|
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: 63.55 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 34 KGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVdgrevagpgpdravvfqnhsllpwltvyqnvelavkqIAGkkgka 113
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY-------------------------------------IDG----- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 114 wiqEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHLQD-----ALMKIQAEL 188
Cdd:smart00382 39 ---EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrLLLLLKSEK 115
|
170 180 190
....*....|....*....|....*....|..
gi 491592515 189 NNTVIMITHDV-----DEAVLLSDKIVMMTNG 215
Cdd:smart00382 116 NLTVILTTNDEkdlgpALLRRRFDRRIVLLLI 147
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
39-215 |
1.78e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 65.89 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 39 SLIGHSGCGKSTVL-------NLVAGLHMPTD----GGVIVDGREVAGPGPDRAVVFQNHSLLPwLTVYQNVELAV---K 104
Cdd:PRK14271 51 SLMGPTGSGKTTFLrtlnrmnDKVSGYRYSGDvllgGRSIFNYRDVLEFRRRVGMLFQRPNPFP-MSIMDNVLAGVrahK 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 105 QIAGKKGKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHLQDALMKI 184
Cdd:PRK14271 130 LVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSL 209
|
170 180 190
....*....|....*....|....*....|.
gi 491592515 185 QAELnnTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:PRK14271 210 ADRL--TVIIVTHNLAQAARISDRAALFFDG 238
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
25-197 |
2.04e-12 |
|
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: 64.47 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGlHM---PTDGGVIVDGREVAGPGPD-RA-----VVFQNhsllPwltv 95
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HPkyeVTEGEILFKGEDITDLPPEeRArlgifLAFQY----P---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 96 yqnvelavKQIAGKKGKAWIQEqVNhyleliqmqhaahkkpDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRA 175
Cdd:cd03217 87 --------PEIPGVKNADFLRY-VN----------------EGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALR 141
|
170 180
....*....|....*....|..
gi 491592515 176 HLQDALMKIqAELNNTVIMITH 197
Cdd:cd03217 142 LVAEVINKL-REEGKSVLIITH 162
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
26-220 |
2.08e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 66.73 E-value: 2.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 26 KNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDRAV------VFQN---HSLLPWLTVY 96
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVkkgmayITESrrdNGFFPNFSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 97 QNVELAVKQIAGKKGKAW-------IQEQVNHYLELIQMQ-HAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGA 168
Cdd:PRK09700 360 QNMAISRSLKDGGYKGAMglfhevdEQRTAENQRELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRG 439
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491592515 169 LDALTRAHLQdALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATI 220
Cdd:PRK09700 440 IDVGAKAEIY-KVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
25-221 |
2.66e-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: 2.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGrEVAGPgPDRAVVfQNHSLlpwltvYQNVeLAVK 104
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-SVAYV-PQQAWI-QNDSL------RENI-LFGK 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 105 QIAGKKGKAWIQE-QVNHYLELIQM--QHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHLQDAL 181
Cdd:TIGR00957 724 ALNEKYYQQVLEAcALLPDLEILPSgdRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHV 803
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 491592515 182 MKIQAEL-NNTVIMITHDVdEAVLLSDKIVMMTNGPAATIG 221
Cdd:TIGR00957 804 IGPEGVLkNKTRILVTHGI-SYLPQVDVIIVMSGGKISEMG 843
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
25-198 |
2.81e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 66.51 E-value: 2.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDG------------REVAGpgpdravvfqnhsllpw 92
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQdlivarlqqdppRNVEG----------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 93 lTVYQNVELAVKQIAGK--------------------KGKAWIQEQVNHY----LE------LIQMQHAAHKKPDEISGG 142
Cdd:PRK11147 82 -TVYDFVAEGIEEQAEYlkryhdishlvetdpseknlNELAKLQEQLDHHnlwqLEnrinevLAQLGLDPDAALSSLSGG 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491592515 143 MKQRVGIARALALQPKVLLMDEPFGALDALTRAHLQDALMkiqaELNNTVIMITHD 198
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLK----TFQGSIIFISHD 212
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
93-214 |
4.55e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 66.21 E-value: 4.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 93 LTVYQNVELAvKQIAGKKG--KAWIQEQVNHYLELIQMQHAAHKKP--DEISGGMKQRVGIARALALQPKVLLMDEPFGA 168
Cdd:PTZ00265 1310 MSIYENIKFG-KEDATREDvkRACKFAAIDEFIESLPNKYDTNVGPygKSLSGGQKQRIAIARALLREPKILLLDEATSS 1388
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 491592515 169 LDALTRAHLQDALMKIQAELNNTVIMITHDVdEAVLLSDKIVMMTN 214
Cdd:PTZ00265 1389 LDSNSEKLIEKTIVDIKDKADKTIITIAHRI-ASIKRSDKIVVFNN 1433
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
26-214 |
7.61e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 65.44 E-value: 7.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 26 KNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDG------------REVAGPGPDRAVVFQN------- 86
Cdd:PTZ00265 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlkdinlkwwRSKIGVVSQDPLLFSNsiknnik 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 87 ---HSL--LPWLTVYQNVELAVKQiAGKKGKAWIQEQVNHYL----------ELIQMQH-----------AAHKK----- 135
Cdd:PTZ00265 482 yslYSLkdLEALSNYYNEDGNDSQ-ENKNKRNSCRAKCAGDLndmsnttdsnELIEMRKnyqtikdsevvDVSKKvlihd 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 136 -----PDE-----------ISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHLQDALMKIQAELNNTVIMITHDV 199
Cdd:PTZ00265 561 fvsalPDKyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRL 640
|
250
....*....|....*
gi 491592515 200 dEAVLLSDKIVMMTN 214
Cdd:PTZ00265 641 -STIRYANTIFVLSN 654
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
24-221 |
1.03e-11 |
|
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: 62.81 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 24 ALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDR-----AVVFQNHSLLPWlTVYQN 98
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDlrsslTIIPQDPTLFSG-TIRSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 99 VELavkqiagkkgkawiqeqVNHYLElIQMQHAAHKKP--DEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAH 176
Cdd:cd03369 102 LDP-----------------FDEYSD-EEIYGALRVSEggLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491592515 177 LQDAlmkIQAELNN-TVIMITHDVdEAVLLSDKIVMMTNGPAATIG 221
Cdd:cd03369 164 IQKT---IREEFTNsTILTIAHRL-RTIIDYDKILVMDAGEVKEYD 205
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
25-215 |
1.13e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 64.90 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAG-LHMPT-DGGVIVDGREVAGPGPDR-AVVFQNHSLLPWLTVYQNVE- 100
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGrIQGNNfTGTILANNRKPTKQILKRtGFVTQDDILYPHLTVRETLVf 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 101 ---LAVKQIAGKKGKAWIQEQVNHYLELIQMQHA--AHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRA 175
Cdd:PLN03211 164 cslLRLPKSLTKQEKILVAESVISELGLTKCENTiiGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAY 243
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 491592515 176 HLQDALMKIqAELNNTVIMITHDVDEAVL-LSDKIVMMTNG 215
Cdd:PLN03211 244 RLVLTLGSL-AQKGKTIVTSMHQPSSRVYqMFDSVLVLSEG 283
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
25-215 |
1.55e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 64.61 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAG-LHMPTDGGVIVDGREVAGPGpdravvfqnhslLPWL---TVYQNVE 100
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVIRGSVAYVPQ------------VSWIfnaTVRENIL 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 101 LAVKQIAGKKGKAWIQEQVNHYLELIQMQHAAH--KKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHLQ 178
Cdd:PLN03232 701 FGSDFESERYWRAIDVTALQHDLDLLPGRDLTEigERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVF 780
|
170 180 190
....*....|....*....|....*....|....*..
gi 491592515 179 DALMKIQAElNNTVIMITHDVdEAVLLSDKIVMMTNG 215
Cdd:PLN03232 781 DSCMKDELK-GKTRVLVTNQL-HFLPLMDRIILVSEG 815
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
24-226 |
1.80e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 64.04 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 24 ALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHmPT---DGGVIVDGREVAGPG----PDRAVVF--QNHSLLPWLT 94
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEVCRFKDirdsEALGIVIihQELALIPYLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 95 VYQNVELAVKQiaGKKGkaWI--QEQVNHYLELIQ---MQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGAL 169
Cdd:NF040905 95 IAENIFLGNER--AKRG--VIdwNETNRRARELLAkvgLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAAL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491592515 170 DALTRAHLQDALMKIQAElNNTVIMITHDVDEAVLLSDKIVMMTNGpaATIgEVLEV 226
Cdd:NF040905 171 NEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDG--RTI-ETLDC 223
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
27-215 |
1.91e-11 |
|
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: 63.69 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 27 NVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPT-DGGVIVDGREVAGPGPDRAVVF---------QNHSLLPWLTVY 96
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQAIRAgiamvpedrKRHGIVPILGVG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 97 QNVELAVKQIAGKKGKAWIQEQVNHYLELIQMQHAAHKKPD----EISGGMKQRVGIARALALQPKVLLMDEPFGALDAL 172
Cdd:TIGR02633 358 KNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFlpigRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVG 437
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 491592515 173 TRAHLQdALMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:TIGR02633 438 AKYEIY-KLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
25-186 |
2.46e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 61.50 E-value: 2.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAgpgPDRA-----VVFQNH--SLLPWLTVYQ 97
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK---KDLCtyqkqLCFVGHrsGINPYLTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 98 NVELAVKQIAGKKGkawiqeqVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTrahL 177
Cdd:PRK13540 94 NCLYDIHFSPGAVG-------ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS---L 163
|
....*....
gi 491592515 178 QDALMKIQA 186
Cdd:PRK13540 164 LTIITKIQE 172
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
20-197 |
3.68e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 61.97 E-value: 3.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 20 GEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGlHmP----TDGGVIVDGREVAGPGPD-RA-----VVFQNHSL 89
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG-H-PaykiLEGDILFKGESILDLEPEeRAhlgifLAFQYPIE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 90 LPWLTVYQNVELAVKQIAGKKGKAWIQ-----EQVNHYLELIQM-QHAAHKKPDE-ISGGMKQRVGIARALALQPKVLLM 162
Cdd:CHL00131 96 IPGVSNADFLRLAYNSKRKFQGLPELDpleflEIINEKLKLVGMdPSFLSRNVNEgFSGGEKKRNEILQMALLDSELAIL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 491592515 163 DEPFGALDAltrahlqDALMKIQAELN------NTVIMITH 197
Cdd:CHL00131 176 DETDSGLDI-------DALKIIAEGINklmtseNSIILITH 209
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
20-197 |
3.95e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 60.97 E-value: 3.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 20 GEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDRavvfqNHSLL--------- 90
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEY-----HQDLLylghqpgik 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 91 PWLTVYQNVELAvKQIAGKKGkawiQEQVNHYLELI----QMQHAAHkkpdEISGGMKQRVGIARaLAL-QPKVLLMDEP 165
Cdd:PRK13538 87 TELTALENLRFY-QRLHGPGD----DEALWEALAQVglagFEDVPVR----QLSAGQQRRVALAR-LWLtRAPLWILDEP 156
|
170 180 190
....*....|....*....|....*....|..
gi 491592515 166 FGALDALTRAHLQdALMKIQAELNNTVIMITH 197
Cdd:PRK13538 157 FTAIDKQGVARLE-ALLAQHAEQGGMVILTTH 187
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
18-216 |
9.47e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 62.06 E-value: 9.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 18 PDGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGlHMPT--DGGVIVDGREvagpgpdrAVVFQnhslLPWL-- 93
Cdd:PLN03130 626 SKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLG-ELPPrsDASVVIRGTV--------AYVPQ----VSWIfn 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 94 -TVYQNVELAVKQIAGKKGKAWIQEQVNHYLELIQM--QHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALD 170
Cdd:PLN03130 693 aTVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGgdLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491592515 171 ALTRAHLQDALMKiqAEL-NNTVIMITHD------VDEAVLLSDKIV--------MMTNGP 216
Cdd:PLN03130 773 AHVGRQVFDKCIK--DELrGKTRVLVTNQlhflsqVDRIILVHEGMIkeegtyeeLSNNGP 831
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
25-198 |
1.59e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 61.29 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVivdgreVAGPGPDRAVVFQNHSLLPWLTVYQNVELAVK 104
Cdd:PRK11819 23 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEA------RPAPGIKVGYLPQEPQLDPEKTVRENVEEGVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 105 QIAGKKGK----------------------AWIQEQVNHY----LELiQMQHAAH--------KKPDEISGGMKQRVGIA 150
Cdd:PRK11819 97 EVKAALDRfneiyaayaepdadfdalaaeqGELQEIIDAAdawdLDS-QLEIAMDalrcppwdAKVTKLSGGERRRVALC 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491592515 151 RALALQPKVLLMDEPFGALDALTRAHLQDALmkiqAELNNTVIMITHD 198
Cdd:PRK11819 176 RLLLEKPDMLLLDEPTNHLDAESVAWLEQFL----HDYPGTVVAVTHD 219
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
17-212 |
3.90e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 60.31 E-value: 3.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 17 TPDGEFIaLKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLhMPTDGGVIVDGrevagpgpdraVVFQNHSLLPWLTVY 96
Cdd:TIGR01271 1228 TEAGRAV-LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDG-----------VSWNSVTLQTWRKAF 1294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 97 QNVELAVKQIAGKKGK------AWIQEQVNHYLELIQMQHAAHKKPDE-----------ISGGMKQRVGIARALALQPKV 159
Cdd:TIGR01271 1295 GVIPQKVFIFSGTFRKnldpyeQWSDEEIWKVAEEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMCLARSILSKAKI 1374
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491592515 160 LLMDEPFGALDALTRAHLQDALMkiQAELNNTVIMITHDVdEAVLLSDKIVMM 212
Cdd:TIGR01271 1375 LLLDEPSAHLDPVTLQIIRKTLK--QSFSNCTVILSEHRV-EALLECQQFLVI 1424
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
28-236 |
6.26e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 59.15 E-value: 6.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 28 VDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDRAV---------------VFQNHSllpw 92
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIragimlcpedrkaegIIPVHS---- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 93 ltVYQNVELAVKQIAGKKG----KAWIQEQVNHYLELIQMQHAAHKKP-DEISGGMKQRVGIARALALQPKVLLMDEPFG 167
Cdd:PRK11288 348 --VADNINISARRHHLRAGclinNRWEAENADRFIRSLNIKTPSREQLiMNLSGGNQQKAILGRWLSEDMKVILLDEPTR 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491592515 168 ALDALTRAHLQDALMKIqAELNNTVIMITHDVDEAVLLSDKIVMMTNG--------PAATIGEVLEVNLPRPRERVA 236
Cdd:PRK11288 426 GIDVGAKHEIYNVIYEL-AAQGVAVLFVSSDLPEVLGVADRIVVMREGriagelarEQATERQALSLALPRTSAAVA 501
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
15-222 |
7.15e-10 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 59.34 E-value: 7.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 15 FPTPDGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDR-----AVVFQNhsl 89
Cdd:PRK10789 321 FTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwrsrlAVVSQT--- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 90 lPWL---TVYQNVELavkqiaGKKGKAwiQEQVNHYLELIQMQHAAHKKPD-----------EISGGMKQRVGIARALAL 155
Cdd:PRK10789 398 -PFLfsdTVANNIAL------GRPDAT--QQEIEHVARLASVHDDILRLPQgydtevgergvMLSGGQKQRISIARALLL 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491592515 156 QPKVLLMDEPFGALDALTRAHLQDALMkiQAELNNTVIMITHDVdEAVLLSDKIVMMTNGPAATIGE 222
Cdd:PRK10789 469 NAEILILDDALSAVDGRTEHQILHNLR--QWGEGRTVIISAHRL-SALTEASEILVMQHGHIAQRGN 532
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
31-210 |
7.18e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.05 E-value: 7.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 31 QINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGP---GPDRAVvfqnhsllpwltvyqNVELAVKQIA 107
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPqyiKPDYDG---------------TVEDLLRSIT 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 108 GKKGKAWIQEQVNHYLELIQMqhaAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHLQDALMKIQAE 187
Cdd:PRK13409 426 DDLGSSYYKSEIIKPLQLERL---LDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEE 502
|
170 180
....*....|....*....|...
gi 491592515 188 LNNTVIMITHDVDEAVLLSDKIV 210
Cdd:PRK13409 503 REATALVVDHDIYMIDYISDRLM 525
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-198 |
7.62e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 59.14 E-value: 7.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 1 MEKAL----LDLTRLGMRFptpDGEFIaLKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGlHMPTDGGViVDGREVAGP 76
Cdd:PRK15064 311 QDKKLhrnaLEVENLTKGF---DNGPL-FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVG-ELEPDSGT-VKWSENANI 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 77 G---PDRAVVFQNH-SLLPWLTVYQNV---ELAVKQIAGKkgkawiqeqvnhyleLIQMQHAAHKKPDEISGGMKQRVGI 149
Cdd:PRK15064 385 GyyaQDHAYDFENDlTLFDWMSQWRQEgddEQAVRGTLGR---------------LLFSQDDIKKSVKVLSGGEKGRMLF 449
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491592515 150 ARALALQPKVLLMDEPFGALDALTRAHLQDALMKIQAelnnTVIMITHD 198
Cdd:PRK15064 450 GKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEG----TLIFVSHD 494
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
20-198 |
9.31e-10 |
|
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: 58.79 E-value: 9.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 20 GEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPtDGGVIVDGREVagpgpDRAVVFQNHSLL-PWLTVYQN 98
Cdd:TIGR03719 333 GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQP-DSGTIEIGETV-----KLAYVDQSRDALdPNKTVWEE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 99 VELAVKQIagKKGKAWIQEQVnhYLELIQMQHAAH-KKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHL 177
Cdd:TIGR03719 407 ISGGLDII--KLGKREIPSRA--YVGRFNFKGSDQqKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRAL 482
|
170 180
....*....|....*....|.
gi 491592515 178 QDALMkiqaELNNTVIMITHD 198
Cdd:TIGR03719 483 EEALL----NFAGCAVVISHD 499
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-215 |
1.06e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 58.98 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 20 GEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDRAVVFQ--------NHSLLP 91
Cdd:NF033858 12 GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVCPRiaympqglGKNLYP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 92 WLTVYQNVelavkQIAGK---KGKAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGA 168
Cdd:NF033858 92 TLSVFENL-----DFFGRlfgQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTG 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491592515 169 LDALTRAHLQDALMKIQAELNN-TVIMITHDVDEAVLLsDKIVMMTNG 215
Cdd:NF033858 167 VDPLSRRQFWELIDRIRAERPGmSVLVATAYMEEAERF-DWLVAMDAG 213
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
25-215 |
1.29e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.48 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGP----DRAVVF-----QNHSLLPWLTV 95
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPqdglANGIVYisedrKRDGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 96 YQNVEL-AVKQIAGKKGK---AWIQEQVNHYLELIQMQHAAHKKP-DEISGGMKQRVGIARALALQPKVLLMDEPFGALD 170
Cdd:PRK10762 348 KENMSLtALRYFSRAGGSlkhADEQQAVSDFIRLFNIKTPSMEQAiGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 491592515 171 ALTRAHLQDALMKIQAElNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:PRK10762 428 VGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEG 471
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
35-218 |
1.92e-09 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 56.99 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 35 GEFVSLIGHSGCGKSTVLNLVAGLHMPTDGgvivdgrEVAGPGPDRAVV--FQNHSLLPWLTVY-----------QNVEL 101
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLG-------KFDDPPDWDEILdeFRGSELQNYFTKLlegdvkvivkpQYVDL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 102 AVKQIAGKKG----KAWIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHL 177
Cdd:cd03236 99 IPKAVKGKVGellkKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 491592515 178 QdALMKIQAELNNTVIMITHDVdeAVL--LSDKIVMMTNGPAA 218
Cdd:cd03236 179 A-RLIRELAEDDNYVLVVEHDL--AVLdyLSDYIHCLYGEPGA 218
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
32-223 |
3.60e-09 |
|
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: 57.33 E-value: 3.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 32 INKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDravVFQNHSLLP-------WLTVYQNVELAVK 104
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISD---VHQNMGYCPqfdaiddLLTGREHLYLYAR 2038
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 105 qIAGKKGKAwIQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHLQDALMKI 184
Cdd:TIGR01257 2039 -LRGVPAEE-IEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSI 2116
|
170 180 190
....*....|....*....|....*....|....*....
gi 491592515 185 QAElNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIGEV 223
Cdd:TIGR01257 2117 IRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTI 2154
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
19-215 |
6.53e-09 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 55.63 E-value: 6.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 19 DGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLhMPTDGGVIVDGrevagpgpdraVVFQNHSLLPWLTVYQN 98
Cdd:cd03289 14 EGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDG-----------VSWNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 99 VELAVKQIAGKKGK------AWIQEQVNHYLELIQMQHAAHKKPDEI-----------SGGMKQRVGIARALALQPKVLL 161
Cdd:cd03289 82 IPQKVFIFSGTFRKnldpygKWSDEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491592515 162 MDEPFGALDALTRAHLQDALMkiQAELNNTVIMITHDVdEAVLLSDKIVMMTNG 215
Cdd:cd03289 162 LDEPSAHLDPITYQVIRKTLK--QAFADCTVILSEHRI-EAMLECQRFLVIEEN 212
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
13-235 |
7.31e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 56.33 E-value: 7.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 13 MRFPtpDGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPG-----------PDRA 81
Cdd:PTZ00243 1316 MRYR--EGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGlrelrrqfsmiPQDP 1393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 82 VVFQNhsllpwlTVYQNVELAVKQIAgkkgkawiqEQVNHYLELIQMQHAAHKKPDEI-----------SGGMKQRVGIA 150
Cdd:PTZ00243 1394 VLFDG-------TVRQNVDPFLEASS---------AEVWAALELVGLRERVASESEGIdsrvleggsnySVGQRQLMCMA 1457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 151 RALALQ-PKVLLMDEPFGALD-ALTRaHLQDALMkiQAELNNTVIMITHDVdEAVLLSDKIVMMTNGPAATIGEvlevnl 228
Cdd:PTZ00243 1458 RALLKKgSGFILMDEATANIDpALDR-QIQATVM--SAFSAYTVITIAHRL-HTVAQYDKIIVMDHGAVAEMGS------ 1527
|
....*..
gi 491592515 229 prPRERV 235
Cdd:PTZ00243 1528 --PRELV 1532
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
24-227 |
7.71e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.89 E-value: 7.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 24 ALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDRAV---------------VFQN-- 86
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAInhgfalvteerrstgIYAYld 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 87 ---HSLLPWLTVYQNVELAVKQIAGKKGKAWIQEQVNhyleliqMQHAAHKKP-DEISGGMKQRVGIARALALQPKVLLM 162
Cdd:PRK10982 343 igfNSLISNIRNYKNKVGLLDNSRMKSDTQWVIDSMR-------VKTPGHRTQiGSLSGGNQQKVIIGRWLLTQPEILML 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491592515 163 DEPFGALDALTRAHLQDALMKIqAELNNTVIMITHDVDEAVLLSDKIVMMTNGPAATIGEVLEVN 227
Cdd:PRK10982 416 DEPTRGIDVGAKFEIYQLIAEL-AKKDKGIIIISSEMPELLGITDRILVMSNGLVAGIVDTKTTT 479
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
34-218 |
1.08e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 55.56 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 34 KGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGgvivdgrEVAGPGPDRAVV--FQNHSLLPWL---------TVY--QNVE 100
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLG-------DYDEEPSWDEVLkrFRGTELQDYFkklangeikVAHkpQYVD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 101 LAVKQIAGK----------KGKAwiqeqvNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALD 170
Cdd:COG1245 171 LIPKVFKGTvrellekvdeRGKL------DELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491592515 171 ALTRAHLQDALMKIqAELNNTVIMITHDVdeAVL--LSDKIVMMTNGPAA 218
Cdd:COG1245 245 IYQRLNVARLIREL-AEEGKYVLVVEHDL--AILdyLADYVHILYGEPGV 291
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
20-210 |
1.20e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 55.56 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 20 GEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGlHMPTDGGvivdgrEVAGPGpDRAVVFQNHSLlPWLTV---- 95
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKN-EISADGG------SYTFPG-NWQLAWVNQET-PALPQpale 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 96 --------YQNVELAVKQ---------IAGKKGK-----AW-IQEQVNHYLELIQMQHAAHKKP-DEISGGMKQRVGIAR 151
Cdd:PRK10636 83 yvidgdreYRQLEAQLHDanerndghaIATIHGKldaidAWtIRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQ 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491592515 152 ALALQPKVLLMDEPFGALDAltrahlqDALMKIQAELNN---TVIMITHDVDEAVLLSDKIV 210
Cdd:PRK10636 163 ALICRSDLLLLDEPTNHLDL-------DAVIWLEKWLKSyqgTLILISHDRDFLDPIVDKII 217
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
24-215 |
1.54e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.12 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 24 ALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDRAV------VFQNHSLLPWLTVYQ 97
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALengismVHQELNLVLQRSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 98 NVELA---VKQIAGKKGKAWiQEQVNHYLELiQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTR 174
Cdd:PRK10982 93 NMWLGrypTKGMFVDQDKMY-RDTKAIFDEL-DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEV 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491592515 175 AHlqdaLMKIQAELNNT---VIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:PRK10982 171 NH----LFTIIRKLKERgcgIVYISHKMEEIFQLCDEITILRDG 210
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-197 |
3.77e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 54.18 E-value: 3.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 18 PDGEFIaLKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPG-----------PDRAVVFQN 86
Cdd:TIGR00957 1296 EDLDLV-LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGlhdlrfkitiiPQDPVLFSG 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 87 H---SLLPWlTVYQNVELavkqiagkkgkaWIQEQVNHYLELIQMQ-----HAAHKKPDEISGGMKQRVGIARALALQPK 158
Cdd:TIGR00957 1375 SlrmNLDPF-SQYSDEEV------------WWALELAHLKTFVSALpdkldHECAEGGENLSVGQRQLVCLARALLRKTK 1441
|
170 180 190
....*....|....*....|....*....|....*....
gi 491592515 159 VLLMDEPFGALDALTRAHLQdALMKIQAElNNTVIMITH 197
Cdd:TIGR00957 1442 ILVLDEATAAVDLETDNLIQ-STIRTQFE-DCTVLTIAH 1478
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
32-217 |
5.04e-08 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 51.80 E-value: 5.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 32 INKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGrevagpgpdravvfqnhsllpwltvyqnVELAVKQiagkkg 111
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG----------------------------ITPVYKP------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 112 kawiqeqvnHYLELiqmqhaahkkpdeiSGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHLQDALMKIQAELNNT 191
Cdd:cd03222 68 ---------QYIDL--------------SGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKT 124
|
170 180
....*....|....*....|....*.
gi 491592515 192 VIMITHDVDEAVLLSDKIVMMTNGPA 217
Cdd:cd03222 125 ALVVEHDLAVLDYLSDRIHVFEGEPG 150
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
25-173 |
7.29e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.19 E-value: 7.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGlhmPTDGGVIVDG-REVAGPGPDRAV------VFQNHSLLPWLTVYQ 97
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE---RVTTGVITGGdRLVNGRPLDSSFqrsigyVQQQDLHLPTSTVRE 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 98 NVELA--VKQIA--GKKGKawiQEQVNHYLELIQMQHAAhkkpDEISG----GM----KQRVGIARALALQPKVLL-MDE 164
Cdd:TIGR00956 856 SLRFSayLRQPKsvSKSEK---MEYVEEVIKLLEMESYA----DAVVGvpgeGLnveqRKRLTIGVELVAKPKLLLfLDE 928
|
....*....
gi 491592515 165 PFGALDALT 173
Cdd:TIGR00956 929 PTSGLDSQT 937
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
116-226 |
8.13e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 52.43 E-value: 8.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 116 QEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHLQDALMKIQAElNNTVIMI 195
Cdd:NF000106 122 RARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLT 200
|
90 100 110
....*....|....*....|....*....|.
gi 491592515 196 THDVDEAVLLSDKIVMMTNGPAATIGEVLEV 226
Cdd:NF000106 201 TQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-217 |
8.68e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 52.86 E-value: 8.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 31 QINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGP---GPDRAvvfqnhsllpwLTVYQNVElavKQIA 107
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYKPqyiSPDYD-----------GTVEEFLR---SANT 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 108 GKKGKAWIQEQVNHYLELiqmQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHLQDALMKIQAE 187
Cdd:COG1245 428 DDFGSSYYKTEIIKPLGL---EKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAEN 504
|
170 180 190
....*....|....*....|....*....|...
gi 491592515 188 LNNTVIMITHDV---DeavLLSDKIVMMTNGPA 217
Cdd:COG1245 505 RGKTAMVVDHDIyliD---YISDRLMVFEGEPG 534
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
16-215 |
1.02e-07 |
|
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: 51.09 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 16 PTPDGEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGlhmPTDGGVI-----VDGRevagPGPD---RAV--VFQ 85
Cdd:cd03232 14 PVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG---RKTAGVItgeilINGR----PLDKnfqRSTgyVEQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 86 NHSLLPWLTVYQNVELAvkqiagkkgkAWIQeqvnhyleliqmqhaahkkpdEISGGMKQRVGIARALALQPKVLLMDEP 165
Cdd:cd03232 87 QDVHSPNLTVREALRFS----------ALLR---------------------GLSVEQRKRLTIGVELAAKPSILFLDEP 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491592515 166 FGALDALTRAHLQDALMKIqAELNNTVIMITHDVDEAVLLS-DKIVMMTNG 215
Cdd:cd03232 136 TSGLDSQAAYNIVRFLKKL-ADSGQAILCTIHQPSASIFEKfDRLLLLKRG 185
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
15-207 |
2.22e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.78 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 15 FPTPD------------------GEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREvagp 76
Cdd:PLN03073 497 FPTPDdrpgppiisfsdasfgypGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKV---- 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 77 gpdRAVVFQNH----------SLLPWLTVYQNV-ELAVKQIAGKKGkawiqeqVNHYLELIQMQhaahkkpdEISGGMKQ 145
Cdd:PLN03073 573 ---RMAVFSQHhvdgldlssnPLLYMMRCFPGVpEQKLRAHLGSFG-------VTGNLALQPMY--------TLSGGQKS 634
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491592515 146 RVGIARALALQPKVLLMDEPFGALDaltrAHLQDALMKIQAELNNTVIMITHD-------VDEAVLLSD 207
Cdd:PLN03073 635 RVAFAKITFKKPHILLLDEPSNHLD----LDAVEALIQGLVLFQGGVLMVSHDehlisgsVDELWVVSE 699
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
25-203 |
7.90e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.95 E-value: 7.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGR-EVAgpgpdravVFQNH--SLLPWLTVYQNVel 101
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKlEVA--------YFDQHraELDPEKTVMDNL-- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 102 avkqiAGKKGKAWIQEQVNHYLELIQ--MQHA--AHKKPDEISGGMKQRVGIARaLALQPKVLL-MDEPFGALDALTRAH 176
Cdd:PRK11147 405 -----AEGKQEVMVNGRPRHVLGYLQdfLFHPkrAMTPVKALSGGERNRLLLAR-LFLKPSNLLiLDEPTNDLDVETLEL 478
|
170 180 190
....*....|....*....|....*....|
gi 491592515 177 LQDALmkiqAELNNTVIMITHD---VDEAV 203
Cdd:PRK11147 479 LEELL----DSYQGTVLLVSHDrqfVDNTV 504
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
42-197 |
9.34e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 48.33 E-value: 9.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 42 GHSGCGKSTVLNLVAGLHMPTDGGVIVDG---REVAGP-----GPDRAV-----VFQNhsLLPWLTVYQNVELAVKQIag 108
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNcniNNIAKPyctyiGHNLGLklemtVFEN--LKFWSEIYNSAETLYAAI-- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 109 kkgkawiqeqvnHYLELiqmQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHLQDaLMKIQAEL 188
Cdd:PRK13541 109 ------------HYFKL---HDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNN-LIVMKANS 172
|
....*....
gi 491592515 189 NNTVIMITH 197
Cdd:PRK13541 173 GGIVLLSSH 181
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
29-213 |
1.07e-06 |
|
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: 47.35 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 29 DLQINKGEFVSLIGHSGCGKSTVLN---LVAGLHMPTDGGvivdgREVAGPGPDRAVVfqnhsllpwltvyqnvelavkq 105
Cdd:cd03227 15 DVTFGEGSLTIITGPNGSGKSTILDaigLALGGAQSATRR-----RSGVKAGCIVAAV---------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 106 iagkkgkawiqeqvnhYLELIQMQHaahkkpdEISGGMKQRVGIARALALQPK----VLLMDEPFGALDALTRAHLQDAL 181
Cdd:cd03227 68 ----------------SAELIFTRL-------QLSGGEKELSALALILALASLkprpLYILDEIDRGLDPRDGQALAEAI 124
|
170 180 190
....*....|....*....|....*....|..
gi 491592515 182 MKiQAELNNTVIMITHDvDEAVLLSDKIVMMT 213
Cdd:cd03227 125 LE-HLVKGAQVIVITHL-PELAELADKLIHIK 154
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
34-218 |
1.41e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.04 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 34 KGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDgrevagPGPD------RAVVFQNH-----------SLLPwltvy 96
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEE------PSWDevlkrfRGTELQNYfkklyngeikvVHKP----- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 97 QNVELAVKQIAGKKGKawIQEQVNH------YLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALD 170
Cdd:PRK13409 167 QYVDLIPKVFKGKVRE--LLKKVDErgkldeVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491592515 171 ALTRAHLQDALMKIQAelNNTVIMITHDVdeAVL--LSDKIVMMTNGPAA 218
Cdd:PRK13409 245 IRQRLNVARLIRELAE--GKYVLVVEHDL--AVLdyLADNVHIAYGEPGA 290
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
28-170 |
1.70e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 47.92 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 28 VDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPGPDRAVVFQNH--SLLPWLTVYQNVELaVKQ 105
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHlpGLKADLSTLENLHF-LCG 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491592515 106 IAGKKGkawiQEQVNHYLELIQMQHAAHKKPDEISGGMKQRVGIARaLALQPKVL-LMDEPFGALD 170
Cdd:PRK13543 109 LHGRRA----KQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALAR-LWLSPAPLwLLDEPYANLD 169
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
20-198 |
4.04e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.86 E-value: 4.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 20 GEFIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGgvivdgrEVAGPGPDRAVVFQNHSLlPWLTVYQNV 99
Cdd:PRK10636 323 GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSG-------EIGLAKGIKLGYFAQHQL-EFLRADESP 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 100 ELAVKQIAGKKgkawIQEQVNHYLELIQMQHAAHKKPDE-ISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHLQ 178
Cdd:PRK10636 395 LQHLARLAPQE----LEQKLRDYLGGFGFQGDKVTEETRrFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALT 470
|
170 180
....*....|....*....|
gi 491592515 179 DALMKIQAELnntvIMITHD 198
Cdd:PRK10636 471 EALIDFEGAL----VVVSHD 486
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
25-222 |
8.04e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.08 E-value: 8.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDgREVAgpgpdraVVFQNhsllPWL---TVYQNVEL 101
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-RSIA-------YVPQQ----AWImnaTVRGNILF 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 102 AVKQIAGKKGKAWIQEQVNHYLELIQ--MQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDaltrAHLQD 179
Cdd:PTZ00243 744 FDEEDAARLADAVRVSQLEADLAQLGggLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALD----AHVGE 819
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491592515 180 ALMK---IQAELNNTVIMITHDVdEAVLLSDKIVMMTNGPAATIGE 222
Cdd:PTZ00243 820 RVVEecfLGALAGKTRVLATHQV-HVVPRADYVVALGDGRVEFSGS 864
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
25-197 |
8.54e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 45.94 E-value: 8.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGL--HMPTDGGVIVDGREVAGPGP-DRA-----VVFQNHSLLPWLTVY 96
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPeDRAgegifMAFQYPVEIPGVSNQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 97 QNVELAVKQIAGKKGKAWI-----QEQVNHYLELIQMQHAAHKKPDEI--SGGMKQRVGIARALALQPKVLLMDEPFGAL 169
Cdd:PRK09580 97 FFLQTALNAVRSYRGQEPLdrfdfQDLMEEKIALLKMPEDLLTRSVNVgfSGGEKKRNDILQMAVLEPELCILDESDSGL 176
|
170 180 190
....*....|....*....|....*....|....*
gi 491592515 170 DAltrahlqDALmKIQAELNNTV-------IMITH 197
Cdd:PRK09580 177 DI-------DAL-KIVADGVNSLrdgkrsfIIVTH 203
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
27-215 |
1.09e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 46.46 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 27 NVDLQINKGEFVSLIGHSGCGKS-TVLNLVAGLHMPTDGGVIVDGREVAGPGPDRAVVF---------QNHSLLPWLTVY 96
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTeLVQCLFGAYPGRWEGEIFIDGKPVKIRNPQQAIAQgiamvpedrKRDGIVPVMGVG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 97 QNVELAV-KQIAGKKgkawiqeQVNHYLEL--IQ--MQHAAHKKPD------EISGGMKQRVGIARALALQPKVLLMDEP 165
Cdd:PRK13549 360 KNITLAAlDRFTGGS-------RIDDAAELktILesIQRLKVKTASpelaiaRLSGGNQQKAVLAKCLLLNPKILILDEP 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491592515 166 FGALDALTRAHLQDaLMKIQAELNNTVIMITHDVDEAVLLSDKIVMMTNG 215
Cdd:PRK13549 433 TRGIDVGAKYEIYK-LINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEG 481
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
138-198 |
1.71e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.65 E-value: 1.71e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491592515 138 EISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHLQDALmkiqAELNNTVIMITHD 198
Cdd:PRK15064 155 EVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVL----NERNSTMIIISHD 211
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
127-197 |
2.03e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.62 E-value: 2.03e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491592515 127 QMQHaahKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHLQDALMKiqaeLNNTVIMITH 197
Cdd:PLN03073 336 EMQV---KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLK----WPKTFIVVSH 399
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
17-197 |
2.03e-05 |
|
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: 45.51 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 17 TPDGEfIALKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLhMPTDGGVivdgREVAGPG-----PDRavvfqnhsllP 91
Cdd:TIGR00954 461 TPNGD-VLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGEL-WPVYGGR----LTKPAKGklfyvPQR----------P 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 92 WLT--------VYQNVELAVKqiagKKGkawIQEQV-NHYLELIQMQH---------AAHKKPDEISGGMKQRVGIARAL 153
Cdd:TIGR00954 525 YMTlgtlrdqiIYPDSSEDMK----RRG---LSDKDlEQILDNVQLTHilereggwsAVQDWMDVLSGGEKQRIAMARLF 597
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491592515 154 ALQPKVLLMDEPFGALDaltrAHLQDALMKIQAELNNTVIMITH 197
Cdd:TIGR00954 598 YHKPQFAILDECTSAVS----VDVEGYMYRLCREFGITLFSVSH 637
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
25-215 |
2.65e-05 |
|
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: 44.51 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTvLNLvAGLHMPT--DGGVIVDGREVagpgpdravvfqnhSLLPWLTVYQNVELA 102
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSS-LSL-AFFRMVDifDGKIVIDGIDI--------------SKLPLHTLRSRLSII 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 103 VKQIAGKKG---------KAWIQEQVNHYLELIQMQHAAHKKP-----------DEISGGMKQRVGIARALALQPKVLLM 162
Cdd:cd03288 101 LQDPILFSGsirfnldpeCKCTDDRLWEALEIAQLKNMVKSLPggldavvteggENFSVGQRQLFCLARAFVRKSSILIM 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491592515 163 DEPFGALDALTRAHLQDALMKIQAElnNTVIMITHDVdEAVLLSDKIVMMTNG 215
Cdd:cd03288 181 DEATASIDMATENILQKVVMTAFAD--RTVVTIAHRV-STILDADLVLVLSRG 230
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
25-215 |
2.73e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 45.61 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMptdGGVIVDGREVAGpGPDRAVVF--------QN--HSllPWLT 94
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKT---GGYIEGDIRISG-FPKKQETFarisgyceQNdiHS--PQVT 969
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 95 VYQNVE----LAVKQIAGKKGKAWIQEQVNHYLELIQMQHAAHKKP--DEISGGMKQRVGIARALALQPKVLLMDEPFGA 168
Cdd:PLN03140 970 VRESLIysafLRLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSG 1049
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491592515 169 LDALTRAHLQDALmKIQAELNNTVIMITH----DVDEAVllsDKIVMMTNG 215
Cdd:PLN03140 1050 LDARAAAIVMRTV-RNTVDTGRTVVCTIHqpsiDIFEAF---DELLLMKRG 1096
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
25-230 |
2.79e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 45.35 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDGREVAGPG-----------PDRAVVFQNhsllpwl 93
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGltdlrrvlsiiPQSPVLFSG------- 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 94 TVYQNVELAVKQIAGKKGKAwiqeqvnhyLELIQMQHAAHKKP-----------DEISGGMKQRVGIARALALQPKVLLM 162
Cdd:PLN03232 1325 TVRFNIDPFSEHNDADLWEA---------LERAHIKDVIDRNPfgldaevseggENFSVGQRQLLSLARALLRRSKILVL 1395
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491592515 163 DEPFGALDALTRAHLQDAlmkIQAELNN-TVIMITHDVDeAVLLSDKIVMMTNgpaatiGEVLEVNLPR 230
Cdd:PLN03232 1396 DEATASVDVRTDSLIQRT---IREEFKScTMLVIAHRLN-TIIDCDKILVLSS------GQVLEYDSPQ 1454
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
26-198 |
5.11e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 44.34 E-value: 5.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 26 KNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPtDGGVIVDGREVagpgpDRAVVFQNH-SLLPWLTVYQNV----- 99
Cdd:PRK11819 341 DDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQP-DSGTIKIGETV-----KLAYVDQSRdALDPNKTVWEEIsggld 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 100 --ELAVKQIAGK--------KGkawiQEQvnhyleliqmqhaaHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGAL 169
Cdd:PRK11819 415 iiKVGNREIPSRayvgrfnfKG----GDQ--------------QKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDL 476
|
170 180
....*....|....*....|....*....
gi 491592515 170 DALTRAHLQDALmkiqAELNNTVIMITHD 198
Cdd:PRK11819 477 DVETLRALEEAL----LEFPGCAVVISHD 501
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
25-174 |
7.66e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.85 E-value: 7.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHmPT--DGGVIVDGREvAGPGP-----DRAVVFQNHSL-------- 89
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDH-PQgySNDLTLFGRR-RGSGEtiwdiKKHIGYVSSSLhldyrvst 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 90 ----------LPWLTVYQNVELAVKQIAgkkgkawiqeqvNHYLELIQMQHAAHKKP-DEISGGMKQRVGIARALALQPK 158
Cdd:PRK10938 354 svrnvilsgfFDSIGIYQAVSDRQQKLA------------QQWLDILGIDKRTADAPfHSLSWGQQRLALIVRALVKHPT 421
|
170
....*....|....*.
gi 491592515 159 VLLMDEPFGALDALTR 174
Cdd:PRK10938 422 LLILDEPLQGLDPLNR 437
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
25-229 |
5.83e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 41.26 E-value: 5.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTVLNLVAGLHMPTDGGVIVDG-----------REVAGPGPDRAVVFQNhsllpwl 93
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGcdiskfglmdlRKVLGIIPQAPVLFSG------- 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 94 TVYQNVElavkqIAGKKGKAWIQEQvnhyLELIQMQHAAHKKP-----------DEISGGMKQRVGIARALALQPKVLLM 162
Cdd:PLN03130 1328 TVRFNLD-----PFNEHNDADLWES----LERAHLKDVIRRNSlgldaevseagENFSVGQRQLLSLARALLRRSKILVL 1398
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491592515 163 DEPFGALDALTRAHLQDAlmkIQAELNN-TVIMITHDVDeAVLLSDKIVMMTNgpaatiGEVLEVNLP 229
Cdd:PLN03130 1399 DEATAAVDVRTDALIQKT---IREEFKScTMLIIAHRLN-TIIDCDRILVLDA------GRVVEFDTP 1456
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
25-224 |
8.44e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 39.93 E-value: 8.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 25 LKNVDLQINKGEFVSLIGHSGCGKSTV----------LNLVAGL---------HMPTDGgviVDgrEVAGPGPDRAVVFQ 85
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqRRYVESLsayarqflgQMDKPD---VD--SIEGLSPAIAIDQK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 86 NHSLLPWLTV------YQNVELAVKQIAGKKGKAWIQEQVNHYLELiqmqhaaHKKPDEISGGMKQRVGIARAL--ALQP 157
Cdd:cd03270 86 TTSRNPRSTVgtvteiYDYLRLLFARVGIRERLGFLVDVGLGYLTL-------SRSAPTLSGGEAQRIRLATQIgsGLTG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491592515 158 KVLLMDEPFGALDALTRAHLQDALMKIQAeLNNTVIMITHDvDEAVLLSDKIVMMtnGPAATI--GEVL 224
Cdd:cd03270 159 VLYVLDEPSIGLHPRDNDRLIETLKRLRD-LGNTVLVVEHD-EDTIRAADHVIDI--GPGAGVhgGEIV 223
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
115-201 |
1.15e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.00 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 115 IQEQVNH------YLELIQMQHAAHKKPDEISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHLQDALMKIQAEl 188
Cdd:PRK10938 106 IQDEVKDparceqLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS- 184
|
90
....*....|...
gi 491592515 189 NNTVIMITHDVDE 201
Cdd:PRK10938 185 GITLVLVLNRFDE 197
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
17-58 |
2.22e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 39.23 E-value: 2.22e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 491592515 17 TPDGEFIA--------LKNVDLQINKGEFVSLIGHSGCGKSTVLN--LVAGL 58
Cdd:TIGR00630 608 PGNGKFLTlkgarennLKNITVSIPLGLFTCITGVSGSGKSTLINdtLYPAL 659
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
137-224 |
4.05e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.46 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 137 DEISGGMKQRVGIARAL--ALQPKVLLMDEPFGALdaltraHLQDALMKIQA-----ELNNTVIMITHDvDEAVLLSDKI 209
Cdd:TIGR00630 487 GTLSGGEAQRIRLATQIgsGLTGVLYVLDEPSIGL------HQRDNRRLINTlkrlrDLGNTLIVVEHD-EDTIRAADYV 559
|
90
....*....|....*..
gi 491592515 210 VMMtnGPAATI--GEVL 224
Cdd:TIGR00630 560 IDI--GPGAGEhgGEVV 574
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
139-242 |
7.84e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 37.90 E-value: 7.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592515 139 ISGGMKQRVGIARALALQPKVLLMDEPFGALDALTRAHLQDALMKIQAELNNTVIMI-------THDV-DEAVLLSD-KI 209
Cdd:PLN03140 337 ISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSllqpapeTFDLfDDIILLSEgQI 416
|
90 100 110
....*....|....*....|....*....|...
gi 491592515 210 VMmtNGPAATIGEVLEVNLPRPRERVALADDAQ 242
Cdd:PLN03140 417 VY--QGPRDHILEFFESCGFKCPERKGTADFLQ 447
|
|
| |
