|
Name |
Accession |
Description |
Interval |
E-value |
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-256 |
7.84e-124 |
|
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: 352.80 E-value: 7.84e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 1 MAFFKVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARMGI 80
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 81 ARTFQNIELFAHMSTMENLMLGRHRYMKTGLFRGAFMWGRrsfAGKEEVANRKKVEEIIDLLDLQSVRNKFVGGLPYGTQ 160
Cdd:COG0411 82 ARTFQNPRLFPELTVLENVLVAAHARLGRGLLAALLRLPR---ARREEREARERAEELLERVGLADRADEPAGNLSYGQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 161 KQVELGRAlalepqllllDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSPIVEGTPE 240
Cdd:COG0411 159 RRLEIARAlatepkllllDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPA 238
|
250
....*....|....*.
gi 1308832087 241 EVQRNPEVLKAYLGEE 256
Cdd:COG0411 239 EVRADPRVIEAYLGEE 254
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-248 |
4.77e-102 |
|
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: 296.66 E-value: 4.77e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARMGIARTF 84
Cdd:cd03219 2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRTF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 85 QNIELFAHMSTMENLMLGRHRYMKtglfRGAFMWGRRsfagKEEVANRKKVEEIIDLLDLQSVRNKFVGGLPYGTQKQVE 164
Cdd:cd03219 82 QIPRLFPELTVLENVMVAAQARTG----SGLLLARAR----REEREARERAEELLERVGLADLADRPAGELSYGQQRRLE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 165 LGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDtLKVTILLIEHDMKMVMDISDRVLVINFGSPIVEGTPEEVQR 244
Cdd:cd03219 154 IARALATDPKLLLLDEPAAGLNPEETEELAELIRELRE-RGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
....
gi 1308832087 245 NPEV 248
Cdd:cd03219 233 NPRV 236
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
5-256 |
1.20e-95 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 281.11 E-value: 1.20e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARMGIARTF 84
Cdd:PRK11300 7 SVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRTF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 85 QNIELFAHMSTMENLMLGRHRYMKTGLFRG-----AFmwgRRSFAGKEEVAnrkkvEEIIDLLDLQSVRNKFVGGLPYGT 159
Cdd:PRK11300 87 QHVRLFREMTVIENLLVAQHQQLKTGLFSGllktpAF---RRAESEALDRA-----ATWLERVGLLEHANRQAGNLAYGQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 160 QKQVELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSPIVEGTP 239
Cdd:PRK11300 159 QRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTP 238
|
250
....*....|....*..
gi 1308832087 240 EEVQRNPEVLKAYLGEE 256
Cdd:PRK11300 239 EEIRNNPDVIKAYLGEA 255
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-255 |
4.05e-55 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 177.62 E-value: 4.05e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 6 VEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARMGIARTFQ 85
Cdd:COG4674 13 VEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIARLGIGRKFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 86 NIELFAHMSTMENLMLGrhryMKTGlfRGAFmwgrRSFAGKEEVANRKKVEEIIDLLDLQSVRNKFVGGLPYGtQKQ-VE 164
Cdd:COG4674 93 KPTVFEELTVFENLELA----LKGD--RGVF----ASLFARLTAEERDRIEEVLETIGLTDKADRLAGLLSHG-QKQwLE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 165 LGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDtlKVTILLIEHDMKMVMDISDRVLVINFGSPIVEGTPEEVQR 244
Cdd:COG4674 162 IGMLLAQDPKLLLLDEPVAGMTDAETERTAELLKSLAG--KHSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGSLDEVQA 239
|
250
....*....|.
gi 1308832087 245 NPEVLKAYLGE 255
Cdd:COG4674 240 DPRVIEVYLGR 250
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-254 |
4.93e-50 |
|
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: 164.00 E-value: 4.93e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 1 MAFFKVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARMGI 80
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 81 ARTFQNIELFAHMSTMENLMLGrhrymktglfrgafmwgrrSFAGKEEVANRKKVEEIIDLL-DLQSVRNKFVGGLPYGT 159
Cdd:COG0410 81 GYVPEGRRIFPSLTVEENLLLG-------------------AYARRDRAEVRADLERVYELFpRLKERRRQRAGTLSGGE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 160 QKQVELGRALALEPQLLLLDEPSAG----MnseekQDMIF-WIKDIQDTlKVTILLIEHDMKMVMDISDRVLVINFGSPI 234
Cdd:COG0410 142 QQMLAIGRALMSRPKLLLLDEPSLGlaplI-----VEEIFeIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIV 215
|
250 260
....*....|....*....|
gi 1308832087 235 VEGTPEEVQRNPEVLKAYLG 254
Cdd:COG0410 216 LEGTAAELLADPEVREAYLG 235
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-245 |
1.03e-47 |
|
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: 157.60 E-value: 1.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARMGIARTF 84
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 85 QNIELFAHMSTMENLMLGRHRymktglfrgafmwgrrsfagKEEVANRKKVEEIIDLL-DLQSVRNKFVGGLPYGTQKQV 163
Cdd:cd03224 82 EGRRIFPELTVEENLLLGAYA--------------------RRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQML 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 164 ELGRALALEPQLLLLDEPSAG---MNSEEKQDMIFWIKDiqdtLKVTILLIEHDMKMVMDISDRVLVINFGSPIVEGTPE 240
Cdd:cd03224 142 AIARALMSRPKLLLLDEPSEGlapKIVEEIFEAIRELRD----EGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAA 217
|
....*
gi 1308832087 241 EVQRN 245
Cdd:cd03224 218 ELLAD 222
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-231 |
1.41e-39 |
|
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: 136.50 E-value: 1.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPdkvARMGIARTF 84
Cdd:cd03259 2 ELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPP---ERRNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 85 QNIELFAHMSTMENLMLG-RHRYMKtglfrgafmwgrrsfagKEEVanRKKVEEIIDLLDLQSVRNKFVGGLPYGTQKQV 163
Cdd:cd03259 79 QDYALFPHLTVAENIAFGlKLRGVP-----------------KAEI--RARVRELLELVGLEGLLNRYPHELSGGQQQRV 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1308832087 164 ELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFG 231
Cdd:cd03259 140 ALARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEG 207
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-242 |
2.16e-39 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 136.91 E-value: 2.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARMGIarTF 84
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGV--LP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 85 QNIELFAHMSTMENLmlgrhRYmkTGLFRGafMWGRrsfagkeevANRKKVEEIIDLLDLQSVRNKFVGGLPYGTQKQVE 164
Cdd:COG4555 81 DERGLYDRLTVRENI-----RY--FAELYG--LFDE---------ELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 165 LGRALALEPQLLLLDEPSAG---MNSEEKQDMIFWIKDiqdtLKVTILLIEHDMKMVMDISDRVLVINFGSPIVEGTPEE 241
Cdd:COG4555 143 LARALVHDPKVLLLDEPTNGldvMARRLLREILRALKK----EGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDE 218
|
.
gi 1308832087 242 V 242
Cdd:COG4555 219 L 219
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-256 |
2.65e-39 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 136.35 E-value: 2.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 6 VEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARMGIArtFQ 85
Cdd:COG1131 3 VRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYV--PQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 86 NIELFAHMSTMENLmlgrhRYMktglfrgafmwgrRSFAGKEEVANRKKVEEIIDLLDLQSVRNKFVGGLPYGTQKQVEL 165
Cdd:COG1131 81 EPALYPDLTVRENL-----RFF-------------ARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 166 GRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTlKVTILLIEHDMKMVMDISDRVLVINFGSPIVEGTPEEVQRN 245
Cdd:COG1131 143 ALALLHDPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
250
....*....|...
gi 1308832087 246 P--EVLKAYLGEE 256
Cdd:COG1131 222 LleDVFLELTGEE 234
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-246 |
3.91e-39 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 139.08 E-value: 3.91e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 1 MAFFKVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKvaRmGI 80
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK--R-NV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 81 ARTFQNIELFAHMSTMENLMLG-RHRYMKtglfrgafmwgrrsfagKEEVanRKKVEEIIDLLDLQSVRNKFVGGLPyGT 159
Cdd:COG3842 80 GMVFQDYALFPHLTVAENVAFGlRMRGVP-----------------KAEI--RARVAELLELVGLEGLADRYPHQLS-GG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 160 QKQ-VELGRAlalepqllllDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSPIVEGT 238
Cdd:COG3842 140 QQQrVALARAlapeprvlllDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGT 219
|
....*...
gi 1308832087 239 PEEVQRNP 246
Cdd:COG3842 220 PEEIYERP 227
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-248 |
1.53e-38 |
|
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: 134.55 E-value: 1.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 6 VEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKV----ARMGIA 81
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELyrlrRRMGML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 82 rtFQNIELFAHMSTMENLMLGrhRYMKTGLFRgafmwgrrsfagkEEVanRKKVEEIIDLLDLQSVRNKFVGGLPYGTQK 161
Cdd:cd03261 83 --FQSGALFDSLTVFENVAFP--LREHTRLSE-------------EEI--REIVLEKLEAVGLRGAEDLYPAELSGGMKK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 162 QVELGRALALEPQLLLLDEPSAG---MNSEEKQDMifwIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSPIVEGT 238
Cdd:cd03261 144 RVALARALALDPELLLYDEPTAGldpIASGVIDDL---IRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGT 220
|
250
....*....|..
gi 1308832087 239 PEEVQR--NPEV 248
Cdd:cd03261 221 PEELRAsdDPLV 232
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-260 |
4.02e-38 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 133.68 E-value: 4.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 1 MAFFKVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPdKVA---- 76
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARR-RIGyvpq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 77 RMGIARTFQnielfahMSTMENLMLGRHRYMktGLFRgafmwgrrsFAGKEEvanRKKVEEIIDLLDLQSVRNKFVGGLP 156
Cdd:COG1121 83 RAEVDWDFP-------ITVRDVVLMGRYGRR--GLFR---------RPSRAD---REAVDEALERVGLEDLADRPIGELS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 157 yGTQKQ-VELGRALALEPQLLLLDEPSAGM--NSEEkqdmifwikDIQDTLK------VTILLIEHDMKMVMDISDRVLV 227
Cdd:COG1121 142 -GGQQQrVLLARALAQDPDLLLLDEPFAGVdaATEE---------ALYELLRelrregKTILVVTHDLGAVREYFDRVLL 211
|
250 260 270
....*....|....*....|....*....|...
gi 1308832087 228 INfGSPIVEGTPEEVQRNPEVLKAYLGEENAIR 260
Cdd:COG1121 212 LN-RGLVAHGPPEEVLTPENLSRAYGGPVALLA 243
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
5-253 |
9.71e-38 |
|
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: 132.41 E-value: 9.71e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKV----ARMGI 80
Cdd:COG1127 7 EVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELyelrRRIGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 81 ArtFQNIELFAHMSTMENLMLG-RhryMKTGLfrgafmwgrrsfaGKEEVanRKKVEEIIDLLDLQSVRNKFVGGLPYGT 159
Cdd:COG1127 87 L--FQGGALFDSLTVFENVAFPlR---EHTDL-------------SEAEI--RELVLEKLELVGLPGAADKMPSELSGGM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 160 QKQVELGRAlalepqllllDEPSAG---MNSEEKQDMifwIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSPIVE 236
Cdd:COG1127 147 RKRVALARAlaldpeillyDEPTAGldpITSAVIDEL---IRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAE 223
|
250
....*....|....*...
gi 1308832087 237 GTPEEVQRNP-EVLKAYL 253
Cdd:COG1127 224 GTPEELLASDdPWVRQFL 241
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-247 |
1.75e-37 |
|
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: 131.59 E-value: 1.75e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKvarMGIARTF 84
Cdd:cd03300 2 ELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK---RPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 85 QNIELFAHMSTMENLMLGRhrymktglfrgafmwgRRSFAGKEEVanRKKVEEIIDLLDLQSVRNKFVGGLPYGTQKQVE 164
Cdd:cd03300 79 QNYALFPHLTVFENIAFGL----------------RLKKLPKAEI--KERVAEALDLVQLEGYANRKPSQLSGGQQQRVA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 165 LGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSPIVEGTPEEVQR 244
Cdd:cd03300 141 IARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYE 220
|
...
gi 1308832087 245 NPE 247
Cdd:cd03300 221 EPA 223
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-251 |
3.36e-37 |
|
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: 130.92 E-value: 3.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 4 FKVEKLSISF-GGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARM-GIa 81
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKvGL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 82 rTFQNIE--LFahMST-MENLMLG-RHRymktGLfrgafmwgrrsfaGKEEVanRKKVEEIIDLLDLQSVRNKFVGGLPY 157
Cdd:COG1122 80 -VFQNPDdqLF--APTvEEDVAFGpENL----GL-------------PREEI--RERVEEALELVGLEHLADRPPHELSG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 158 GtQKQ---------------VeLgralalepqllllDEPSAGMNSEEKQDMIFWIKDIQDTlKVTILLIEHDMKMVMDIS 222
Cdd:COG1122 138 G-QKQrvaiagvlamepevlV-L-------------DEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELA 201
|
250 260
....*....|....*....|....*....
gi 1308832087 223 DRVLVINFGSPIVEGTPEEVQRNPEVLKA 251
Cdd:COG1122 202 DRVIVLDDGRIVADGTPREVFSDYELLEE 230
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
5-246 |
4.55e-37 |
|
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: 130.92 E-value: 4.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRrpdKVARMGIARTF 84
Cdd:cd03296 4 EVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDV---PVQERNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 85 QNIELFAHMSTMENLMLG---RHRymktglfrgafmwgrRSFAGKEEVanRKKVEEIIDLLDLQSVRNKFVGGLPYGTQK 161
Cdd:cd03296 81 QHYALFRHMTVFDNVAFGlrvKPR---------------SERPPEAEI--RAKVHELLKLVQLDWLADRYPAQLSGGQRQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 162 QVELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSPIVEGTPEE 241
Cdd:cd03296 144 RVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDE 223
|
....*
gi 1308832087 242 VQRNP 246
Cdd:cd03296 224 VYDHP 228
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-254 |
3.34e-36 |
|
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: 128.43 E-value: 3.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 4 FKVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARMGIART 83
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 84 FQNIELFAHMSTMENLMlgrhrymktglfrgAFMwgrrSFAGKEEVANRKKVEEIIDLLDLQSVRNKFVGGLPYGTQKQV 163
Cdd:cd03218 81 PQEASIFRKLTVEENIL--------------AVL----EIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 164 ELGRALALEPQLLLLDEPSAGMnseekqDMIFwIKDIQDTLK------VTILLIEHDMKMVMDISDRVLVINFGSPIVEG 237
Cdd:cd03218 143 EIARALATNPKFLLLDEPFAGV------DPIA-VQDIQKIIKilkdrgIGVLITDHNVRETLSITDRAYIIYEGKVLAEG 215
|
250
....*....|....*..
gi 1308832087 238 TPEEVQRNPEVLKAYLG 254
Cdd:cd03218 216 TPEEIAANELVRKVYLG 232
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-243 |
1.34e-35 |
|
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: 126.72 E-value: 1.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 6 VEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQgRRPDKVaRMGIARTFQ 85
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV-REPREV-RRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 86 NIELFAHMSTMENLmlgrhrYMKTGLFrgAFMWGRRsfagkeevanRKKVEEIIDLLDLQSVRNKFVGGLPYGTQKQVEL 165
Cdd:cd03265 81 DLSVDDELTGWENL------YIHARLY--GVPGAER----------RERIDELLDFVGLLEAADRLVKTYSGGMRRRLEI 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1308832087 166 GRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSPIVEGTPEEVQ 243
Cdd:cd03265 143 ARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
18-247 |
2.79e-35 |
|
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: 126.16 E-value: 2.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 18 ALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKV--ARMGIARTFQNIELFAHMST 95
Cdd:cd03258 20 ALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkARRRIGMIFQHFNLLSSRTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 96 MENLMLGrhryMKtglfrgafmwgrrsFAGKEEVANRKKVEEIIDLLDLQSVRNKFVGGLPyGTQKQ-VELGRALALEPQ 174
Cdd:cd03258 100 FENVALP----LE--------------IAGVPKAEIEERVLELLELVGLEDKADAYPAQLS-GGQKQrVGIARALANNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1308832087 175 LLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSPIVEGTPEEVQRNPE 247
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-251 |
2.92e-35 |
|
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: 126.70 E-value: 2.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 4 FKVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARMgIART 83
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARR-IAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 84 FQNIELFAHMSTMENLMLGRHRYMKtglfrgafMWGRRSfagkeeVANRKKVEEIIDLLDLQSVRNKFV----GGlpygt 159
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGRYPHLG--------LFGRPS------AEDREAVEEALERTGLEHLADRPVdelsGG----- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 160 QKQ-VELGRAlalepqllllDEPSAGMnseekqDM-----IF-WIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGS 232
Cdd:COG1120 142 ERQrVLIARAlaqeppllllDEPTSHL------DLahqleVLeLLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGR 215
|
250
....*....|....*....
gi 1308832087 233 PIVEGTPEEVQrNPEVLKA 251
Cdd:COG1120 216 IVAQGPPEEVL-TPELLEE 233
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
5-257 |
6.24e-35 |
|
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: 125.14 E-value: 6.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISFGGLDaLSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKvarMGIARTF 84
Cdd:cd03299 2 KVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK---RDISYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 85 QNIELFAHMSTMENLMLG-RHRYMKtglfrgafmwgrrsfagKEEVAnrKKVEEIIDLLDLQSVRNKFVGGLPYGTQKQV 163
Cdd:cd03299 78 QNYALFPHMTVYKNIAYGlKKRKVD-----------------KKEIE--RKVLEIAEMLGIDHLLNRKPETLSGGEQQRV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 164 ELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSPIVEGTPEEVQ 243
Cdd:cd03299 139 AIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVF 218
|
250
....*....|....*.
gi 1308832087 244 RNP--EVLKAYLGEEN 257
Cdd:cd03299 219 KKPknEFVAEFLGFNN 234
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-231 |
1.15e-34 |
|
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: 122.68 E-value: 1.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 4 FKVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQ-GRRPDKVARMGIAR 82
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 83 TFQNIELFAHMSTMENLMLgrhrymktglfrgafmwgrrsfagkeevanrkkveeiidlldlqsvrnkfvgGLPYGTQKQ 162
Cdd:cd03229 81 VFQDFALFPHLTVLENIAL----------------------------------------------------GLSGGQQQR 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1308832087 163 VELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFG 231
Cdd:cd03229 109 VALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
6-260 |
1.62e-34 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 126.80 E-value: 1.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 6 VEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPdkVARMGIARTFQ 85
Cdd:COG1118 5 VRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLP--PRERRVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 86 NIELFAHMSTMENLmlgrhrymktglfrgAFmwG-RRSFAGKEEVanRKKVEEIIDLLDLQSVRNKFVGGLPyGTQKQ-V 163
Cdd:COG1118 83 HYALFPHMTVAENI---------------AF--GlRVRPPSKAEI--RARVEELLELVQLEGLADRYPSQLS-GGQRQrV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 164 ELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSPIVEGTPEEVQ 243
Cdd:COG1118 143 ALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVY 222
|
250
....*....|....*....
gi 1308832087 244 RNPEVLKAY--LGEENAIR 260
Cdd:COG1118 223 DRPATPFVArfLGCVNVLR 241
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-231 |
1.69e-33 |
|
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: 120.65 E-value: 1.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISFGGLD--ALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARMgIAR 82
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRK-VGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 83 TFQNIE--LFAHM------STMENLMLGRhrymktglfrgafmwgrrsfagkEEVanRKKVEEIIDLLDLQSVRNKFVGG 154
Cdd:cd03225 80 VFQNPDdqFFGPTveeevaFGLENLGLPE-----------------------EEI--EERVEEALELVGLEGLRDRSPFT 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1308832087 155 LPYGTQKQVELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKvTILLIEHDMKMVMDISDRVLVINFG 231
Cdd:cd03225 135 LSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGK-TIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-231 |
5.20e-33 |
|
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: 119.67 E-value: 5.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKvarMGIARTF 84
Cdd:cd03301 2 ELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD---RDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 85 QNIELFAHMSTMENLmlgrhrymktglfrgAFMWGRRSFaGKEEVanRKKVEEIIDLLDLQSVRNKFVGGLPYGTQKQVE 164
Cdd:cd03301 79 QNYALYPHMTVYDNI---------------AFGLKLRKV-PKDEI--DERVREVAELLQIEHLLDRKPKQLSGGQRQRVA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1308832087 165 LGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFG 231
Cdd:cd03301 141 LGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDG 207
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
4-256 |
7.26e-33 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 120.07 E-value: 7.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 4 FKVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARMGIART 83
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLGIGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 84 FQNIELFAHMSTMENLMlgrhrymktglfrgAFMWGRRSFAGKEEvanRKKVEEIIDLLDLQSVRNKFVGGLPYGTQKQV 163
Cdd:TIGR04406 82 PQEASIFRKLTVEENIM--------------AVLEIRKDLDRAER---EERLEALLEEFQISHLRDNKAMSLSGGERRRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 164 ELGRALALEPQLLLLDEPSAGMNSEEKQDmifwIKDIQDTLK---VTILLIEHDMKMVMDISDRVLVINFGSPIVEGTPE 240
Cdd:TIGR04406 145 EIARALATNPKFILLDEPFAGVDPIAVGD----IKKIIKHLKergIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPA 220
|
250
....*....|....*.
gi 1308832087 241 EVQRNPEVLKAYLGEE 256
Cdd:TIGR04406 221 EIVANEKVRRVYLGEQ 236
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
14-260 |
8.18e-33 |
|
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: 122.65 E-value: 8.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 14 GGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDK---VARMGIARTFQNIELF 90
Cdd:TIGR01186 4 GGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVElreVRRKKIGMVFQQFALF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 91 AHMSTMENLMLGrhryMKtglfrgafmwgrrsFAGKEEVANRKKVEEIIDLLDLQSVRNKFVGGLPYGTQKQVELGRALA 170
Cdd:TIGR01186 84 PHMTILQNTSLG----PE--------------LLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 171 LEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSPIVEGTPEEVQRNP--EV 248
Cdd:TIGR01186 146 AEPDILLMDEAFSALDPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPanEY 225
|
250
....*....|..
gi 1308832087 249 LKAYLGEENAIR 260
Cdd:TIGR01186 226 VEEFIGKVDLSQ 237
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-228 |
1.04e-32 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 124.36 E-value: 1.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 1 MAFFKVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARMGI 80
Cdd:COG1129 2 EPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 81 ARTFQNIELFAHMSTMENLMLGRHRyMKTGLFRGAFMwgrrsfagkeevanRKKVEEIIDLLDLQ-SVRNKfVGGLPYGT 159
Cdd:COG1129 82 AIIHQELNLVPNLSVAENIFLGREP-RRGGLIDWRAM--------------RRRARELLARLGLDiDPDTP-VGDLSVAQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1308832087 160 QKQVELGRALALEPQLLLLDEPSAGMNSEEKqDMIFwikDIQDTLK---VTILLIEHDMKMVMDISDRVLVI 228
Cdd:COG1129 146 QQLVEIARALSRDARVLILDEPTASLTEREV-ERLF---RIIRRLKaqgVAIIYISHRLDEVFEIADRVTVL 213
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-246 |
1.82e-32 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 121.72 E-value: 1.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 1 MAFFKVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKvaRmGI 80
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD--R-NI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 81 ARTFQNIELFAHMSTMENLMLGrhryMKtglFRGAfmwgrrsfaGKEEVanRKKVEEIIDLLDLQSVRNKFVGGLPYGtQ 160
Cdd:COG3839 78 AMVFQSYALYPHMTVYENIAFP----LK---LRKV---------PKAEI--DRRVREAAELLGLEDLLDRKPKQLSGG-Q 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 161 KQ-VELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGspIVE--G 237
Cdd:COG3839 139 RQrVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDG--RIQqvG 216
|
....*....
gi 1308832087 238 TPEEVQRNP 246
Cdd:COG3839 217 TPEELYDRP 225
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
6-257 |
7.14e-32 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 120.19 E-value: 7.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 6 VEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIqGRRPDKVARMGIarTFQ 85
Cdd:PRK10851 5 IANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV-SRLHARDRKVGF--VFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 86 NIELFAHMSTMENLMLGRHrymktglfrgafMWGRRSFAGKEEVanRKKVEEIIDLLDLQSVRNKFVGGLPyGTQKQ-VE 164
Cdd:PRK10851 82 HYALFRHMTVFDNIAFGLT------------VLPRRERPNAAAI--KAKVTQLLEMVQLAHLADRYPAQLS-GGQKQrVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 165 LGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSPIVEGTPEEVQR 244
Cdd:PRK10851 147 LARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWR 226
|
250
....*....|....*.
gi 1308832087 245 NPE---VLKaYLGEEN 257
Cdd:PRK10851 227 EPAtrfVLE-FMGEVN 241
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-243 |
1.79e-31 |
|
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: 116.51 E-value: 1.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 4 FKVEKLSISFGGLD-ALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKV--ARMGI 80
Cdd:cd03256 1 IEVENLSKTYPNGKkALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 81 ARTFQNIELFAHMSTMENLMLGRHRYMKTglfrgafmWgrRSFAGKEEVANRKKVEEIIDLLDLQSVRNKFVGGLPYGTQ 160
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRLGRRST--------W--RSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 161 KQVELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSPIVEGTPE 240
Cdd:cd03256 151 QRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPA 230
|
...
gi 1308832087 241 EVQ 243
Cdd:cd03256 231 ELT 233
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-229 |
5.39e-31 |
|
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: 114.49 E-value: 5.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISFGGLD----ALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDkvarmgI 80
Cdd:cd03293 2 EVRNVSKTYGGGGgavtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 81 ARTFQNIELFAHMSTMENLMLGRhrymktglfrgafmwgRRSFAGKEEVanRKKVEEIIDLLDLQSVRNKFVGGLPYGTQ 160
Cdd:cd03293 76 GYVFQQDALLPWLTVLDNVALGL----------------ELQGVPKAEA--RERAEELLELVGLSGFENAYPHQLSGGMR 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1308832087 161 KQVELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVIN 229
Cdd:cd03293 138 QRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLS 206
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-229 |
5.96e-31 |
|
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: 114.17 E-value: 5.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRpDKVA----RMGI 80
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER-KRIGyvpqRRSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 81 ARTFQnielfahMSTMENLMLGRhrymktglfrgafmWGRRSFAGKEEVANRKKVEEIIDLLDLQSVRNKFVGGLPYGTQ 160
Cdd:cd03235 80 DRDFP-------ISVRDVVLMGL--------------YGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQ 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1308832087 161 KQVELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKvTILLIEHDMKMVMDISDRVLVIN 229
Cdd:cd03235 139 QRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGM-TILVVTHDLGLVLEYFDRVLLLN 206
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-241 |
2.20e-30 |
|
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: 112.98 E-value: 2.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISFGGLD--ALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIqgRRPDKVARMGIAR 82
Cdd:cd03263 2 QIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI--RTDRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 83 TFQNIELFAHMSTMENLMLgrhrymktglfrgafmWGRrsFAGKEEVANRKKVEEIIDLLDLQSVRNKFVGGLPYGTQKQ 162
Cdd:cd03263 80 CPQFDALFDELTVREHLRF----------------YAR--LKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 163 VELGRALALEPQLLLLDEPSAGMNSEEKQDMifW--IKDIQDtlKVTILLIEHDMKMVMDISDRVLVINFGSPIVEGTPE 240
Cdd:cd03263 142 LSLAIALIGGPSVLLLDEPTSGLDPASRRAI--WdlILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQ 217
|
.
gi 1308832087 241 E 241
Cdd:cd03263 218 E 218
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-256 |
4.09e-30 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 112.82 E-value: 4.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 1 MAFFKVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARMGI 80
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 81 ARTFQNIELFAHMSTMENLMlgrhrymktglfrgAFMwgrrSFAGKEEVANRKKVEEIIDLLDLQSVRNKFVGGLPYGTQ 160
Cdd:COG1137 81 GYLPQEASIFRKLTVEDNIL--------------AVL----ELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGER 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 161 KQVELGRALALEPQLLLLDEPSAG---MNSEEKQDMIFWIKDiqdtLKVTILLIEHDMKMVMDISDRVLVINFGSPIVEG 237
Cdd:COG1137 143 RRVEIARALATNPKFILLDEPFAGvdpIAVADIQKIIRHLKE----RGIGVLITDHNVRETLGICDRAYIISEGKVLAEG 218
|
250
....*....|....*....
gi 1308832087 238 TPEEVQRNPEVLKAYLGEE 256
Cdd:COG1137 219 TPEEILNNPLVRKVYLGED 237
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
3-257 |
1.31e-29 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 114.05 E-value: 1.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 3 FFKVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIvFKD------REIQGRrpdkva 76
Cdd:PRK11432 6 FVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQI-FIDgedvthRSIQQR------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 77 rmGIARTFQNIELFAHMSTMENLMLGrhryMKtglfrgafMWGRrsfaGKEEVANRkkVEEIIDLLDLQSVRNKFVGGLP 156
Cdd:PRK11432 79 --DICMVFQSYALFPHMSLGENVGYG----LK--------MLGV----PKEERKQR--VKEALELVDLAGFEDRYVDQIS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 157 YGTQKQVELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSPIVE 236
Cdd:PRK11432 139 GGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQI 218
|
250 260
....*....|....*....|...
gi 1308832087 237 GTPEEVQRNP--EVLKAYLGEEN 257
Cdd:PRK11432 219 GSPQELYRQPasRFMASFMGDAN 241
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-246 |
3.09e-29 |
|
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: 115.00 E-value: 3.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISF-----GGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARMG 79
Cdd:COG1123 262 EVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRELR 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 80 --IARTFQNIE--LFAHMSTMENLM--LGRHRYMKtglfrgafmwgrrsfagKEEVanRKKVEEIIDLLDLQ-SVRNKFV 152
Cdd:COG1123 342 rrVQMVFQDPYssLNPRMTVGDIIAepLRLHGLLS-----------------RAER--RERVAELLERVGLPpDLADRYP 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 153 GGLPYGtQKQ-VELGRALALEPQLLLLDEPSAG---------MNSeekqdmifwIKDIQDTLKVTILLIEHDMKMVMDIS 222
Cdd:COG1123 403 HELSGG-QRQrVAIARALALEPKLLILDEPTSAldvsvqaqiLNL---------LRDLQRELGLTYLFISHDLAVVRYIA 472
|
250 260
....*....|....*....|....*
gi 1308832087 223 DRVLVINFGSpIVE-GTPEEVQRNP 246
Cdd:COG1123 473 DRVAVMYDGR-IVEdGPTEEVFANP 496
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-256 |
4.56e-29 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 109.98 E-value: 4.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 1 MAFFKVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARMGI 80
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 81 ARTFQNIELFAHMSTMENLMlgrhrymktglfrgAFMWGRRSFAGKEEvanRKKVEEIIDLLDLQSVRNKFVGGLPYGTQ 160
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLM--------------AVLQIRDDLSAEQR---EDRANELMEEFHIEHLRDSMGQSLSGGER 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 161 KQVELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTlKVTILLIEHDMKMVMDISDRVLVINFGSPIVEGTPE 240
Cdd:PRK10895 144 RRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPT 222
|
250
....*....|....*.
gi 1308832087 241 EVQRNPEVLKAYLGEE 256
Cdd:PRK10895 223 EILQDEHVKRVYLGED 238
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
5-255 |
4.64e-29 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 109.84 E-value: 4.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISFGGLdaLSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKvaRmGIARTF 84
Cdd:COG3840 3 RLDDLTYRYGDF--PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE--R-PVSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 85 QNIELFAHMSTMENLMLGRHRYMKTGlfrgafmwgrrsfagkeeVANRKKVEEIIDLLDLQSVRNKFVGGLPYGTQKQVE 164
Cdd:COG3840 78 QENNLFPHLTVAQNIGLGLRPGLKLT------------------AEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 165 LGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSPIVEGTPEEVQ- 243
Cdd:COG3840 140 LARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLd 219
|
250
....*....|...
gi 1308832087 244 -RNPEVLKAYLGE 255
Cdd:COG3840 220 gEPPPALAAYLGI 232
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
18-246 |
9.62e-29 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 110.04 E-value: 9.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 18 ALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQG---RRPDKVARMGIARTFQNIELFAHMS 94
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAmsrKELRELRRKKISMVFQSFALLPHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 95 TMENLMLGRhrymktglfrgafmwgrrSFAGKEEVANRKKVEEIIDLLDLQSVRNKFVGGLPYGTQKQVELGRALALEPQ 174
Cdd:cd03294 119 VLENVAFGL------------------EVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPD 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1308832087 175 LLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSPIVEGTPEEVQRNP 246
Cdd:cd03294 181 ILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNP 252
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-226 |
1.11e-28 |
|
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: 108.39 E-value: 1.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 4 FKVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPD-KVARMGIAR 82
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNiNELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 83 TFQNIELFAHMSTMENLMLgrhrymktglfrgAFMWGRrsfaGKEEVANRKKVEEIIDLLDLQSVRNKFVGGLPYGTQKQ 162
Cdd:cd03262 81 VFQQFNLFPHLTVLENITL-------------APIKVK----GMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 163 VELGRALALEPQLLLLDEPSAGMNSEekqdmifWIKDIQDTLK------VTILLIEHDMKMVMDISDRVL 226
Cdd:cd03262 144 VAIARALAMNPKVMLFDEPTSALDPE-------LVGEVLDVMKdlaeegMTMVVVTHEMGFAREVADRVI 206
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-228 |
3.33e-28 |
|
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: 107.19 E-value: 3.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISFGGLD----ALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVAR--- 77
Cdd:cd03255 2 ELKNLSKTYGGGGekvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAfrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 78 --MGIarTFQNIELFAHMSTMENLMLGRHrymktglfrgafmwgrrsFAGKEEVANRKKVEEIIDLLDLQSVRNKFVGGL 155
Cdd:cd03255 82 rhIGF--VFQSFNLLPDLTALENVELPLL------------------LAGVPKKERRERAEELLERVGLGDRLNHYPSEL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1308832087 156 PYGTQKQVELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVmDISDRVLVI 228
Cdd:cd03255 142 SGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIEL 213
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
22-246 |
3.85e-28 |
|
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: 110.20 E-value: 3.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 22 INFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRR-----PDKVARMGIarTFQNIELFAHMSTM 96
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRkgiflPPEKRRIGY--VFQEARLFPHLSVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 97 ENLMLGRHRYMktglfrgafmwgrrsfaGKEEVANRkkvEEIIDLLDLQSVRNKFVGGLPYGTQKQVELGRALALEPQLL 176
Cdd:TIGR02142 94 GNLRYGMKRAR-----------------PSERRISF---ERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 177 LLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSPIVEGTPEEVQRNP 246
Cdd:TIGR02142 154 LMDEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
12-228 |
5.53e-28 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 111.66 E-value: 5.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 12 SFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARMGIARTFQNIELFA 91
Cdd:COG3845 14 RFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALGIGMVHQHFMLVP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 92 HMSTMENLMLGRHRymktglfrgafmwGRRSFAGKEEVanRKKVEEIIDLLDLQsVR-NKFVGGLPYGTQKQVELGRALA 170
Cdd:COG3845 94 NLTVAENIVLGLEP-------------TKGGRLDRKAA--RARIRELSERYGLD-VDpDAKVEDLSVGEQQRVEILKALY 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1308832087 171 LEPQLLLLDEPSAGMNSEEKQDMIfwikdiqDTLK------VTILLIEHDMKMVMDISDRVLVI 228
Cdd:COG3845 158 RGARILILDEPTAVLTPQEADELF-------EILRrlaaegKSIIFITHKLREVMAIADRVTVL 214
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-256 |
9.59e-28 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 111.03 E-value: 9.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 3 FFKVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARMGIAR 82
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 83 TFQNIELFAHMSTMENLMLGRHRYMKtglfrgafMWGRRSFAGKEEvanRKKVEEIIDLLDLQSVRNKFVGGLPYGTQKQ 162
Cdd:PRK09700 85 IYQELSVIDELTVLENLYIGRHLTKK--------VCGVNIIDWREM---RVRAAMMLLRVGLKVDLDEKVANLSISHKQM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 163 VELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKvTILLIEHDMKMVMDISDRVLVINFGSPIVEGTPEEV 242
Cdd:PRK09700 154 LEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGT-AIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
250
....*....|....
gi 1308832087 243 QrNPEVLKAYLGEE 256
Cdd:PRK09700 233 S-NDDIVRLMVGRE 245
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-101 |
9.79e-28 |
|
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: 104.40 E-value: 9.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARMGIArtF 84
Cdd:cd03230 2 EVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYL--P 79
|
90
....*....|....*..
gi 1308832087 85 QNIELFAHMSTMENLML 101
Cdd:cd03230 80 EEPSLYENLTVRENLKL 96
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
21-234 |
1.85e-27 |
|
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: 105.07 E-value: 1.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 21 NINFEVqEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDR-----EIQGRRPdkVARMGIARTFQNIELFAHMST 95
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsRKKINLP--PQQRKIGLVFQQYALFPHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 96 MENLMLGrhryMKtglfrgafmwgrrsfaGKEEVANRKKVEEIIDLLDLQSVRNKFVGGLPYGTQKQVELGRALALEPQL 175
Cdd:cd03297 93 RENLAFG----LK----------------RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPEL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1308832087 176 LLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSPI 234
Cdd:cd03297 153 LLLDEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-251 |
2.29e-27 |
|
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: 109.99 E-value: 2.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 6 VEKLSISF--GGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPS---RGRIVFKDREIQGRRPDKVARMgI 80
Cdd:COG1123 7 VRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR-I 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 81 ARTFQNIELFAHMSTMENLMlgrhrymktglfrgAFMWGRRSFAGKEEvanRKKVEEIIDLLDLQSVRNKFVGGLPyGTQ 160
Cdd:COG1123 86 GMVFQDPMTQLNPVTVGDQI--------------AEALENLGLSRAEA---RARVLELLEAVGLERRLDRYPHQLS-GGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 161 KQ-VELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSPIVEGTP 239
Cdd:COG1123 148 RQrVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPP 227
|
250
....*....|..
gi 1308832087 240 EEVQRNPEVLKA 251
Cdd:COG1123 228 EEILAAPQALAA 239
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-254 |
3.61e-27 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 105.08 E-value: 3.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVA-RMGIART 83
Cdd:COG1126 3 EIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKlRRKVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 84 FQNIELFAHMSTMENLMLG--RHRYMKtglfrgafmwgrrsfagKEEVanRKKVEEIIDLLDLQSVRNKFVGGLPyGTQK 161
Cdd:COG1126 83 FQQFNLFPHLTVLENVTLApiKVKKMS-----------------KAEA--EERAMELLERVGLADKADAYPAQLS-GGQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 162 Q-VELGRALALepqlllldEPSAgmnseekqdMIF----------WIKDIQDTLK------VTILLIEHDMKMVMDISDR 224
Cdd:COG1126 143 QrVAIARALAM--------EPKV---------MLFdeptsaldpeLVGEVLDVMRdlakegMTMVVVTHEMGFAREVADR 205
|
250 260 270
....*....|....*....|....*....|..
gi 1308832087 225 VLVINFGSPIVEGTPEEVQRNP--EVLKAYLG 254
Cdd:COG1126 206 VVFMDGGRIVEEGPPEEFFENPqhERTRAFLS 237
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-227 |
1.06e-26 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 104.02 E-value: 1.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 1 MAFFKVEKLSISF----GGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDkva 76
Cdd:COG1116 5 APALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 77 rMGIArtFQNIELFAHMSTMENLMLGRHrymktglfrgafmwgrrsFAGKEEVANRKKVEEIIDLLDLQSVRNKFvgglP 156
Cdd:COG1116 82 -RGVV--FQEPALLPWLTVLDNVALGLE------------------LRGVPKAERRERARELLELVGLAGFEDAY----P 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1308832087 157 Y---GTQKQ-VELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDmkmvMD----ISDRVLV 227
Cdd:COG1116 137 HqlsGGMRQrVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHD----VDeavfLADRVVV 211
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-259 |
1.16e-26 |
|
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: 103.53 E-value: 1.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISFGGLD-ALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIqgRRPDKVA-RMGIAR 82
Cdd:cd03295 2 EFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDI--REQDPVElRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 83 TFQNIELFAHMSTMENLMLgrhrymktglfrgafmwgRRSFAGKEEVANRKKVEEIIDLLDL--QSVRNKFVGGLPYGTQ 160
Cdd:cd03295 80 VIQQIGLFPHMTVEENIAL------------------VPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 161 KQVELGRALALEPQLLLLDEPSAG---MNSEEKQDMifwIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSPIVEG 237
Cdd:cd03295 142 QRVGVARALAADPPLLLMDEPFGAldpITRDQLQEE---FKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVG 218
|
250 260
....*....|....*....|....
gi 1308832087 238 TPEEVQRNP--EVLKAYLGEENAI 259
Cdd:cd03295 219 TPDEILRSPanDFVAEFVGADRLL 242
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-254 |
2.12e-26 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 103.03 E-value: 2.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 1 MAFFKVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARMGI 80
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 81 ARTFQNIELFAHMSTMENLMLgrhrymktglfrGAFmwgrrsFAGKEEVANRkkVEEIIDLLD-LQSVRNKFVGGLPYGT 159
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAM------------GGF------FAERDQFQER--IKWVYELFPrLHERRIQRAGTMSGGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 160 QKQVELGRALALEPQLLLLDEPSAGMNSeekqdmiFWIKDIQDTLK------VTILLIEHDMKMVMDISDRVLVINFGSP 233
Cdd:PRK11614 143 QQMLAIGRALMSQPRLLLLDEPSLGLAP-------IIIQQIFDTIEqlreqgMTIFLVEQNANQALKLADRGYVLENGHV 215
|
250 260
....*....|....*....|.
gi 1308832087 234 IVEGTPEEVQRNPEVLKAYLG 254
Cdd:PRK11614 216 VLEDTGDALLANEAVRSAYLG 236
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-237 |
2.12e-26 |
|
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: 102.30 E-value: 2.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQgRRPDKVARMGIArtf 84
Cdd:cd03268 2 KTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ-KNIEALRRIGAL--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 85 qnIE---LFAHMSTMENLMLGRHRYMKtglfrgafmwgrrsfagkeevaNRKKVEEIIDLLDLQSVRNKFVGGLPYGTQK 161
Cdd:cd03268 78 --IEapgFYPNLTARENLRLLARLLGI----------------------RKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 162 QVELGRALALEPQLLLLDEPSAGMNSEEkqdmifwIKDIQDTLK------VTILLIEHDMKMVMDISDRVLVINFGSPIV 235
Cdd:cd03268 134 RLGIALALLGNPDLLILDEPTNGLDPDG-------IKELRELILslrdqgITVLISSHLLSEIQKVADRIGIINKGKLIE 206
|
..
gi 1308832087 236 EG 237
Cdd:cd03268 207 EG 208
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
2-237 |
4.78e-26 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 102.03 E-value: 4.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 2 AFFKVEKLSIsfgglDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARMGIA 81
Cdd:cd03267 25 SLFKRKYREV-----EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 82 RTfQNIELFAHMSTMENLMLGRHRYmktglfrgafmwgrrsfaGKEEVANRKKVEEIIDLLDLQSVRNKFVGGLPYGTQK 161
Cdd:cd03267 100 FG-QKTQLWWDLPVIDSFYLLAAIY------------------DLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1308832087 162 QVELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSPIVEG 237
Cdd:cd03267 161 RAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
8-256 |
4.90e-26 |
|
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: 104.41 E-value: 4.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 8 KLSISFGGLDaLsNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQ----------GRRPdkvar 77
Cdd:COG4148 6 DFRLRRGGFT-L-DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQdsargiflppHRRR----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 78 mgIARTFQNIELFAHMSTMENLMLGRhrymktglfrgafmwgRRSFAGkeevANRKKVEEIIDLLDLQSVRNKFVGGLPy 157
Cdd:COG4148 79 --IGYVFQEARLFPHLSVRGNLLYGR----------------KRAPRA----ERRISFDEVVELLGIGHLLDRRPATLS- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 158 GTQKQ-VELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSPIVE 236
Cdd:COG4148 136 GGERQrVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVAS 215
|
250 260
....*....|....*....|
gi 1308832087 237 GTPEEVQRNPEVLKAYLGEE 256
Cdd:COG4148 216 GPLAEVLSRPDLLPLAGGEE 235
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
18-252 |
6.40e-25 |
|
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: 99.83 E-value: 6.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 18 ALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKV----ARMGIArtFQNIE--LFA 91
Cdd:TIGR04521 20 ALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLkdlrKKVGLV--FQFPEhqLFE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 92 hMSTMENLMLGRHRYmktGLfrgafmwgrrsfaGKEEVANRkkVEEIIDLLdlqsvrnkfvgGLPY-----------GTQ 160
Cdd:TIGR04521 98 -ETVYKDIAFGPKNL---GL-------------SEEEAEER--VKEALELV-----------GLDEeylerspfelsGGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 161 K-------------QVELgralalepqlllLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLV 227
Cdd:TIGR04521 148 MrrvaiagvlamepEVLI------------LDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIV 215
|
250 260
....*....|....*....|....*
gi 1308832087 228 INFGSPIVEGTPEEVQRNPEVLKAY 252
Cdd:TIGR04521 216 MHKGKIVLDGTPREVFSDVDELEKI 240
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-253 |
9.16e-25 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 98.63 E-value: 9.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 1 MAFFKveKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPD-KVARMG 79
Cdd:PRK09493 1 MIEFK--NVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDeRLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 80 IARTFQNIELFAHMSTMENLMLGRHRymktglFRGafmwgrrsfAGKEEVanRKKVEEIIDLLDLQSVRNKFVGGLPYGT 159
Cdd:PRK09493 79 AGMVFQQFYLFPHLTALENVMFGPLR------VRG---------ASKEEA--EKQARELLAKVGLAERAHHYPSELSGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 160 QKQVELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTlKVTILLIEHDMKMVMDISDRVLVINFGSPIVEGTP 239
Cdd:PRK09493 142 QQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDP 220
|
250
....*....|....*.
gi 1308832087 240 EEVQRNP--EVLKAYL 253
Cdd:PRK09493 221 QVLIKNPpsQRLQEFL 236
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-247 |
1.06e-24 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 98.67 E-value: 1.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 1 MAFFKVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRP-------D 73
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSlsqqkglI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 74 KVARMGIARTFQNIELFAHMSTMENLMLGRHRYMKT----GLFRGAFMWGRRSFAGKEEVANRKkveeiidlldlqsvrn 149
Cdd:PRK11264 81 RQLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEpkeeATARARELLAKVGLAGKETSYPRR---------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 150 kfvggLPYGTQKQVELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTlKVTILLIEHDMKMVMDISDRVLVIN 229
Cdd:PRK11264 145 -----LSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMD 218
|
250
....*....|....*...
gi 1308832087 230 FGSPIVEGTPEEVQRNPE 247
Cdd:PRK11264 219 QGRIVEQGPAKALFADPQ 236
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-183 |
1.51e-24 |
|
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: 95.41 E-value: 1.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 19 LSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQgRRPDKVARMGIARTFQNIELFAHMSTMEN 98
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLT-DDERKSLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 99 LMLGRHRYmktGLFRGAFmwgrrsfagkeevanRKKVEEIIDLLDLQSVRNKFVGGLPY---GTQKQ-VELGRALALEPQ 174
Cdd:pfam00005 80 LRLGLLLK---GLSKREK---------------DARAEEALEKLGLGDLADRPVGERPGtlsGGQRQrVAIARALLTKPK 141
|
....*....
gi 1308832087 175 LLLLDEPSA 183
Cdd:pfam00005 142 LLLLDEPTA 150
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
15-250 |
1.87e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 98.77 E-value: 1.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 15 GLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFkdreiqGRRPDKVARMGIARTFQNI------- 87
Cdd:PRK13636 18 GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILF------DGKPIDYSRKGLMKLRESVgmvfqdp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 88 --ELFAhMSTMENLMLGrhrYMKTGLfrgafmwgrrsfaGKEEVanRKKVEEIIDLLDLQSVRNKFVGGLPYGTQKQVEL 165
Cdd:PRK13636 92 dnQLFS-ASVYQDVSFG---AVNLKL-------------PEDEV--RKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 166 GRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSPIVEGTPEEVQRN 245
Cdd:PRK13636 153 AGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
....*
gi 1308832087 246 PEVLK 250
Cdd:PRK13636 233 KEMLR 237
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-247 |
1.97e-24 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 99.77 E-value: 1.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISF----GGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKV--ARM 78
Cdd:COG1135 3 ELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELraARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 79 GIARTFQNIELFAHMSTMENLMLGrhryMKtglfrgafmwgrrsFAGKEEVANRKKVEEIIDLLDLQSVRNKFV----GG 154
Cdd:COG1135 83 KIGMIFQHFNLLSSRTVAENVALP----LE--------------IAGVPKAEIRKRVAELLELVGLSDKADAYPsqlsGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 155 lpygtQKQ-VELGRAlalepqllllDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSp 233
Cdd:COG1135 145 -----QKQrVGIARAlannpkvllcDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGR- 218
|
250
....*....|....*
gi 1308832087 234 IVE-GTPEEVQRNPE 247
Cdd:COG1135 219 IVEqGPVLDVFANPQ 233
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
14-255 |
2.10e-24 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 99.88 E-value: 2.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 14 GGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQ--GRRPDKVARMGIARTFQNIELFA 91
Cdd:PRK11153 16 RTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTalSEKELRKARRQIGMIFQHFNLLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 92 HMSTMENLMLGrhryMKtglfrgafmwgrrsFAGKEEVANRKKVEEIIDLLDLQSVRNKFVGGLPyGTQKQ-VELGRALA 170
Cdd:PRK11153 96 SRTVFDNVALP----LE--------------LAGTPKAEIKARVTELLELVGLSDKADRYPAQLS-GGQKQrVAIARALA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 171 LEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSPIVEGTPEEVQRNP--EV 248
Cdd:PRK11153 157 SNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPkhPL 236
|
....*..
gi 1308832087 249 LKAYLGE 255
Cdd:PRK11153 237 TREFIQS 243
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-242 |
4.94e-24 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 96.27 E-value: 4.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISF-GGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVA----RMG 79
Cdd:COG2884 3 RFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPylrrRIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 80 IarTFQNIELFAHMSTMENLMLGrhryMKtglfrgafmwgrrsFAGKEEVANRKKVEEIIDLLDLQSVRNKFVGGLPYGT 159
Cdd:COG2884 83 V--VFQDFRLLPDRTVYENVALP----LR--------------VTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 160 QKQVELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDtLKVTILLIEHDMKMVMDISDRVLVINFGSpIVEGTP 239
Cdd:COG2884 143 QQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGR-LVRDEA 220
|
...
gi 1308832087 240 EEV 242
Cdd:COG2884 221 RGV 223
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-242 |
6.32e-24 |
|
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: 96.10 E-value: 6.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 4 FKVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIY-----RPSRGRIVFKDREIQGRRPDKVA-R 77
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVDVLElR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 78 MGIARTFQNIELFaHMSTMENLMLG-RHRymktGlfrgafMWGRRSFAGKEEVANRKkveeiIDLLDlqSVRNKFVG-GL 155
Cdd:cd03260 81 RRVGMVFQKPNPF-PGSIYDNVAYGlRLH----G------IKLKEELDERVEEALRK-----AALWD--EVKDRLHAlGL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 156 PYGTQKQVELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDtlKVTILLIEHDMKMVMDISDRVLVINFGSPIV 235
Cdd:cd03260 143 SGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKK--EYTIVIVTHNMQQAARVADRTAFLLNGRLVE 220
|
....*..
gi 1308832087 236 EGTPEEV 242
Cdd:cd03260 221 FGPTEQI 227
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-246 |
7.92e-24 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 98.75 E-value: 7.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQG----RRPdkvarmgI 80
Cdd:PRK11607 21 EIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHvppyQRP-------I 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 81 ARTFQNIELFAHMSTMENLMLGRhrymktglfrgafmwgRRSFAGKEEVANRkkVEEIIDLLDLQSVRNKFVGGLPYGTQ 160
Cdd:PRK11607 94 NMMFQSYALFPHMTVEQNIAFGL----------------KQDKLPKAEIASR--VNEMLGLVHMQEFAKRKPHQLSGGQR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 161 KQVELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSPIVEGTPE 240
Cdd:PRK11607 156 QRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPE 235
|
....*.
gi 1308832087 241 EVQRNP 246
Cdd:PRK11607 236 EIYEHP 241
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-231 |
9.05e-24 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 94.03 E-value: 9.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 4 FKVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARMGIART 83
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 84 FQnielfahmstmenlmlgrhrymktglfrgafmwgrrsfagkeevanrkkveeiidlldlqsvrnkfvggLPYGTQKQV 163
Cdd:cd03216 81 YQ---------------------------------------------------------------------LSVGERQMV 91
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1308832087 164 ELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTlKVTILLIEHDMKMVMDISDRVLVINFG 231
Cdd:cd03216 92 EIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDG 158
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
15-250 |
1.12e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 96.69 E-value: 1.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 15 GLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKV-ARMGIARTFQNI--ELFA 91
Cdd:PRK13639 14 GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLeVRKTVGIVFQNPddQLFA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 92 HmSTMENLMLGRhryMKTGLfrgafmwgrrsfaGKEEVANRkkVEEIIDLLDLQSVRNKFVGGLPYGTQKQVELGRALAL 171
Cdd:PRK13639 94 P-TVEEDVAFGP---LNLGL-------------SKEEVEKR--VKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1308832087 172 EPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTlKVTILLIEHDMKMVMDISDRVLVINFGSPIVEGTPEEVQRNPEVLK 250
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETIR 232
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
5-228 |
1.71e-23 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 94.73 E-value: 1.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISFG----GLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARM-- 78
Cdd:COG1136 6 ELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARLrr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 79 ---GIArtFQNIELFAHMSTMENLMLGRHrymktglfrgafmwgrrsFAGKEEVANRKKVEEIIDLLDLQSVRNKFV--- 152
Cdd:COG1136 86 rhiGFV--FQFFNLLPELTALENVALPLL------------------LAGVSRKERRERARELLERVGLGDRLDHRPsql 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 153 -GGlpygtQKQ-VELGRALALEPQLLLLDEPSA---GMNSEEKQDMifwIKDIQDTLKVTILLIEHDMKmVMDISDRVLV 227
Cdd:COG1136 146 sGG-----QQQrVAIARALVNRPKLILADEPTGnldSKTGEEVLEL---LRELNRELGTTIVMVTHDPE-LAARADRVIR 216
|
.
gi 1308832087 228 I 228
Cdd:COG1136 217 L 217
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
34-260 |
1.74e-23 |
|
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: 96.79 E-value: 1.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 34 IIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDkvaRMGIARTFQNIELFAHMSTMENLMLGRhrymktglfr 113
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH---LRHINMVFQSYALFPHMTVEENVAFGL---------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 114 gafmwgRRSFAGKEEVANRkkVEEIIDLLDLQSVRNKFVGGLPYGTQKQVELGRALALEPQLLLLDEPSAGMNSEEKQDM 193
Cdd:TIGR01187 68 ------KMRKVPRAEIKPR--VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQM 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1308832087 194 IFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSPIVEGTPEEVQRNP--EVLKAYLGEENAIR 260
Cdd:TIGR01187 140 QLELKTIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPanLFVARFIGEINVFE 208
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-237 |
1.94e-23 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 94.27 E-value: 1.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARMGIARTf 84
Cdd:cd03269 2 EVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIGYLPEERG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 85 qnieLFAHMSTMENLM-LGRHRYMKtglfrgafmwgrrsfagKEEVANRkkVEEIIDLLDLQSVRNKFVGGLPYGTQKQV 163
Cdd:cd03269 81 ----LYPKMKVIDQLVyLAQLKGLK-----------------KEEARRR--IDEWLERLELSEYANKRVEELSKGNQQKV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 164 ELGRALALEPQLLLLDEPSAG---MNSEekqdmifWIKDIQDTLK---VTILLIEHDMKMVMDISDRVLVINFGSPIVEG 237
Cdd:cd03269 138 QFIAAVIHDPELLILDEPFSGldpVNVE-------LLKDVIRELAragKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-231 |
3.80e-23 |
|
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: 92.31 E-value: 3.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIqGRRPDKVARMGIARTF 84
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDI-AKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 85 QnielfahMStmenlmlgrhrymktglfrgafmwgrrsfagkeevanrkkveeiidlldlqsvrnkfvGGlpygtQKQ-V 163
Cdd:cd00267 80 Q-------LS----------------------------------------------------------GG-----QRQrV 89
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1308832087 164 ELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTlKVTILLIEHDMKMVMDISDRVLVINFG 231
Cdd:cd00267 90 ALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-244 |
4.57e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 95.18 E-value: 4.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARM----Gi 80
Cdd:COG4152 3 ELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRIGYLpeerG- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 81 artfqnieLFAHMSTMENLM-LGRHRYMKtglfrgafmwgrrsfagKEEVanRKKVEEIIDLLDLQSVRNKFVGGLPYGT 159
Cdd:COG4152 82 --------LYPKMKVGEQLVyLARLKGLS-----------------KAEA--KRRADEWLERLGLGDRANKKVEELSKGN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 160 QKQVELGRALALEPQLLLLDEPSAG---MNSEekqdmifWIKDIQDTLK---VTILLIEHDMKMVMDISDRVLVINFGSP 233
Cdd:COG4152 135 QQKVQLIAALLHDPELLILDEPFSGldpVNVE-------LLKDVIRELAakgTTVIFSSHQMELVEELCDRIVIINKGRK 207
|
250
....*....|.
gi 1308832087 234 IVEGTPEEVQR 244
Cdd:COG4152 208 VLSGSVDEIRR 218
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-168 |
6.32e-23 |
|
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: 92.93 E-value: 6.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 4 FKVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARMGIArt 83
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYL-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 84 FQNIELFAHMSTMENLMLGRHrymktglfrgafMWGRRsfagkeevANRKKVEEIIDLLDLQSVRNKFVGGLPYGTQKQV 163
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAA------------LYGLR--------ADREAIDEALEAVGLAGLADLPVRQLSAGQKRRV 140
|
....*
gi 1308832087 164 ELGRA 168
Cdd:COG4133 141 ALARL 145
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
18-250 |
7.76e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 94.34 E-value: 7.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 18 ALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRR---PDKVARMGIARTFQNIELFAHms 94
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKvklSDIRKKVGLVFQYPEYQLFEE-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 95 TMENLMlgrhrymktglfrgAFmwGRRSFA-GKEEVANR-KKVEEIIDLlDLQSVRNKFVGGLPYGTQKQVELGRALALE 172
Cdd:PRK13637 100 TIEKDI--------------AF--GPINLGlSEEEIENRvKRAMNIVGL-DYEDYKDKSPFELSGGQKRRVAIAGVVAME 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1308832087 173 PQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSPIVEGTPEEVQRNPEVLK 250
Cdd:PRK13637 163 PKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVETLE 240
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-249 |
1.18e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 93.71 E-value: 1.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 1 MAFFKVEKLSISF-GGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVaRMG 79
Cdd:PRK13652 1 MHLIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREV-RKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 80 IARTFQNIELFAHMSTME-NLMLGRhryMKTGLfrgafmwgrrsfaGKEEVANRkkVEEIIDLLDLQSVRNKFVGGLPYG 158
Cdd:PRK13652 80 VGLVFQNPDDQIFSPTVEqDIAFGP---INLGL-------------DEETVAHR--VSSALHMLGLEELRDRVPHHLSGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 159 TQKQVELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSPIVEGT 238
Cdd:PRK13652 142 EKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGT 221
|
250
....*....|.
gi 1308832087 239 PEEVQRNPEVL 249
Cdd:PRK13652 222 VEEIFLQPDLL 232
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
14-231 |
2.66e-22 |
|
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: 91.32 E-value: 2.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 14 GGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVA--RMGIARTFQNIELFA 91
Cdd:cd03292 12 NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPylRRKIGVVFQDFRLLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 92 HMSTMENLMLGRhrymktglfrgafmwgRRSFAGKEEVanRKKVEEIIDLLDLQSVRNKFVGGLPYGTQKQVELGRALAL 171
Cdd:cd03292 92 DRNVYENVAFAL----------------EVTGVPPREI--RKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 172 EPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTlKVTILLIEHDMKMVMDISDRVLVINFG 231
Cdd:cd03292 154 SPTILIADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERG 212
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-237 |
2.71e-22 |
|
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: 90.57 E-value: 2.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARmgiartf 84
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELAR------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 85 qnielfahmstmenlmlgrhrymktglfrgafmwgRRSFagkeevanrkkVEEIIDLLDLQSVRNKFVGGLPyGTQKQ-V 163
Cdd:cd03214 74 -----------------------------------KIAY-----------VPQALELLGLAHLADRPFNELS-GGERQrV 106
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1308832087 164 ELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSPIVEG 237
Cdd:cd03214 107 LLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-236 |
2.91e-22 |
|
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: 91.80 E-value: 2.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISF----GGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQG--RRPDKVARM 78
Cdd:cd03257 3 EVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKlsRRLRKIRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 79 GIARTFQNIelfahMSTMENLM-LGRHrymktgLFRGAFMWGRRSfagKEEVANRKKVEEIIDLLDLQSVRNKFvgglPY 157
Cdd:cd03257 83 EIQMVFQDP-----MSSLNPRMtIGEQ------IAEPLRIHGKLS---KKEARKEAVLLLLVGVGLPEEVLNRY----PH 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 158 ---GTQKQ-VELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSp 233
Cdd:cd03257 145 elsGGQRQrVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGK- 223
|
...
gi 1308832087 234 IVE 236
Cdd:cd03257 224 IVE 226
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-261 |
4.55e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 92.95 E-value: 4.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 3 FFKVEKlsiSFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARMGIAR 82
Cdd:PRK13537 10 FRNVEK---RYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 83 TFQNIElfAHMSTMENLMLgrhrymktglfrgafmWGRrsFAGKEEVANRKKVEEIIDLLDLQSVRNKFVGGLPYGTQKQ 162
Cdd:PRK13537 87 QFDNLD--PDFTVRENLLV----------------FGR--YFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 163 VELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKvTILLIEHDMKMVMDISDRVLVINFGSPIVEGTPEEV 242
Cdd:PRK13537 147 LTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
250 260
....*....|....*....|..
gi 1308832087 243 ---QRNPEVLKAYLGEENAIRD 261
Cdd:PRK13537 226 iesEIGCDVIEIYGPDPVALRD 247
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-114 |
5.99e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 91.69 E-value: 5.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 18 ALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARMgIARTFQNIEL--FAHMST 95
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKY-IGRVFQDPMMgtAPSMTI 99
|
90
....*....|....*....
gi 1308832087 96 MENLMLGRHRYMKTGLFRG 114
Cdd:COG1101 100 EENLALAYRRGKRRGLRRG 118
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-259 |
8.06e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 93.37 E-value: 8.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 1 MAFFKVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARMgI 80
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRR-V 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 81 ARTFQNIELFAHMSTMENLMLGRHRYmktglfrgafmwgRRSFAGKEEvANRKKVEEIIDLLDLQSVRNKFVGGLPYGTQ 160
Cdd:PRK09536 80 ASVPQDTSLSFEFDVRQVVEMGRTPH-------------RSRFDTWTE-TDRAAVERAMERTGVAQFADRPVTSLSGGER 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 161 KQVELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIeHDMKMVMDISDRVLVINFGSPIVEGTPE 240
Cdd:PRK09536 146 QRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLADGRVRAAGPPA 224
|
250
....*....|....*....
gi 1308832087 241 EVqRNPEVLKAYLGEENAI 259
Cdd:PRK09536 225 DV-LTADTLRAAFDARTAV 242
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-237 |
1.24e-21 |
|
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: 89.56 E-value: 1.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISFGGLDALSNINFEVQEGqIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIqGRRPDKVARMgIARTF 84
Cdd:cd03264 2 QLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV-LKQPQKLRRR-IGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 85 QNIELFAHMSTMENLmlgrhRYMktglfrgAFMWGRRSfagKEEvanRKKVEEIIDLLDLQSVRNKFVGGLPYGTQKQVE 164
Cdd:cd03264 79 QEFGVYPNFTVREFL-----DYI-------AWLKGIPS---KEV---KARVDEVLELVNLGDRAKKKIGSLSGGMRRRVG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1308832087 165 LGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTlkVTILLIEHDMKMVMDISDRVLVINFGSPIVEG 237
Cdd:cd03264 141 IAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGED--RIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
12-256 |
2.94e-21 |
|
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: 92.58 E-value: 2.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 12 SFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYrPS---RGRIVFKDREIQGRRPDKVARMGIARTFQNIE 88
Cdd:TIGR02633 10 TFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHgtwDGEIYWSGSPLKASNIRDTERAGIVIIHQELT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 89 LFAHMSTMENLMLGRHRYMKTGLFRGAFMWGRrsfagkeevanrkkVEEIIDLLDLQSVRN-KFVGGLPYGTQKQVELGR 167
Cdd:TIGR02633 89 LVPELSVAENIFLGNEITLPGGRMAYNAMYLR--------------AKNLLRELQLDADNVtRPVGDYGGGQQQLVEIAK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 168 ALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTlKVTILLIEHDMKMVMDISDRVLVINFGSPIVEgTPEEVQRNPE 247
Cdd:TIGR02633 155 ALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHVAT-KDMSTMSEDD 232
|
....*....
gi 1308832087 248 VLKAYLGEE 256
Cdd:TIGR02633 233 IITMMVGRE 241
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-247 |
1.06e-20 |
|
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: 87.94 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISFG----GLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRpDKVARMGI 80
Cdd:COG1124 3 EVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRR-RKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 81 ARTFQNIELFAHmstmenlmlGRHRYmktglfrgafmwgRRSFA------GKEEVANRkkVEEIIDLLDL-QSVRNKFV- 152
Cdd:COG1124 82 QMVFQDPYASLH---------PRHTV-------------DRILAeplrihGLPDREER--IAELLEQVGLpPSFLDRYPh 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 153 ---GGlpygtQKQ-VELGRALALEPQLLLLDEPSAGMnseekqDMIF------WIKDIQDTLKVTILLIEHDMKMVMDIS 222
Cdd:COG1124 138 qlsGG-----QRQrVAIARALILEPELLLLDEPTSAL------DVSVqaeilnLLKDLREERGLTYLFVSHDLAVVAHLC 206
|
250 260
....*....|....*....|....*.
gi 1308832087 223 DRVLVINFGSpIVE-GTPEEVQRNPE 247
Cdd:COG1124 207 DRVAVMQNGR-IVEeLTVADLLAGPK 231
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
9-257 |
1.09e-20 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 90.01 E-value: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 9 LSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKvarMGIARTFQNIE 88
Cdd:PRK09452 20 ISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN---RHVNTVFQSYA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 89 LFAHMSTMENLMLGRhRYMKTglfrgafmwgrrsfaGKEEVANRkkVEEIIDLLDLQSVRNKFVGGLPYGTQKQVELGRA 168
Cdd:PRK09452 97 LFPHMTVFENVAFGL-RMQKT---------------PAAEITPR--VMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 169 LALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSPIVEGTPEEVQRNPEV 248
Cdd:PRK09452 159 VVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKN 238
|
250
....*....|.
gi 1308832087 249 L--KAYLGEEN 257
Cdd:PRK09452 239 LfvARFIGEIN 249
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
12-234 |
5.35e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 88.83 E-value: 5.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 12 SFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYrPS---RGRIVFKDREIQGRRPDKVARMGIARTFQNIE 88
Cdd:PRK13549 14 TFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIRDTERAGIAIIHQELA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 89 LFAHMSTMENLMLGrHRYMKTGLFRGAFMWGRrsfagkeevanrkkVEEIIDLLDLQSVRNKFVGGLPYGTQKQVELGRA 168
Cdd:PRK13549 93 LVKELSVLENIFLG-NEITPGGIMDYDAMYLR--------------AQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1308832087 169 LALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTlKVTILLIEHDMKMVMDISDRVLVINFGSPI 234
Cdd:PRK13549 158 LNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGRHI 222
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
5-240 |
6.58e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 86.33 E-value: 6.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISF-GGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQgRRPDKVARMGIART 83
Cdd:PRK13647 6 EVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVN-AENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 84 FQNI--ELFAhMSTMENLMLGRhryMKTGLfrgafmwgrrsfaGKEEVANRkkVEEIIDLLDLQSVRNKFVGGLPYGTQK 161
Cdd:PRK13647 85 FQDPddQVFS-STVWDDVAFGP---VNMGL-------------DKDEVERR--VEEALKAVRMWDFRDKPPYHLSYGQKK 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1308832087 162 QVELGRALALEPQLLLLDEPSAGMNSeEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSPIVEGTPE 240
Cdd:PRK13647 146 RVAIAGVLAMDPDVIVLDEPMAYLDP-RGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS 223
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-214 |
7.89e-20 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 85.68 E-value: 7.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 1 MAFFKVEKLSISFGGLD----ALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKva 76
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 77 rmgiARTFQNIELFAHMSTMENLMLGrhrymktglFRgafmwgrrsFAGKEEVANRKKVEEIIDLLDLQSVRNKFVGGLP 156
Cdd:COG4525 79 ----GVVFQKDALLPWLNVLDNVAFG---------LR---------LRGVPKAERRARAEELLALVGLADFARRRIWQLS 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1308832087 157 YGTQKQVELGRALALEPQLLLLDEPSAG---MNSEEKQDMIF--WikdiQDTLKvTILLIEHD 214
Cdd:COG4525 137 GGMRQRVGIARALAADPRFLLMDEPFGAldaLTREQMQELLLdvW----QRTGK-GVFLITHS 194
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-227 |
9.49e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 88.04 E-value: 9.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 1 MAFFKVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARMGI 80
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 81 ARTFQNIELFAHMSTMENLMLGRhrymktglFRGAFMWGRRSFAgKEEVanRKKVEEIIDLLDLQSVrnkfVGGLPYGTQ 160
Cdd:PRK11288 82 AIIYQELHLVPEMTVAENLYLGQ--------LPHKGGIVNRRLL-NYEA--REQLEHLGVDIDPDTP----LKYLSIGQR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1308832087 161 KQVELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVtILLIEHDMKMVMDISDRVLV 227
Cdd:PRK11288 147 QMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRV-ILYVSHRMEEIFALCDAITV 212
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
19-255 |
1.19e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 86.04 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 19 LSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQ---GRRPDKVARMGIARTFQnielFAHMST 95
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetGNKNLKKLRKKVSLVFQ----FPEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 96 MENLMLGRhrymktglfrgaFMWGRRSFAGKEEVANRKKVEEIIDLLDLQSVRNKFVGGLPYGTQKQVELGRALALEPQL 175
Cdd:PRK13641 99 FENTVLKD------------VEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 176 LLLDEPSAGMNSEEKQDMIFWIKDIQDTLKvTILLIEHDMKMVMDISDRVLVINFGSPIVEGTPEEVQRNPEVL-KAYLG 254
Cdd:PRK13641 167 LCLDEPAAGLDPEGRKEMMQLFKDYQKAGH-TVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEWLkKHYLD 245
|
.
gi 1308832087 255 E 255
Cdd:PRK13641 246 E 246
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
10-242 |
1.90e-19 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 87.17 E-value: 1.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 10 SISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDRE----IQGRRPDKVAR----MGIa 81
Cdd:TIGR03269 291 SVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDewvdMTKPGPDGRGRakryIGI- 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 82 rTFQNIELFAHMSTMENLM----------LGRHRYMKTglfrgafmwgrRSFAGKEEvanrKKVEEIIDlldlqsvrnKF 151
Cdd:TIGR03269 370 -LHQEYDLYPHRTVLDNLTeaiglelpdeLARMKAVIT-----------LKMVGFDE----EKAEEILD---------KY 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 152 VGGLPYGTQKQVELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFG 231
Cdd:TIGR03269 425 PDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDG 504
|
250
....*....|.
gi 1308832087 232 SPIVEGTPEEV 242
Cdd:TIGR03269 505 KIVKIGDPEEI 515
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
18-246 |
1.96e-19 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 85.53 E-value: 1.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 18 ALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVaRMGIARTFQNIELFAHMSTME 97
Cdd:COG1125 17 AVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVEL-RRRIGYVIQQIGLFPHMTVAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 98 N-----LMLGrhrymktglfrgafmWGRRsfagkeevANRKKVEEIIDL--LDLQSVRNKFvgglPY---GTQKQ-VELG 166
Cdd:COG1125 96 NiatvpRLLG---------------WDKE--------RIRARVDELLELvgLDPEEYRDRY----PHelsGGQQQrVGVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 167 RALALEPQLLLLDEP-SA--GMNSEEKQDMIfwiKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSpIVE-GTPEEV 242
Cdd:COG1125 149 RALAADPPILLMDEPfGAldPITREQLQDEL---LRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGR-IVQyDTPEEI 224
|
....
gi 1308832087 243 QRNP 246
Cdd:COG1125 225 LANP 228
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
18-237 |
2.03e-19 |
|
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: 83.96 E-value: 2.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 18 ALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIvfkdrEIQG----RRPDKV-ARMGIarTFQNIELFAH 92
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFA-----TVDGfdvvKEPAEArRRLGF--VSDSTGLYDR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 93 MSTMENLmlgrhrymktGLFRGAFMWGRRSFAGkeevanrkKVEEIIDLLDLQSVRNKFVGGLPYGTQKQVELGRALALE 172
Cdd:cd03266 93 LTARENL----------EYFAGLYGLKGDELTA--------RLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1308832087 173 PQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKvTILLIEHDMKMVMDISDRVLVINFGSPIVEG 237
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIRQLRALGK-CILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
6-247 |
3.20e-19 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 84.25 E-value: 3.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 6 VEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPD----KVA----- 76
Cdd:PRK10619 8 VIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlKVAdknql 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 77 ---RMGIARTFQNIELFAHMSTMENLMLGRHRYMktglfrgafmwgrrsfaGKEEVANRKKVEEIIDLLDL-QSVRNKFV 152
Cdd:PRK10619 88 rllRTRLTMVFQHFNLWSHMTVLENVMEAPIQVL-----------------GLSKQEARERAVKYLAKVGIdERAQGKYP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 153 GGLPYGTQKQVELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKvTILLIEHDMKMVMDISDRVLVINFGS 232
Cdd:PRK10619 151 VHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHVSSHVIFLHQGK 229
|
250
....*....|....*
gi 1308832087 233 PIVEGTPEEVQRNPE 247
Cdd:PRK10619 230 IEEEGAPEQLFGNPQ 244
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
9-242 |
1.50e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 83.73 E-value: 1.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 9 LSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARMGIARTFQNIE 88
Cdd:PRK13536 47 VSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVVPQFDNLD 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 89 LfaHMSTMENLML-GRHRYMKTglfrgafmwgrrsfagkeevanrKKVEEII-DLLDLQSVRNKF---VGGLPYGTQKQV 163
Cdd:PRK13536 127 L--EFTVRENLLVfGRYFGMST-----------------------REIEAVIpSLLEFARLESKAdarVSDLSGGMKRRL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 164 ELGRALALEPQLLLLDEPSAGMNSEEKQdmIFWiKDIQDTLK--VTILLIEHDMKMVMDISDRVLVINFGSPIVEGTPEE 241
Cdd:PRK13536 182 TLARALINDPQLLILDEPTTGLDPHARH--LIW-ERLRSLLArgKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHA 258
|
.
gi 1308832087 242 V 242
Cdd:PRK13536 259 L 259
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
9-231 |
1.52e-18 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 84.40 E-value: 1.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 9 LSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARMGIARTFQNIE 88
Cdd:PRK10982 4 ISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQELN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 89 LFAHMSTMENLMLGrhRYMKTGLFrgafmwgrrsfagKEEVANRKKVEEIIDLLDLQSVRNKFVGGLPYGTQKQVELGRA 168
Cdd:PRK10982 84 LVLQRSVMDNMWLG--RYPTKGMF-------------VDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1308832087 169 LALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTlKVTILLIEHDMKMVMDISDRVLVINFG 231
Cdd:PRK10982 149 FSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
6-246 |
1.96e-18 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 83.93 E-value: 1.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 6 VEKLSISFGGLDAlsniNFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKD---REIQGRRPDKVARMGIAR 82
Cdd:PRK10070 35 LEKTGLSLGVKDA----SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKISDAELREVRRKKIAM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 83 TFQNIELFAHMSTMENLMLGRHrymktglfrgafmwgrrsFAGKEEVANRKKVEEIIDLLDLQSVRNKFVGGLPYGTQKQ 162
Cdd:PRK10070 111 VFQSFALMPHMTVLDNTAFGME------------------LAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 163 VELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSPIVEGTPEEV 242
Cdd:PRK10070 173 VGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
....
gi 1308832087 243 QRNP 246
Cdd:PRK10070 253 LNNP 256
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-232 |
1.96e-18 |
|
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: 80.76 E-value: 1.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 6 VEKLSISFG-GLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARMgiartf 84
Cdd:cd03226 2 IENISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSIGY------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 85 qnielfahmsTMENlmLGRHRYMKT---GLFRGAfmwgrrsfagKEEVANRKKVEEIIDLLDLqsvrNKFVGGLPY---G 158
Cdd:cd03226 76 ----------VMQD--VDYQLFTDSvreELLLGL----------KELDAGNEQAETVLKDLDL----YALKERHPLslsG 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1308832087 159 TQKQ-VELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTlKVTILLIEHDMKMVMDISDRVLVINFGS 232
Cdd:cd03226 130 GQKQrLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGA 203
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-242 |
3.89e-18 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 80.93 E-value: 3.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 6 VEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARM-GIARtf 84
Cdd:COG4559 4 AENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRrAVLP-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 85 QNIEL-FAhMSTMENLMLGRHRYmktglfrgafmwgrrsfaGKEEVANRKKVEEIIDLLDLQSVRNKFVGGLPYGTQKQV 163
Cdd:COG4559 82 QHSSLaFP-FTVEEVVALGRAPH------------------GSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 164 ELGRA-------LALEPQLLLLDEPSAGMnseekqdmifwikDI---QDTL---------KVTILLIEHDMKMVMDISDR 224
Cdd:COG4559 143 QLARVlaqlwepVDGGPRWLFLDEPTSAL-------------DLahqHAVLrlarqlarrGGGVVAVLHDLNLAAQYADR 209
|
250
....*....|....*...
gi 1308832087 225 VLVINFGSPIVEGTPEEV 242
Cdd:COG4559 210 ILLLHQGRLVAQGTPEEV 227
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-242 |
4.99e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 81.21 E-value: 4.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 19 LSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQ-GRRPDKVARMGIARTFQNIELFAHMSTME 97
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDySKRGLLALRQQVATVFQDPEQQIFYTDID 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 98 NLMlgrhrymktglfrgAFMWgRRSFAGKEEVANRkkVEEIIDLLDLQSVRNKFVGGLPYGTQKQVELGRALALEPQLLL 177
Cdd:PRK13638 97 SDI--------------AFSL-RNLGVPEAEITRR--VDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1308832087 178 LDEPSAGMNSEEKQDMIFWIKDIQDTLKvTILLIEHDMKMVMDISDRVLVINFGSPIVEGTPEEV 242
Cdd:PRK13638 160 LDEPTAGLDPAGRTQMIAIIRRIVAQGN-HVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEV 223
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
6-247 |
5.29e-18 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 80.96 E-value: 5.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 6 VEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQG--RRPDKVARMGIART 83
Cdd:PRK11831 10 MRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAmsRSRLYTVRKRMSML 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 84 FQNIELFAHMSTMENLM--LGRHRYMKTGLFRGAFMwgrrsfagkeevanrKKVEEIidllDLQSVRNKFVGGLPYGTQK 161
Cdd:PRK11831 90 FQSGALFTDMNVFDNVAypLREHTQLPAPLLHSTVM---------------MKLEAV----GLRGAAKLMPSELSGGMAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 162 QVELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSPIVEGTPEE 241
Cdd:PRK11831 151 RAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQA 230
|
....*.
gi 1308832087 242 VQRNPE 247
Cdd:PRK11831 231 LQANPD 236
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-242 |
6.86e-18 |
|
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: 82.96 E-value: 6.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 4 FKVEKLSISFGGLD--ALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARMgIA 81
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQ-IG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 82 RTFQNIELFaHMSTMENLMLGRHRymktglfrgafmwgrrsfagkeevANRKKVEEIIDLLDLQSvrnkFVGGLP--Y-- 157
Cdd:COG2274 553 VVLQDVFLF-SGTIRENITLGDPD------------------------ATDEEIIEAARLAGLHD----FIEALPmgYdt 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 158 ----------GTQKQ-VELGRALALEPQLLLLDEPSAGMNSE-EKQdmifwikdIQDTLK-----VTILLIEHDMKMVMD 220
Cdd:COG2274 604 vvgeggsnlsGGQRQrLAIARALLRNPRILILDEATSALDAEtEAI--------ILENLRrllkgRTVIIIAHRLSTIRL 675
|
250 260
....*....|....*....|..
gi 1308832087 221 iSDRVLVINFGSPIVEGTPEEV 242
Cdd:COG2274 676 -ADRIIVLDKGRIVEDGTHEEL 696
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
12-236 |
8.54e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 82.36 E-value: 8.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 12 SFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARMGIARTFQNIELFA 91
Cdd:PRK10762 13 AFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGIGIIHQELNLIP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 92 HMSTMENLMLGRHrymKTGLFrGAFMWgrrsfagkeevanRKKVEEIIDLLDLQSVR---NKFVGGLPYGTQKQVELGRA 168
Cdd:PRK10762 93 QLTIAENIFLGRE---FVNRF-GRIDW-------------KKMYAEADKLLARLNLRfssDKLVGELSIGEQQMVEIAKV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1308832087 169 LALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTlKVTILLIEHDMKMVMDISDRVLVINFGSPIVE 236
Cdd:PRK10762 156 LSFESKVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRLKEIFEICDDVTVFRDGQFIAE 222
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
6-247 |
1.63e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 79.39 E-value: 1.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 6 VEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVarmgiartfq 85
Cdd:PRK09544 7 LENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKL---------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 86 nielfaHMSTMENLMLGRHRYMKTGLFRGAFMwgrrsfagkeEVANRKKVEEIIDLlDLQsvrnKFVGGlpyGTQKqVEL 165
Cdd:PRK09544 77 ------YLDTTLPLTVNRFLRLRPGTKKEDIL----------PALKRVQAGHLIDA-PMQ----KLSGG---ETQR-VLL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 166 GRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINfGSPIVEGTPEEVQRN 245
Cdd:PRK09544 132 ARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLN-HHICCSGTPEVVSLH 210
|
..
gi 1308832087 246 PE 247
Cdd:PRK09544 211 PE 212
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
5-242 |
1.92e-17 |
|
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: 78.81 E-value: 1.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISF-GGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGrRPDKVARMGIART 83
Cdd:cd03254 4 EFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRD-ISRKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 84 FQNIELFAHmSTMENLMLGRHRymktglfrgafmwgrrsfAGKEEVANRKKV----EEIIDLLD-LQSVRNKFVGGLPYG 158
Cdd:cd03254 83 LQDTFLFSG-TIMENIRLGRPN------------------ATDEEVIEAAKEagahDFIMKLPNgYDTVLGENGGNLSQG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 159 tQKQ-VELGRALALEPQLLLLDEPSAGMNSEEKqdmifwiKDIQDTLKV-----TILLIEHDMKMVMDiSDRVLVINFGS 232
Cdd:cd03254 144 -ERQlLAIARAMLRDPKILILDEATSNIDTETE-------KLIQEALEKlmkgrTSIIIAHRLSTIKN-ADKILVLDDGK 214
|
250
....*....|
gi 1308832087 233 PIVEGTPEEV 242
Cdd:cd03254 215 IIEEGTHDEL 224
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
17-237 |
2.01e-17 |
|
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: 78.40 E-value: 2.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 17 DALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDkVARMGIARTFQNIELFAHmSTM 96
Cdd:cd03245 18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPA-DLRRNIGYVPQDVTLFYG-TLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 97 ENLMLGRHRYMKTGLFRGAfmwgrrSFAGKEEVANRKKveeiiDLLDLQsvrnkfVG----GLPyGTQKQ-VELGRALAL 171
Cdd:cd03245 96 DNITLGAPLADDERILRAA------ELAGVTDFVNKHP-----NGLDLQ------IGergrGLS-GGQRQaVALARALLN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 172 EPQLLLLDEPSAGM--NSEE--KQDMIFWIKDIqdtlkvTILLIEHDMKMvMDISDRVLVINFGSPIVEG 237
Cdd:cd03245 158 DPPILLLDEPTSAMdmNSEErlKERLRQLLGDK------TLIIITHRPSL-LDLVDRIIVMDSGRIVADG 220
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
6-245 |
2.54e-17 |
|
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: 80.96 E-value: 2.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 6 VEKLSISF-GGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPD----KVARMGi 80
Cdd:COG4988 339 LEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAswrrQIAWVP- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 81 artfQNIELFaHMSTMENLMLGRHRymktglfrgafmwgrrsfagkeevANRKKVEEIIDLLDLqsvrNKFVGGLPYG-- 158
Cdd:COG4988 418 ----QNPYLF-AGTIRENLRLGRPD------------------------ASDEELEAALEAAGL----DEFVAALPDGld 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 159 T------------QKQ-VELGRALALEPQLLLLDEPSAG--MNSEEkqdmifwikDIQDTLK-----VTILLIEHDMKMV 218
Cdd:COG4988 465 TplgeggrglsggQAQrLALARALLRDAPLLLLDEPTAHldAETEA---------EILQALRrlakgRTVILITHRLALL 535
|
250 260
....*....|....*....|....*..
gi 1308832087 219 MDiSDRVLVINFGSPIVEGTPEEVQRN 245
Cdd:COG4988 536 AQ-ADRILVLDDGRIVEQGTHEELLAK 561
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
18-253 |
2.95e-17 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 78.58 E-value: 2.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 18 ALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIvfkdrEIQGRrpdkVARMgiartfqnIEL---F-AHM 93
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV-----EVNGR----VSAL--------LELgagFhPEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 94 STMENLMlgrhrymktglFRGAFMwGRRsfagKEEVanRKKVEEIIDlldlqsvrnkFvgglpygtqkqVELGRAlalep 173
Cdd:COG1134 104 TGRENIY-----------LNGRLL-GLS----RKEI--DEKFDEIVE----------F-----------AELGDF----- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 174 qlllLDEP----SAGMN--------------------------------SEEKqdmifwIKDIQDTLKvTILLIEHDMKM 217
Cdd:COG1134 140 ----IDQPvktySSGMRarlafavatavdpdillvdevlavgdaafqkkCLAR------IRELRESGR-TVIFVSHSMGA 208
|
250 260 270
....*....|....*....|....*....|....*.
gi 1308832087 218 VMDISDRVLVINFGSPIVEGTPEevqrnpEVLKAYL 253
Cdd:COG1134 209 VRRLCDRAIWLEKGRLVMDGDPE------EVIAAYE 238
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-245 |
3.63e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 79.36 E-value: 3.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 18 ALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARMGIA---RTfqniELFAHMS 94
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARRIGVVfgqRS----QLWWDLP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 95 TMENLMLGRHRYmktGLFRGAFmwgrrsfagkeevanRKKVEEIIDLLDLQSVRNKFVGGLPYGTQKQVELGRALALEPQ 174
Cdd:COG4586 113 AIDSFRLLKAIY---RIPDAEY---------------KKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPK 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1308832087 175 LLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSPIVEGTPEEVQRN 245
Cdd:COG4586 175 ILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKER 245
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-251 |
3.71e-17 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 78.20 E-value: 3.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVAR-MGIARt 83
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKrLAILR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 84 fQNIELFAHMSTMENLMLGRHRYMKtglfrgafmwGRRSfagkeeVANRKKVEEIIDLLDLQSVRNKFVGGLPyGTQKQ- 162
Cdd:COG4604 82 -QENHINSRLTVRELVAFGRFPYSK----------GRLT------AEDREIIDEAIAYLDLEDLADRYLDELS-GGQRQr 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 163 -------------VELgralalepqllllDEP--------SAGMnseEKQdmifwIKDIQDTLKVTILLIEHDMKMVMDI 221
Cdd:COG4604 144 afiamvlaqdtdyVLL-------------DEPlnnldmkhSVQM---MKL-----LRRLADELGKTVVIVLHDINFASCY 202
|
250 260 270
....*....|....*....|....*....|
gi 1308832087 222 SDRVLVINFGSPIVEGTPEEVQRnPEVLKA 251
Cdd:COG4604 203 ADHIVAMKDGRVVAQGTPEEIIT-PEVLSD 231
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
5-86 |
4.63e-17 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 77.18 E-value: 4.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGI--YRPSRGRIVFKDREIQGRRPDKVARMGIAR 82
Cdd:cd03217 2 EIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERARLGIFL 81
|
....
gi 1308832087 83 TFQN 86
Cdd:cd03217 82 AFQY 85
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
18-249 |
9.66e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 78.35 E-value: 9.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 18 ALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKvaRMGIARTFQNIELFAHMSTME 97
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNH--ELITNPYSKKIKNFKELRRRV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 98 NLMLGRHRYMktgLFRGA----FMWGRRSFAGKEEVAnRKKVEEIIDLLDLQSV---RNKFvgGLPYGTQKQVELGRALA 170
Cdd:PRK13631 119 SMVFQFPEYQ---LFKDTiekdIMFGPVALGVKKSEA-KKLAKFYLNKMGLDDSyleRSPF--GLSGGQKRRVAIAGILA 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1308832087 171 LEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKvTILLIEHDMKMVMDISDRVLVINFGSPIVEGTPEEVQRNPEVL 249
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNK-TVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQHII 270
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
5-241 |
1.20e-16 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 77.36 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIY---RPSRGRIVFKDREIQ--GR--RPDKVAR 77
Cdd:PRK09984 6 RVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQreGRlaRDIRKSR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 78 MGIARTFQNIELFAHMSTMENLMLGrhRYMKTGLFRGAFMWGRRsfagkeevANRKKVEEIIDLLDLQSVRNKFVGGLPY 157
Cdd:PRK09984 86 ANTGYIFQQFNLVNRLSVLENVLIG--ALGSTPFWRTCFSWFTR--------EQKQRALQALTRVGMVHFAHQRVSTLSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 158 GTQKQVELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSPIVEG 237
Cdd:PRK09984 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDG 235
|
....
gi 1308832087 238 TPEE 241
Cdd:PRK09984 236 SSQQ 239
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
18-252 |
1.41e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 77.51 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 18 ALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVAR-----MGIARTFQNIELFAh 92
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRpvrkrIGMVFQFPESQLFE- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 93 mSTMENLMLgrhrymktglfrgafmWGRRSFAGKEEVANRKKVEEIIDLLDLQSVRNKFVGGLPYGTQKQVELGRALALE 172
Cdd:PRK13646 101 -DTVEREII----------------FGPKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 173 PQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSPIVEGTPEEVQRNPEVLKAY 252
Cdd:PRK13646 164 PDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKKKLADW 243
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
5-237 |
1.47e-16 |
|
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: 75.99 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISFGGLdalsNINFEVQ--EGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPdkvARMGIAR 82
Cdd:cd03298 2 RLDKIRFSYGEQ----PMHFDLTfaQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPP---ADRPVSM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 83 TFQNIELFAHMSTMENLMLGRHRYMKTglfrgafmwgrrsfagKEEvaNRKKVEEIIDLLDLQSVRNKFVGGLPYGTQKQ 162
Cdd:cd03298 75 LFQENNLFAHLTVEQNVGLGLSPGLKL----------------TAE--DRQAIEVALARVGLAGLEKRLPGELSGGERQR 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1308832087 163 VELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSPIVEG 237
Cdd:cd03298 137 VALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-242 |
2.01e-16 |
|
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: 76.28 E-value: 2.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 1 MAFFKVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGrivfKDREIQGRRPDKV----- 75
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYG----NDVRLFGERRGGEdvwel 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 76 -ARMGIARTFQNIELFAHMSTMENLMLGRhrYMKTGLFRgafmwgrrsfagKEEVANRKKVEEIIDLLDLQSVRNKFVGG 154
Cdd:COG1119 77 rKRIGLVSPALQLRFPRDETVLDVVLSGF--FDSIGLYR------------EPTDEQRERARELLELLGLAHLADRPFGT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 155 LPYGTQKQVELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSPI 234
Cdd:COG1119 143 LSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVV 222
|
....*...
gi 1308832087 235 VEGTPEEV 242
Cdd:COG1119 223 AAGPKEEV 230
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
14-247 |
3.45e-16 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 76.81 E-value: 3.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 14 GGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPdkvARMGIARTFQNIELFAHM 93
Cdd:PRK11650 15 GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEP---ADRDIAMVFQNYALYPHM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 94 STMENLMLG-RHRYMktglfrgafmwgrrsfaGKEEVanRKKVEEIIDLLDLQsvrnkfvgglPY---------GTQKQ- 162
Cdd:PRK11650 92 SVRENMAYGlKIRGM-----------------PKAEI--EERVAEAARILELE----------PLldrkprelsGGQRQr 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 163 VELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGspIVE--GTPE 240
Cdd:PRK11650 143 VAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGG--VAEqiGTPV 220
|
....*..
gi 1308832087 241 EVQRNPE 247
Cdd:PRK11650 221 EVYEKPA 227
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-243 |
4.15e-16 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 75.00 E-value: 4.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 23 NFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKD----REIQGRRPdkvarmgIARTFQNIELFAHMSTMEN 98
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGqdhtTTPPSRRP-------VSMLFQENNLFSHLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 99 LMLGRHrymkTGLfrgafmwgrrsfagKEEVANRKKVEEIIDLLDLQSVRNKFVGGLPYGTQKQVELGRALALEPQLLLL 178
Cdd:PRK10771 92 IGLGLN----PGL--------------KLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1308832087 179 DEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSPIVEGTPEEVQ 243
Cdd:PRK10771 154 DEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELL 218
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
5-254 |
6.21e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 75.41 E-value: 6.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISF-GGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDreIQGRRPDKVA--RMGIA 81
Cdd:PRK13644 3 RLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG--IDTGDFSKLQgiRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 82 RTFQNIEL-FAHMSTMENLMLGRHRYMKTGLfrgafmwgrrsfagkeEVanRKKVEEIIDLLDLQSVRNKFVGGLPYGTQ 160
Cdd:PRK13644 81 IVFQNPETqFVGRTVEEDLAFGPENLCLPPI----------------EI--RKRVDRALAEIGLEKYRHRSPKTLSGGQG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 161 KQVELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKvTILLIEHDMKMVMDiSDRVLVINFGSPIVEGTPE 240
Cdd:PRK13644 143 QCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGK-TIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPE 220
|
250
....*....|....
gi 1308832087 241 EVQRNPEVlkAYLG 254
Cdd:PRK13644 221 NVLSDVSL--QTLG 232
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
5-253 |
9.06e-16 |
|
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: 76.34 E-value: 9.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISF--GGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARMgIAR 82
Cdd:COG4987 335 ELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRR-IAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 83 TFQNIELFaHMSTMENLMLGRHRymktglfrgafmwgrrsfAGKEEVanrkkvEEIIDLLDLQsvrnKFVGGLPYG--T- 159
Cdd:COG4987 414 VPQRPHLF-DTTLRENLRLARPD------------------ATDEEL------WAALERVGLG----DWLAALPDGldTw 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 160 -----------QKQ-VELGRALALEPQLLLLDEPSAGMNSEEKQDMifwIKDIQDTLKV-TILLIEHDMKmVMDISDRVL 226
Cdd:COG4987 465 lgeggrrlsggERRrLALARALLRDAPILLLDEPTEGLDAATEQAL---LADLLEALAGrTVLLITHRLA-GLERMDRIL 540
|
250 260
....*....|....*....|....*..
gi 1308832087 227 VINFGSPIVEGTPEEVQRNPEVLKAYL 253
Cdd:COG4987 541 VLEDGRIVEQGTHEELLAQNGRYRQLY 567
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-251 |
1.21e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 75.86 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIvfkdrEIQGRR-----PDKVARMG 79
Cdd:PRK15439 13 CARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTL-----EIGGNPcarltPAKAHQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 80 IARTFQNIELFAHMSTMENLMLGRHRYMKTglfrgafmwgrrsfagkeevanRKKVEEIIDLLDLQSVRNKFVGGLPYGT 159
Cdd:PRK15439 88 IYLVPQEPLLFPNLSVKENILFGLPKRQAS----------------------MQKMKQLLAALGCQLDLDSSAGSLEVAD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 160 QKQVELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDtLKVTILLIEHDMKMVMDISDRVLVINFGSPIVEGTP 239
Cdd:PRK15439 146 RQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLA-QGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKT 224
|
250
....*....|..
gi 1308832087 240 EEVQRNpEVLKA 251
Cdd:PRK15439 225 ADLSTD-DIIQA 235
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
6-215 |
1.56e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 73.97 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 6 VEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGrrPDkvARMGIarTFQ 85
Cdd:PRK11248 4 ISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG--PG--AERGV--VFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 86 NIELFAHMSTMENLMLGRHrymktglfrgafmwgrrsFAGKEEVANRKKVEEIIDLLDLQSVRNKFVGGLPYGTQKQVEL 165
Cdd:PRK11248 78 NEGLLPWRNVQDNVAFGLQ------------------LAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGI 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1308832087 166 GRALALEPQLLLLDEPSAGMNS---EEKQDMIF--WikdiQDTLKvTILLIEHDM 215
Cdd:PRK11248 140 ARALAANPQLLLLDEPFGALDAftrEQMQTLLLklW----QETGK-QVLLITHDI 189
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-247 |
1.74e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 75.07 E-value: 1.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 1 MAFFKVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGrivfkDREIQGRRPDKV--ARM 78
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSG-----DLFIGEKRMNDVppAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 79 GIARTFQNIELFAHMSTMENlmlgrhryMKTGLfrgafmwgRRSFAGKEEVANR-KKVEEIIDLLDLQSVRNKFVGGlpy 157
Cdd:PRK11000 76 GVGMVFQSYALYPHLSVAEN--------MSFGL--------KLAGAKKEEINQRvNQVAEVLQLAHLLDRKPKALSG--- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 158 GTQKQVELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSPIVEG 237
Cdd:PRK11000 137 GQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
|
250
....*....|
gi 1308832087 238 TPEEVQRNPE 247
Cdd:PRK11000 217 KPLELYHYPA 226
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
4-249 |
1.87e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 73.87 E-value: 1.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 4 FKVEKLSISFGGLD--ALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQgRRPDKVARMGIA 81
Cdd:PRK13632 8 IKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIS-KENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 82 RTFQNIElfahmstmenlmlgrhrymktGLFRGAFMWGRRSFAGKEEVANRKKVEEIIDLLDLQSVRNKFVGGLPY---G 158
Cdd:PRK13632 87 IIFQNPD---------------------NQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQnlsG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 159 TQKQ-VELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMdISDRVLVINFGSPIVEG 237
Cdd:PRK13632 146 GQKQrVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQG 224
|
250
....*....|..
gi 1308832087 238 TPEEVQRNPEVL 249
Cdd:PRK13632 225 KPKEILNNKEIL 236
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
18-249 |
3.07e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 73.50 E-value: 3.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 18 ALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQG--RRPDKVARM----GIARTFQNIELFa 91
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlKKIKEVKRLrkeiGLVFQFPEYQLF- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 92 hMSTMEnlmlgrhrymKTGLFrGAFMWGrrsfAGKEEVanRKKVEEiidLLDLQSVRNKFVGGLPY----GTQKQVELGR 167
Cdd:PRK13645 105 -QETIE----------KDIAF-GPVNLG----ENKQEA--YKKVPE---LLKLVQLPEDYVKRSPFelsgGQKRRVALAG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 168 ALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSPIVEGTPEEVQRNPE 247
Cdd:PRK13645 164 IIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQE 243
|
..
gi 1308832087 248 VL 249
Cdd:PRK13645 244 LL 245
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
4-254 |
3.12e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 73.28 E-value: 3.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 4 FKVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARMgIART 83
Cdd:PRK10575 12 FALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARK-VAYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 84 FQNIELFAHMSTMENLMLGRHRYmktglfRGAFmwgrrsfaGKEEVANRKKVEEIIDLLDLQSVRNKFVGGLPYGTQKQV 163
Cdd:PRK10575 91 PQQLPAAEGMTVRELVAIGRYPW------HGAL--------GRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 164 ELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSPIVEGTPEEVQ 243
Cdd:PRK10575 157 WIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELM 236
|
250
....*....|.
gi 1308832087 244 RnPEVLKAYLG 254
Cdd:PRK10575 237 R-GETLEQIYG 246
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
18-252 |
3.26e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 73.61 E-value: 3.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 18 ALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRI---------VFKDREIQGRRpdkvARMGIARTFQNIE 88
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdivvssTSKQKEIKPVR----KKVGVVFQFPESQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 89 LFAhmstmenlmlgrhrymKTGLFRGAFmwGRRSFAGKEEVANRKKVEEiidlLDLQSVRNKFVGGLPY----GTQKQVE 164
Cdd:PRK13643 97 LFE----------------ETVLKDVAF--GPQNFGIPKEKAEKIAAEK----LEMVGLADEFWEKSPFelsgGQMRRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 165 LGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKvTILLIEHDMKMVMDISDRVLVINFGSPIVEGTPEEVQR 244
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQ-TVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
|
....*...
gi 1308832087 245 NPEVLKAY 252
Cdd:PRK13643 234 EVDFLKAH 241
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
16-250 |
4.62e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 73.20 E-value: 4.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 16 LDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRI--VFKDRE----------------IQGRRPDKVA- 76
Cdd:PRK13651 20 LKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewIFKDEKnkkktkekekvleklvIQKTRFKKIKk 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 77 ------RMGIARTFQNIELFAhmSTMENlmlgrhrymktglfrgAFMWGRRSFAGKEEVAnRKKVEEIIDLLDL-QSVRN 149
Cdd:PRK13651 100 ikeirrRVGVVFQFAEYQLFE--QTIEK----------------DIIFGPVSMGVSKEEA-KKRAAKYIELVGLdESYLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 150 KFVGGLPYGTQKQVELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKvTILLIEHDMKMVMDISDRVLVIN 229
Cdd:PRK13651 161 RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNVLEWTKRTIFFK 239
|
250 260
....*....|....*....|.
gi 1308832087 230 FGSPIVEGTPEEVQRNPEVLK 250
Cdd:PRK13651 240 DGKIIKDGDTYDILSDNKFLI 260
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
18-242 |
8.86e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 72.09 E-value: 8.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 18 ALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVaRMGIARTFQNielfahmstME 97
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKL-RKHIGIVFQN---------PD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 98 NLMLGrhrymKTGLFRGAFMWGRRSFAGKEEVANRKKVEEIIDLLD-LQSVRNKFVGGlpygtQKQ-VELGRALALEPQL 175
Cdd:PRK13648 94 NQFVG-----SIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLErADYEPNALSGG-----QKQrVAIAGVLALNPSV 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1308832087 176 LLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDiSDRVLVINFGSPIVEGTPEEV 242
Cdd:PRK13648 164 IILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEI 229
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
6-228 |
9.56e-15 |
|
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: 73.47 E-value: 9.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 6 VEKLSISFGGLD-ALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDkVARMGIARTF 84
Cdd:TIGR02857 324 FSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADAD-SWRDQIAWVP 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 85 QNIELFAHmSTMENLMLGRhrymktglfRGAfmwgrrSFAGKEEVANRKKVEEIIDllDLQSVRNKFVG----GLPYGTQ 160
Cdd:TIGR02857 403 QHPFLFAG-TIAENIRLAR---------PDA------SDAEIREALERAGLDEFVA--ALPQGLDTPIGeggaGLSGGQA 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1308832087 161 KQVELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTlkVTILLIEHDMKmVMDISDRVLVI 228
Cdd:TIGR02857 465 QRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQG--RTVLLVTHRLA-LAALADRIVVL 529
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
5-231 |
1.04e-14 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 71.06 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISF-GGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVA--RMGIA 81
Cdd:PRK10908 3 RFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPflRRQIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 82 RTFQNIELFAHMSTMENLMLgrhrymktglfrgafmwgRRSFAGKEEVANRKKVEEIIDLLDLQSVRNKFVGGLPYGTQK 161
Cdd:PRK10908 83 MIFQDHHLLMDRTVYDNVAI------------------PLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 162 QVELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIqDTLKVTILLIEHDMKMVMDISDRVLVINFG 231
Cdd:PRK10908 145 RVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEF-NRVGVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
12-234 |
1.05e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 73.29 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 12 SFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYrPS---RGRIVFKDREIQGRRPDKVARMGIARTFQNIE 88
Cdd:NF040905 10 TFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEVCRFKDIRDSEALGIVIIHQELA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 89 LFAHMSTMENLMLGRHRYMktglfRGAFMWgRRSFAGKEEVANRKKVEEIIDLLdlqsvrnkfVGGLPYGTQKQVELGRA 168
Cdd:NF040905 89 LIPYLSIAENIFLGNERAK-----RGVIDW-NETNRRARELLAKVGLDESPDTL---------VTDIGVGKQQLVEIAKA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1308832087 169 LALEPQLLLLDEPSAGMNSEEKQDMIFWIKDiqdtLK---VTILLIEHDMKMVMDISDRVLVINFGSPI 234
Cdd:NF040905 154 LSKDVKLLILDEPTAALNEEDSAALLDLLLE----LKaqgITSIIISHKLNEIRRVADSITVLRDGRTI 218
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
18-99 |
1.16e-14 |
|
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: 69.72 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 18 ALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARMgIARTFQNIELFaHMSTME 97
Cdd:cd03228 17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN-IAYVPQDPFLF-SGTIRE 94
|
..
gi 1308832087 98 NL 99
Cdd:cd03228 95 NI 96
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
18-251 |
2.02e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 71.27 E-value: 2.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 18 ALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARMGIARTFQNI--ELFAHMsT 95
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDIRNKAGMVFQNPdnQIVATI-V 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 96 MENLMLGRHRYmktglfrgafmwgrrsfaGKEEVANRKKVEEIIDLLDLQSVRnKFVGGLPYGTQKQ-VELGRALALEPQ 174
Cdd:PRK13633 104 EEDVAFGPENL------------------GIPPEEIRERVDESLKKVGMYEYR-RHAPHLLSGGQKQrVAIAGILAMRPE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1308832087 175 LLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDiSDRVLVINFGSPIVEGTPEEVQRNPEVLKA 251
Cdd:PRK13633 165 CIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKEVEMMKK 240
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-140 |
2.14e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 72.37 E-value: 2.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 4 FKVEKLSI-SFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARMGIAR 82
Cdd:COG3845 258 LEVENLSVrDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVAY 337
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1308832087 83 tfqnI-E------LFAHMSTMENLMLGRHRymKTGLFRGAFMwgRRSFAgkeevanRKKVEEIID 140
Cdd:COG3845 338 ----IpEdrlgrgLVPDMSVAENLILGRYR--RPPFSRGGFL--DRKAI-------RAFAEELIE 387
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
22-256 |
2.33e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 71.83 E-value: 2.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 22 INFEVQEGQ-------------IFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREI----QG-------RRpdkvar 77
Cdd:PRK11144 4 LNFKQQLGDlcltvnltlpaqgITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLfdaeKGiclppekRR------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 78 mgIARTFQNIELFAHMSTMENLMLGRHRYMKtGLFrgafmwgrrsfagkeevanrkkvEEIIDLLDLQSVRNKFVGGLPY 157
Cdd:PRK11144 78 --IGYVFQDARLFPHYKVRGNLRYGMAKSMV-AQF-----------------------DKIVALLGIEPLLDRYPGSLSG 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 158 GTQKQVELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSPIVEG 237
Cdd:PRK11144 132 GEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFG 211
|
250
....*....|....*....
gi 1308832087 238 TPEEVQRNPeVLKAYLGEE 256
Cdd:PRK11144 212 PLEEVWASS-AMRPWLPKE 229
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
17-251 |
5.87e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 70.05 E-value: 5.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 17 DALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQ-GRRPDKVARM----GIARTFQNIELFA 91
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITaGKKNKKLKPLrkkvGIVFQFPEHQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 92 hmSTMENLMlgrhrymktglfrgAFmwGRRSFAGKEEVAnRKKVEEIIDLLDL-QSVRNKFVGGLPYGTQKQVELGRALA 170
Cdd:PRK13634 101 --ETVEKDI--------------CF--GPMNFGVSEEDA-KQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 171 LEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSPIVEGTPEEVQRNPEVLK 250
Cdd:PRK13634 162 MEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDELE 241
|
.
gi 1308832087 251 A 251
Cdd:PRK13634 242 A 242
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-242 |
6.85e-14 |
|
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: 70.99 E-value: 6.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGI--YRPSRGRIVFKDR--------EIQGRRPDK 74
Cdd:TIGR03269 2 EVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHVAlcekcgyvERPSKVGEP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 75 VARMGIARTFQNIELFAHMSTMenlmlgRHRYMKtglfRGAFMWgRRSFA---------------------GKEEVanrK 133
Cdd:TIGR03269 82 CPVCGGTLEPEEVDFWNLSDKL------RRRIRK----RIAIML-QRTFAlygddtvldnvlealeeigyeGKEAV---G 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 134 KVEEIIDLLDLQSVRNKFVGGLPYGTQKQVELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEH 213
Cdd:TIGR03269 148 RAVDLIEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSH 227
|
250 260
....*....|....*....|....*....
gi 1308832087 214 DMKMVMDISDRVLVINFGSPIVEGTPEEV 242
Cdd:TIGR03269 228 WPEVIEDLSDKAIWLENGEIKEEGTPDEV 256
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-231 |
9.05e-14 |
|
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: 67.46 E-value: 9.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 4 FKVEKLSISfgglDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARMGIA-- 81
Cdd:cd03215 5 LEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAyv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 82 ---RtfQNIELFAHMSTMENLMLGRHrymktglfrgafmwgrrsfagkeevanrkkveeiidlldlqsvrnkfvggLPYG 158
Cdd:cd03215 81 pedR--KREGLVLDLSVAENIALSSL--------------------------------------------------LSGG 108
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1308832087 159 TQKQVELGRALALEPQLLLLDEPSAGMNSEEKQdmifwikDIQDTLK------VTILLIEHDMKMVMDISDRVLVINFG 231
Cdd:cd03215 109 NQQKVVLARWLARDPRVLILDEPTRGVDVGAKA-------EIYRLIReladagKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
5-236 |
1.10e-13 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 68.50 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQ-GRRPDKVA----RMG 79
Cdd:PRK11124 4 QLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDfSKTPSDKAirelRRN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 80 IARTFQNIELFAHMSTMENLMLGRHRYMktGLfrgafmwgrrsfaGKEEVanRKKVEEIIDLLDLQSVRNKFVGGLPYGT 159
Cdd:PRK11124 84 VGMVFQQYNLWPHLTVQQNLIEAPCRVL--GL-------------SKDQA--LARAEKLLERLRLKPYADRFPLHLSGGQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1308832087 160 QKQVELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTlKVTILLIEHDMKMVMDISDRVLVINFGSpIVE 236
Cdd:PRK11124 147 QQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAET-GITQVIVTHEVEVARKTASRVVYMENGH-IVE 221
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-237 |
1.74e-13 |
|
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: 67.68 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 16 LDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPS---RGRIVFKDREiqgRRPDKVARMgIARTFQNIELFAH 92
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQP---RKPDQFQKC-VAYVRQDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 93 MSTMENLmlgrhRYMktglfrgAFMWGRRSFAGKEevanRKKVEEIIDLLDL--QSVRNKFVGGLPYGTQKQVELGRALA 170
Cdd:cd03234 96 LTVRETL-----TYT-------AILRLPRKSSDAI----RKKRVEDVLLRDLalTRIGGNLVKGISGGERRRVSIAVQLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1308832087 171 LEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSPIVEG 237
Cdd:cd03234 160 WDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
6-78 |
2.33e-13 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 67.87 E-value: 2.33e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1308832087 6 VEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARM 78
Cdd:PRK13548 5 ARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARR 77
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
5-250 |
2.45e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 67.73 E-value: 2.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARMgIARTF 84
Cdd:PRK11231 4 RTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARR-LALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 85 QNIELFAHMSTMENLMLGRHRYMKtglfrgafMWGRRSfagkeeVANRKKVEEIIDLLDLQSVRNKFVGGLPYGTQKQVE 164
Cdd:PRK11231 83 QHHLTPEGITVRELVAYGRSPWLS--------LWGRLS------AEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 165 LGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKvTILLIEHDMKMVMDISDRVLVINFGSPIVEGTPEEVQr 244
Cdd:PRK11231 149 LAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGK-TVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVM- 226
|
....*.
gi 1308832087 245 NPEVLK 250
Cdd:PRK11231 227 TPGLLR 232
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
19-242 |
2.52e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 68.22 E-value: 2.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 19 LSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQgrrPDKV--ARMGIARTFQNIELFAHMSTM 96
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLT---EENVwdIRHKIGMVFQNPDNQFVGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 97 ENLMlgrhrymktglfrgAFMWGRRSFAGKEEvanRKKVEEIIDLLDLQSVRNKFVGGLPYGTQKQVELGRALALEPQLL 176
Cdd:PRK13650 100 EDDV--------------AFGLENKGIPHEEM---KERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKII 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1308832087 177 LLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMdISDRVLVINFGSPIVEGTPEEV 242
Cdd:PRK13650 163 ILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPREL 227
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
7-242 |
2.55e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 68.09 E-value: 2.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 7 EKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARMgIARTFQN 86
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARR-IGLLAQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 87 IELFAHMSTMEnlMLGRHRYMKTGLFRgafMWGRRSfagkEEVANRKKVEEIIDLLDLQSVRNkfvggLPYGTQKQVELG 166
Cdd:PRK10253 90 ATTPGDITVQE--LVARGRYPHQPLFT---RWRKED----EEAVTKAMQATGITHLADQSVDT-----LSGGQRQRAWIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1308832087 167 RALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSPIVEGTPEEV 242
Cdd:PRK10253 156 MVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
5-247 |
3.89e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 67.11 E-value: 3.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCIN--GIYRPS---RGRIVFKDREIQGRRPDKVA-RM 78
Cdd:PRK14239 7 QVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPEvtiTGSIVYNGHNIYSPRTDTVDlRK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 79 GIARTFQNIELFAhMSTMENLMLG--------RHRY---MKTGLfRGAFMWgrrsfagkeevanrkkvEEIIDLLDLQSV 147
Cdd:PRK14239 87 EIGMVFQQPNPFP-MSIYENVVYGlrlkgikdKQVLdeaVEKSL-KGASIW-----------------DEVKDRLHDSAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 148 rnkfvgGLPYGTQKQVELGRALALEPQLLLLDEPSAGMN---SEEKQDMIFWIKDiqdtlKVTILLIEHDMKMVMDISDR 224
Cdd:PRK14239 148 ------GLSGGQQQRVCIARVLATSPKIILLDEPTSALDpisAGKIEETLLGLKD-----DYTMLLVTRSMQQASRISDR 216
|
250 260
....*....|....*....|...
gi 1308832087 225 VLVINFGSPIVEGTPEEVQRNPE 247
Cdd:PRK14239 217 TGFFLDGDLIEYNDTKQMFMNPK 239
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-108 |
5.74e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 68.17 E-value: 5.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 6 VEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVfkdreiqgRRPDkvARMGIARtfQ 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVS--------IPKG--LRIGYLP--Q 68
|
90 100
....*....|....*....|...
gi 1308832087 86 NIELFAHMSTMENLMLGRHRYMK 108
Cdd:COG0488 69 EPPLDDDLTVLDTVLDGDAELRA 91
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-62 |
8.64e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 67.40 E-value: 8.64e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1308832087 4 FKVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVF 62
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL 374
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
6-105 |
1.02e-12 |
|
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: 64.54 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 6 VEKLSISFGGLDA--LSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARMgIART 83
Cdd:cd03246 3 VENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDH-VGYL 81
|
90 100
....*....|....*....|..
gi 1308832087 84 FQNIELFAHmSTMENLMLGRHR 105
Cdd:cd03246 82 PQDDELFSG-SIAENILSGGQR 102
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-60 |
1.07e-12 |
|
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: 63.62 E-value: 1.07e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1308832087 5 KVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRI 60
Cdd:cd03221 2 ELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV 57
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
5-66 |
1.71e-12 |
|
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: 65.15 E-value: 1.71e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1308832087 5 KVEKLSISF-----GG--LDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDRE 66
Cdd:COG4778 6 EVENLSKTFtlhlqGGkrLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDG 74
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
18-60 |
1.71e-12 |
|
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: 64.86 E-value: 1.71e-12
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1308832087 18 ALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRI 60
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV 79
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
6-240 |
2.14e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 65.29 E-value: 2.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 6 VEKLSISF-GGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIvfkdrEIQGRRPDKVARMG-IART 83
Cdd:PRK15056 9 VNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKI-----SILGQPTRQALQKNlVAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 84 FQNIELFAHMSTM--ENLMLGRHRYMKtglfrgafmWGRRSFAgkeevANRKKVEEIIDLLDLQSVRNKFVGGLPYGTQK 161
Cdd:PRK15056 84 PQSEEVDWSFPVLveDVVMMGRYGHMG---------WLRRAKK-----RDRQIVTAALARVDMVEFRHRQIGELSGGQKK 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1308832087 162 QVELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKvTILLIEHDMKMVMDISDRVLVINfGSPIVEGTPE 240
Cdd:PRK15056 150 RVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGK-TMLVSTHNLGSVTEFCDYTVMVK-GTVLASGPTE 226
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-246 |
5.71e-12 |
|
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: 64.69 E-value: 5.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISF----GGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRP---SRGRIVFKDREIQGRRPDKVAR 77
Cdd:COG0444 3 EVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 78 M---GIARTFQNielfaHMST-----------MENLMLgrHRYMKtglfrgafmwgrrsfagKEEVanRKKVEEIIDLLD 143
Cdd:COG0444 83 IrgrEIQMIFQD-----PMTSlnpvmtvgdqiAEPLRI--HGGLS-----------------KAEA--RERAIELLERVG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 144 L---QSVRNK----FVGGlpygtQKQ-VELGRAlalepqllllDEPSAGMN-SEEKQ--DMIfwiKDIQDTLKVTILLIE 212
Cdd:COG0444 137 LpdpERRLDRypheLSGG-----MRQrVMIARAlalepklliaDEPTTALDvTIQAQilNLL---KDLQRELGLAILFIT 208
|
250 260 270
....*....|....*....|....*....|....*
gi 1308832087 213 HDMKMVMDISDRVLVINFGSpIVE-GTPEEVQRNP 246
Cdd:COG0444 209 HDLGVVAEIADRVAVMYAGR-IVEeGPVEELFENP 242
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
18-242 |
9.70e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 63.50 E-value: 9.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 18 ALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQgrrPDKV--ARMGIARTFQNIElfahmst 95
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLS---EETVwdVRRQVGMVFQNPD------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 96 menlmlgrhrymktGLFRGAFMWGRRSFA------GKEEVANRkkVEEIIDLLDLQSvrnkFVGGLPY---GTQKQ-VEL 165
Cdd:PRK13635 92 --------------NQFVGATVQDDVAFGlenigvPREEMVER--VDQALRQVGMED----FLNREPHrlsGGQKQrVAI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1308832087 166 GRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDiSDRVLVINFGSPIVEGTPEEV 242
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEI 227
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
11-246 |
1.04e-11 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 64.42 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 11 ISF---GGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKV-ARMGIArtFQN 86
Cdd:COG1132 345 VSFsypGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLrRQIGVV--PQD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 87 IELFaHMSTMENLMLGRhrymktglfrgafmwgrrsfagkeEVANRKKVEEIIDLLDLqsvrNKFVGGLP--YGT----- 159
Cdd:COG1132 423 TFLF-SGTIRENIRYGR------------------------PDATDEEVEEAAKAAQA----HEFIEALPdgYDTvvger 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 160 -------QKQ-VELGRAlalepqllllDEPSAGMNSE-EKQdmifwikdIQDTLKV-----TILLIEHDMKMVMDiSDRV 225
Cdd:COG1132 474 gvnlsggQRQrIAIARAllkdppililDEATSALDTEtEAL--------IQEALERlmkgrTTIVIAHRLSTIRN-ADRI 544
|
250 260
....*....|....*....|...
gi 1308832087 226 LVINFGSpIVE-GTPEE-VQRNP 246
Cdd:COG1132 545 LVLDDGR-IVEqGTHEElLARGG 566
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
21-256 |
1.37e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 64.04 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 21 NINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARMGIARTFQNIE---LFAHMSTME 97
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAYITESRRdngFFPNFSIAQ 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 98 NLMLGrhRYMKTGLFRGAfmWGRrsFAGKEEvanRKKVEEIIDLLDLQ-SVRNKFVGGLPYGTQKQVELGRALALEPQLL 176
Cdd:PRK09700 361 NMAIS--RSLKDGGYKGA--MGL--FHEVDE---QRTAENQRELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVI 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 177 LLDEPSAGMNSEEKQDMIFWIKDIQDTLKVtILLIEHDMKMVMDISDRVLVINFGSPIVEGTPEEVQRNPEVLKAYLGEE 256
Cdd:PRK09700 432 IFDEPTRGIDVGAKAEIYKVMRQLADDGKV-ILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDMSEEEIMAWALPQE 510
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
15-239 |
1.45e-11 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 64.26 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 15 GLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRpdKVARMGIARTFQNIELFAHMS 94
Cdd:TIGR01257 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNL--DAVRQSLGMCPQHNILFHHLT 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 95 TMENLMLgrhrYMKtglfrgafmwgrrsFAGKEEVANRKKVEEIIDLLDLQSVRNKFVGGLPYGTQKQVELGRALALEPQ 174
Cdd:TIGR01257 1020 VAEHILF----YAQ--------------LKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAK 1081
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1308832087 175 LLLLDEPSAGMNSEEKQDMifWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSPIVEGTP 239
Cdd:TIGR01257 1082 VVVLDEPTSGVDPYSRRSI--WDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-102 |
1.52e-11 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 62.75 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 4 FKVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGI---YRPSR--GRIVFKDREIQGRRPDKVA-R 77
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndlIPGARveGEILLDGEDIYDPDVDVVElR 91
|
90 100
....*....|....*....|....*
gi 1308832087 78 MGIARTFQNIELFAhMSTMENLMLG 102
Cdd:COG1117 92 RRVGMVFQKPNPFP-KSIYDNVAYG 115
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-229 |
1.87e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 63.50 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 4 FKVEKLSisfgGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARMGIA-- 81
Cdd:COG1129 257 LEVEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRAGIAyv 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 82 ---RTFQNieLFAHMSTMENLMLGR-HRYMKTGLFRGAfmwgrrsfagKEevanRKKVEEIIDLLDL--QSVRNKfVGGL 155
Cdd:COG1129 333 pedRKGEG--LVLDLSIRENITLASlDRLSRGGLLDRR----------RE----RALAEEYIKRLRIktPSPEQP-VGNL 395
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1308832087 156 PYGTQKQVELGRALALEPQLLLLDEPSAGMNSEEKQDmifwIKDIQDTLK---VTILLIEHDMKMVMDISDRVLVIN 229
Cdd:COG1129 396 SGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAE----IYRLIRELAaegKAVIVISSELPELLGLSDRILVMR 468
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
4-86 |
2.99e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 61.97 E-value: 2.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 4 FKVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCING--IYRPSRGRIVFKDREIQGRRPDKVARMGIA 81
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERAHLGIF 87
|
....*
gi 1308832087 82 RTFQN 86
Cdd:CHL00131 88 LAFQY 92
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-247 |
7.03e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 60.70 E-value: 7.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 1 MAFFKVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTL---FNCINGIYRPSR--------GRIVFKDREIQG 69
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLlrvFNRLIELYPEARvsgevyldGQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 70 RRPdkvarmgIARTFQNIELFAHMSTMENLMLG--RHRYMKTglfrgafmwgrrsfagKEEVANRkkVEEIIDLLDL-QS 146
Cdd:PRK14247 81 RRR-------VQMVFQIPNPIPNLSIFENVALGlkLNRLVKS----------------KKELQER--VRWALEKAQLwDE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 147 VRNKF---VGGLPYGTQKQVELGRALALEPQLLLLDEPSAGMNSEEKQDmifwIKDIQDTLK--VTILLIEHDMKMVMDI 221
Cdd:PRK14247 136 VKDRLdapAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAK----IESLFLELKkdMTIVLVTHFPQQAARI 211
|
250 260
....*....|....*....|....*.
gi 1308832087 222 SDRVLVINFGSPIVEGTPEEVQRNPE 247
Cdd:PRK14247 212 SDYVAFLYKGQIVEWGPTREVFTNPR 237
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-247 |
8.76e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 60.88 E-value: 8.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 9 LSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGI------YRPSrGRIVFKDREIQGRRPDKVARMGIAR 82
Cdd:PRK14271 27 LTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMndkvsgYRYS-GDVLLGGRSIFNYRDVLEFRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 83 TFQNIELFAhMSTMENLMLGrhrymktglFRGAFMWGRRSFAGkeeVANRKKVEeiIDLLDlqSVRNKFVGG---LPYGT 159
Cdd:PRK14271 106 LFQRPNPFP-MSIMDNVLAG---------VRAHKLVPRKEFRG---VAQARLTE--VGLWD--AVKDRLSDSpfrLSGGQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 160 QKQVELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDtlKVTILLIEHDMKMVMDISDRVLVINFGSPIVEGTP 239
Cdd:PRK14271 169 QQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLAD--RLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPT 246
|
....*...
gi 1308832087 240 EEVQRNPE 247
Cdd:PRK14271 247 EQLFSSPK 254
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
15-242 |
9.38e-11 |
|
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: 60.19 E-value: 9.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 15 GLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARMgIARTFQNIELFAHmS 94
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQ-VGVVLQENVLFNR-S 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 95 TMENLMLGRHRYMKTGLFRGAFMWGRRSFagkeevanrkkveeiidLLDLQSVRNKFVG----GLPYGTQKQVELGRALA 170
Cdd:cd03252 92 IRDNIALADPGMSMERVIEAAKLAGAHDF-----------------ISELPEGYDTIVGeqgaGLSGGQRQRIAIARALI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1308832087 171 LEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLkvTILLIEHDMKMVMDiSDRVLVINFGSPIVEGTPEEV 242
Cdd:cd03252 155 HNPRILIFDEATSALDYESEHAIMRNMHDICAGR--TVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDEL 223
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
16-246 |
9.60e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 60.88 E-value: 9.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 16 LDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVF--KD-------------REIQGRRPDKVA---- 76
Cdd:PRK15079 34 LKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWlgKDllgmkddewravrSDIQMIFQDPLAslnp 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 77 RMGIA-------RTFQnielfAHMSTME------NLMlgrhryMKTGLFrgafmwgrrsfagkEEVANRKKVEeiidlld 143
Cdd:PRK15079 114 RMTIGeiiaeplRTYH-----PKLSRQEvkdrvkAMM------LKVGLL--------------PNLINRYPHE------- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 144 lqsvrnkFVGGlpygtQKQ-VELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDIS 222
Cdd:PRK15079 162 -------FSGG-----QCQrIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHIS 229
|
250 260
....*....|....*....|....
gi 1308832087 223 DRVLVINFGSPIVEGTPEEVQRNP 246
Cdd:PRK15079 230 DRVLVMYLGHAVELGTYDEVYHNP 253
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
19-241 |
1.31e-10 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 61.22 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 19 LSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGiyRPSRGRIVFKDREIQGRRPDKVARMGIARTFQNIELF-AHMSTME 97
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAF--RSPKGVKGSGSVLLNGMPIDAKEMRAISAYVQQDDLFiPTLTVRE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 98 NLMLGRHRYMKtglfrgafmwgrRSFAGKEEvanRKKVEEIIDLLDLQSVRNKFVG------GLPYGTQKQVELGRALAL 171
Cdd:TIGR00955 119 HLMFQAHLRMP------------RRVTKKEK---RERVDEVLQALGLRKCANTRIGvpgrvkGLSGGERKRLAFASELLT 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 172 EPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSPIVEGTPEE 241
Cdd:TIGR00955 184 DPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQ 253
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
6-91 |
1.33e-10 |
|
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: 60.92 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 6 VEKLSISFGGLDA--LSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARMgIART 83
Cdd:COG4618 333 VENLTVVPPGSKRpiLRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRH-IGYL 411
|
....*...
gi 1308832087 84 FQNIELFA 91
Cdd:COG4618 412 PQDVELFD 419
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-231 |
1.40e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 60.08 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 6 VEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIvfkdreIQGRRPDKVARMGIARTFQ 85
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL------LAGTAPLAEAREDTRLMFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 86 NIELFAHMSTMENLMLGrhrymktglFRGAfmWgrrsfagkeevanRKKVEEIIDLLDLQSVRNKFVGGLPyGTQKQ-VE 164
Cdd:PRK11247 89 DARLLPWKKVIDNVGLG---------LKGQ--W-------------RDAALQALAAVGLADRANEWPAALS-GGQKQrVA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1308832087 165 LGRALALEPQLLLLDEPSAGMNSE---EKQDMI--FWIKDiqdtlKVTILLIEHDMKMVMDISDRVLVINFG 231
Cdd:PRK11247 144 LARALIHRPGLLLLDEPLGALDALtriEMQDLIesLWQQH-----GFTVLLVTHDVSEAVAMADRVLLIEEG 210
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
6-247 |
1.60e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 61.02 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 6 VEKLSISF----GGLDALSNINFEVQEGQIFSIIGPNGAGKT----TLFNCI---------NGIYRPSRGRIVFKDREIQ 68
Cdd:PRK10261 15 VENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqagglvqcDKMLLRRRSRQVIELSEQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 69 GRRPDKVARMGIARTFQNielfaHMSTMENLM-LGRHRYMKTGLFRGafmwgrrsFAGKEEVANRKKVEEIIDLLDLQSV 147
Cdd:PRK10261 95 AAQMRHVRGADMAMIFQE-----PMTSLNPVFtVGEQIAESIRLHQG--------ASREEAMVEAKRMLDQVRIPEAQTI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 148 RNKFVGGLPYGTQKQVELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLV 227
Cdd:PRK10261 162 LSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLV 241
|
250 260
....*....|....*....|
gi 1308832087 228 INFGSPIVEGTPEEVQRNPE 247
Cdd:PRK10261 242 MYQGEAVETGSVEQIFHAPQ 261
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
6-190 |
1.62e-10 |
|
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: 59.04 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 6 VEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDreiqgrRPDKVARMGIARtfq 85
Cdd:cd03231 3 ADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNG------GPLDFQRDSIAR--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 86 NIELFAH-------MSTMENLMLgrhrymktglfrgafmWgrRSFAGKEEvanrkkVEEIIDLLDLQSVRNKFVGGLPYG 158
Cdd:cd03231 74 GLLYLGHapgikttLSVLENLRF----------------W--HADHSDEQ------VEEALARVGLNGFEDRPVAQLSAG 129
|
170 180 190
....*....|....*....|....*....|....
gi 1308832087 159 TQKQVELGRALALEPQLLLLDEPSAGM--NSEEK 190
Cdd:cd03231 130 QQRRVALARLLLSGRPLWILDEPTTALdkAGVAR 163
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-82 |
1.68e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 59.55 E-value: 1.68e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1308832087 5 KVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREiqGRRPDkVARMGIAR 82
Cdd:PRK11701 8 SVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRD--GQLRD-LYALSEAE 82
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
6-67 |
2.22e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 58.73 E-value: 2.22e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1308832087 6 VEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREI 67
Cdd:PRK13539 5 GEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI 66
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-247 |
3.03e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 59.09 E-value: 3.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 7 EKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRR-------PDKVaRMG 79
Cdd:PRK14267 8 VNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRNiyspdvdPIEV-RRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 80 IARTFQNIELFAHMSTMENLMLGrhrYMKTGLFRGA------FMWGRRSFAGKEEVANRkkveeiidlldlqsvRNKFVG 153
Cdd:PRK14267 87 VGMVFQYPNPFPHLTIYDNVAIG---VKLNGLVKSKkelderVEWALKKAALWDEVKDR---------------LNDYPS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 154 GLPYGTQKQVELGRALALEPQLLLLDEPSAGMN---SEEKQDMIFWIKDiqdtlKVTILLIEHDMKMVMDISDRVLVINF 230
Cdd:PRK14267 149 NLSGGQRQRLVIARALAMKPKILLMDEPTANIDpvgTAKIEELLFELKK-----EYTIVLVTHSPAQAARVSDYVAFLYL 223
|
250
....*....|....*..
gi 1308832087 231 GSPIVEGTPEEVQRNPE 247
Cdd:PRK14267 224 GKLIEVGPTRKVFENPE 240
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-238 |
4.88e-10 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 58.19 E-value: 4.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 25 EVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIvfkdreiqgrrpdKVARMGIARTFQNIELFAHMSTMENLM---- 100
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI-------------EIELDTVSYKPQYIKADYEGTVRDLLSsitk 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 101 -LGRHRYMKTglfrgafmwgrrsfagkeEVANRKKVEEIIDlldlQSVRNkfvggLPYGTQKQVELGRALALEPQLLLLD 179
Cdd:cd03237 88 dFYTHPYFKT------------------EIAKPLQIEQILD----REVPE-----LSGGELQRVAIAACLSKDADIYLLD 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1308832087 180 EPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINfGSPIVEGT 238
Cdd:cd03237 141 EPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFE-GEPSVNGV 198
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-223 |
6.50e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 58.12 E-value: 6.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPS-----RGRIVFKDREIQGRRPD-KVARM 78
Cdd:PRK14258 9 KVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIYERRVNlNRLRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 79 GIARTFQNIELFAhMSTMENLMlgrhrymktglfrgafmWGRRSFAGKEEVANRKKVEEIIDLLDL-QSVRNKFVGG--- 154
Cdd:PRK14258 89 QVSMVHPKPNLFP-MSVYDNVA-----------------YGVKIVGWRPKLEIDDIVESALKDADLwDEIKHKIHKSald 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1308832087 155 LPYGTQKQVELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISD 223
Cdd:PRK14258 151 LSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSD 219
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
18-250 |
6.61e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 58.22 E-value: 6.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 18 ALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVAR-----MGIARTFQNIELFAh 92
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKqirkkVGLVFQFPESQLFE- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 93 mstmenlmlgrhrymKTGLFRGAFmwGRRSFAGKEEVANRKKVEEII------DLLDlqsvRNKFvgGLPYGTQKQVELG 166
Cdd:PRK13649 101 ---------------ETVLKDVAF--GPQNFGVSQEEAEALAREKLAlvgiseSLFE----KNPF--ELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 167 RALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTlKVTILLIEHDMKMVMDISDRVLVINFGSPIVEGTPEEVQRNP 246
Cdd:PRK13649 158 GILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQDV 236
|
....
gi 1308832087 247 EVLK 250
Cdd:PRK13649 237 DFLE 240
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
18-246 |
1.01e-09 |
|
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: 56.99 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 18 ALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRP----SRGRIVFKDREIQgrrPDKVARMGIARTFQN-IELFAH 92
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGRPLL---PLSIRGRHIATIMQNpRTAFNP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 93 MSTMenlmlgRHRYMKTGLFRGAFMWGRRSFAGKE-EVANRKKVEEIIDLLDLQsvrnkfvggLPYGTQKQVELGRALAL 171
Cdd:TIGR02770 78 LFTM------GNHAIETLRSLGKLSKQARALILEAlEAVGLPDPEEVLKKYPFQ---------LSGGMLQRVMIALALLL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1308832087 172 EPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSPIVEGTPEEVQRNP 246
Cdd:TIGR02770 143 EPPFLIADEPTTDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNP 217
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
18-250 |
1.22e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 57.50 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 18 ALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRP---SRGRIVFKDREIQGRRP-DKVARMGIarTFQNIELFAHM 93
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVwDIREKVGI--VFQNPDNQFVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 94 STMENLMlgrhrymktglfrgAFMWGRRSFAGKEEVANRKKVEEIIDLLDLQSVRNKFVGGlpyGTQKQVELGRALALEP 173
Cdd:PRK13640 100 ATVGDDV--------------AFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSG---GQKQRVAIAGILAVEP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1308832087 174 QLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVmDISDRVLVINFGSPIVEGTPEEVQRNPEVLK 250
Cdd:PRK13640 163 KIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVEMLK 238
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
4-242 |
1.24e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 57.41 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 4 FKVEKLSisfgGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGrIVFKDREIQGRRPDKVARMGIART 83
Cdd:PRK13642 12 FKYEKES----DVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEG-KVKIDGELLTAENVWNLRRKIGMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 84 FQNIELFAHMSTMENLMlgrhrymktglfrgAFMWGRRSFAGKEEVanrKKVEEIIDLLDLQSVRNKFVGGLPYGTQKQV 163
Cdd:PRK13642 87 FQNPDNQFVGATVEDDV--------------AFGMENQGIPREEMI---KRVDEALLAVNMLDFKTREPARLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1308832087 164 ELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDiSDRVLVINFGSPIVEGTPEEV 242
Cdd:PRK13642 150 AVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSEL 227
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
5-231 |
1.68e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 57.71 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISfggldALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARMGIARTF 84
Cdd:PRK10762 259 KVDNLSGP-----GVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANGIVYIS 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 85 QNIE---LFAHMSTMENLMLGRHRYMKTGLFRgafmwgrrsFAGKEEvanRKKVEEIIDLLDLQS-VRNKFVGGLPYGTQ 160
Cdd:PRK10762 334 EDRKrdgLVLGMSVKENMSLTALRYFSRAGGS---------LKHADE---QQAVSDFIRLFNIKTpSMEQAIGLLSGGNQ 401
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1308832087 161 KQVELGRALALEPQLLLLDEPSAGMNSEEKQDmifwIKDIQDTLK---VTILLIEHDMKMVMDISDRVLVINFG 231
Cdd:PRK10762 402 QKVAIARGLMTRPKVLILDEPTRGVDVGAKKE----IYQLINQFKaegLSIILVSSEMPEVLGMSDRILVMHEG 471
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-247 |
1.68e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 56.98 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 4 FKVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCIN---GIYRPS---RGRIVFKDREIqgRRPDKVA- 76
Cdd:PRK14246 11 FNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNrliEIYDSKikvDGKVLYFGKDI--FQIDAIKl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 77 RMGIARTFQNIELFAHMSTMENLMlgrhrymktglfrgafmWGRRSFAGKEEVANRKKVEEIIDLLDL-QSVRNKF---V 152
Cdd:PRK14246 89 RKEVGMVFQQPNPFPHLSIYDNIA-----------------YPLKSHGIKEKREIKKIVEECLRKVGLwKEVYDRLnspA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 153 GGLPYGTQKQVELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDtlKVTILLIEHDMKMVMDISDRVLVINFGS 232
Cdd:PRK14246 152 SQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKN--EIAIVIVSHNPQQVARVADYVAFLYNGE 229
|
250
....*....|....*
gi 1308832087 233 PIVEGTPEEVQRNPE 247
Cdd:PRK14246 230 LVEWGSSNEIFTSPK 244
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-64 |
2.47e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 57.25 E-value: 2.47e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKD 64
Cdd:TIGR03719 324 EAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGE 383
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
19-252 |
2.58e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 56.09 E-value: 2.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 19 LSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYrPSRGRIVFKDREIQGRRPDKVARMgiaRTF---QNIELFAhMST 95
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARH---RAYlsqQQTPPFA-MPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 96 MENLMLGRHrymktglfrgafmwgrrsfAGKEEVANRKKVEEIIDLLDLQSVRNKFVGGLPYGTQKQVELG-------RA 168
Cdd:PRK03695 87 FQYLTLHQP-------------------DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAavvlqvwPD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 169 LALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQdTLKVTILLIEHDMKMVMDISDRVLVINFGSPIVEGTPEEVQRNPEV 248
Cdd:PRK03695 148 INPAGQLLLLDEPMNSLDVAQQAALDRLLSELC-QQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENL 226
|
....
gi 1308832087 249 LKAY 252
Cdd:PRK03695 227 AQVF 230
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
6-183 |
2.75e-09 |
|
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: 55.44 E-value: 2.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 6 VEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVarmgiartfQ 85
Cdd:TIGR01189 3 ARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPH---------E 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 86 NIELFAH-------MSTMENLMLGRHrymktgLFRGAfmwgrrsfagkeevanRKKVEEIIDLLDLQSVRNKFVGGLPYG 158
Cdd:TIGR01189 74 NILYLGHlpglkpeLSALENLHFWAA------IHGGA----------------QRTIEDALAAVGLTGFEDLPAAQLSAG 131
|
170 180
....*....|....*....|....*
gi 1308832087 159 TQKQVELGRALALEPQLLLLDEPSA 183
Cdd:TIGR01189 132 QQRRLALARLWLSRRPLWILDEPTT 156
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
20-231 |
3.36e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.98 E-value: 3.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 20 SNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARMGIartfqnielfahmstmenL 99
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGL------------------V 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 100 MLGRHRyMKTGLFRGA--------FMWGRRSF---AGKEevanRKKVEEIIDLLDLQ-SVRNKFVGGLPYGTQKQVELGR 167
Cdd:PRK15439 342 YLPEDR-QSSGLYLDAplawnvcaLTHNRRGFwikPARE----NAVLERYRRALNIKfNHAEQAARTLSGGNQQKVLIAK 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1308832087 168 ALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTlKVTILLIEHDMKMVMDISDRVLVINFG 231
Cdd:PRK15439 417 CLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQG 479
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
5-103 |
5.51e-09 |
|
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: 56.21 E-value: 5.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISF-GGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARMgIART 83
Cdd:TIGR02868 336 ELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRR-VSVC 414
|
90 100
....*....|....*....|
gi 1308832087 84 FQNIELFAhMSTMENLMLGR 103
Cdd:TIGR02868 415 AQDAHLFD-TTVRENLRLAR 433
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6-60 |
6.75e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 56.05 E-value: 6.75e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1308832087 6 VEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRI 60
Cdd:PRK15064 322 VENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
19-78 |
7.11e-09 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 54.85 E-value: 7.11e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 19 LSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYrPSRGRIVFKDREIQGRRPDKVARM 78
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARH 70
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
18-63 |
7.24e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 56.05 E-value: 7.24e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1308832087 18 ALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFK 63
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIK 84
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
18-105 |
7.26e-09 |
|
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: 54.54 E-value: 7.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 18 ALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARMgIARTFQNIELFaHMSTME 97
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQ-IGLVSQDVFLF-NDTVAE 94
|
....*...
gi 1308832087 98 NLMLGRHR 105
Cdd:cd03251 95 NIAYGRPG 102
|
|
| BCA_ABC_TP_C |
pfam12399 |
Branched-chain amino acid ATP-binding cassette transporter; This domain family is found in ... |
234-256 |
7.70e-09 |
|
Branched-chain amino acid ATP-binding cassette transporter; This domain family is found in bacteria, archaea and eukaryotes, and is approximately 30 amino acids in length. The family is found in association with pfam00005. There is a conserved AYLG sequence motif. This family is the C terminal of an ATP dependent branched-chain amino acid transporter. This domain is essential for LPS transport, through critical interactions with Walker A and switch helix domains.
Pssm-ID: 463560 Cd Length: 25 Bit Score: 49.94 E-value: 7.70e-09
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
11-241 |
7.91e-09 |
|
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: 54.54 E-value: 7.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 11 ISFG---GLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARMgIARTFQNI 87
Cdd:cd03253 6 VTFAydpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRA-IGVVPQDT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 88 ELFaHMSTMENLmlgrhRYmktglfrgafmwGRRSfAGKEEVANRKKVEEIIDLldLQSVRNKF---VG--GLPY-GTQK 161
Cdd:cd03253 85 VLF-NDTIGYNI-----RY------------GRPD-ATDEEVIEAAKAAQIHDK--IMRFPDGYdtiVGerGLKLsGGEK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 162 Q-VELGRALALEPQLLLLDEPSAGMNSEEKQdmifwikDIQDTLKV-----TILLIEHDMKMVMDiSDRVLVINFGSPIV 235
Cdd:cd03253 144 QrVAIARAILKNPPILLLDEATSALDTHTER-------EIQAALRDvskgrTTIVIAHRLSTIVN-ADKIIVLKDGRIVE 215
|
....*.
gi 1308832087 236 EGTPEE 241
Cdd:cd03253 216 RGTHEE 221
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-61 |
1.32e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.12 E-value: 1.32e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1308832087 6 VEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIV 61
Cdd:PRK11819 327 AENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIK 382
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
16-246 |
2.43e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 54.34 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 16 LDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARM---GIARTFQNIELFAH 92
Cdd:PRK10535 21 VEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLrreHFGFIFQRYHLLSH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 93 MSTMENLMLgrhrymktglfrgafmwgRRSFAGKEEVANRKKVEEIIDLLDLQSVRNKFVGGLPYGTQKQVELGRALALE 172
Cdd:PRK10535 101 LTAAQNVEV------------------PAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1308832087 173 PQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKvTILLIEHDMKmVMDISDRVLVINFGSpIVEGTPEEVQRNP 246
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQLRDRGH-TVIIVTHDPQ-VAAQAERVIEIRDGE-IVRNPPAQEKVNV 233
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
16-246 |
2.44e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 53.64 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 16 LDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQ----GRRPDKVaRMgiartfqnieLFA 91
Cdd:PRK15112 26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgdySYRSQRI-RM----------IFQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 92 HMSTMENlmlGRHRYMKTGLFrgafmwgrrSFAGKEEVANRKKVEEIIDLLDLQSVRNKFVGGLPY----GTQKQVELGR 167
Cdd:PRK15112 95 DPSTSLN---PRQRISQILDF---------PLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHmlapGQKQRLGLAR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1308832087 168 ALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSPIVEGTPEEVQRNP 246
Cdd:PRK15112 163 ALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASP 241
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
18-239 |
2.81e-08 |
|
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: 52.88 E-value: 2.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 18 ALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVaRMGIARTFQNIELFAhmSTM- 96
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDL-RSRISIIPQDPVLFS--GTIr 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 97 ENL-MLGRHRymktglfrGAFMWgrrsfAGKEEVANRKKVEEIIDLLDLQSVRNKfvGGLPYGtQKQ-VELGRALALEPQ 174
Cdd:cd03244 96 SNLdPFGEYS--------DEELW-----QALERVGLKEFVESLPGGLDTVVEEGG--ENLSVG-QRQlLCLARALLRKSK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1308832087 175 LLLLDEPSAGMNSEekQDMIfwikdIQDTLK-----VTILLIEHDMKMVMDiSDRVLVINFGSpIVE-GTP 239
Cdd:cd03244 160 ILVLDEATASVDPE--TDAL-----IQKTIReafkdCTVLTIAHRLDTIID-SDRILVLDKGR-VVEfDSP 221
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
7-245 |
2.88e-08 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 54.20 E-value: 2.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 7 EKLSISFGGL-DALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIvfkdrEIQGRRPDKVARMG----IA 81
Cdd:PRK13657 338 DDVSFSYDNSrQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRI-----LIDGTDIRTVTRASlrrnIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 82 RTFQNIELFAHmSTMENLMLGRHRymktglfrgafmwgrrsfAGKEEVANRKKVEEIIDLLDLQSVRNKFVGG-----LP 156
Cdd:PRK13657 413 VVFQDAGLFNR-SIEDNIRVGRPD------------------ATDEEMRAAAERAQAHDFIERKPDGYDTVVGergrqLS 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 157 YGTQKQVELGRALALEPQLLLLDEPSAGMNSE-EKQdmifwIKDIQDTLKV--TILLIEHDMKMVMDiSDRVLVINFGSP 233
Cdd:PRK13657 474 GGERQRLAIARALLKDPPILILDEATSALDVEtEAK-----VKAALDELMKgrTTFIIAHRLSTVRN-ADRILVFDNGRV 547
|
250
....*....|...
gi 1308832087 234 IVEGTPEE-VQRN 245
Cdd:PRK13657 548 VESGSFDElVARG 560
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
21-231 |
4.63e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 53.29 E-value: 4.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 21 NINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYrPSR--GRIVFKDREIQGRRPDKVARMGIA-----RTFQNIelFAHM 93
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAY-PGKfeGNVFINGKPVDIRNPAQAIRAGIAmvpedRKRHGI--VPIL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 94 STMENLMLGrhrymktglfrgafmwGRRSFAGK---EEVANRKKVEEIIDLLDLQSVRNKF-VGGLPYGTQKQVELGRAL 169
Cdd:TIGR02633 355 GVGKNITLS----------------VLKSFCFKmriDAAAELQIIGSAIQRLKVKTASPFLpIGRLSGGNQQKAVLAKML 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1308832087 170 ALEPQLLLLDEPSAGMNSEEKQDmIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFG 231
Cdd:TIGR02633 419 LTNPRVLILDEPTRGVDVGAKYE-IYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-246 |
6.71e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 52.42 E-value: 6.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 1 MAFFKVEKLSISFGGLD----ALSNINFEVQEGQIFSIIGPNGAGKT-TLFnCINGIYrPSRGRI----VFKDREIQGRR 71
Cdd:PRK09473 10 DALLDVKDLRVTFSTPDgdvtAVNDLNFSLRAGETLGIVGESGSGKSqTAF-ALMGLL-AANGRIggsaTFNGREILNLP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 72 PDKVARM---GIARTFQN--IELFAHMST----MENLMLgrHRYMktglfrgafmwgrrsfaGKEEVanrkkVEEIIDLL 142
Cdd:PRK09473 88 EKELNKLraeQISMIFQDpmTSLNPYMRVgeqlMEVLML--HKGM-----------------SKAEA-----FEESVRML 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 143 DlqSVR----NKFVGGLPY----GTQKQVELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHD 214
Cdd:PRK09473 144 D--AVKmpeaRKRMKMYPHefsgGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHD 221
|
250 260 270
....*....|....*....|....*....|..
gi 1308832087 215 MKMVMDISDRVLVINFGSPIVEGTPEEVQRNP 246
Cdd:PRK09473 222 LGVVAGICDKVLVMYAGRTMEYGNARDVFYQP 253
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
4-229 |
7.01e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 52.09 E-value: 7.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 4 FKVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGI------YRpSRGRIVFKDREIQGRRPDKVA- 76
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndlipgFR-VEGKVTFHGKNLYAPDVDPVEv 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 77 RMGIARTFQNIELFAHmSTMENLMLG-RHRYMKTGL-------FRGAFMWgrrsfagkEEVANRKKVEEIidlldlqsvr 148
Cdd:PRK14243 90 RRRIGMVFQKPNPFPK-SIYDNIAYGaRINGYKGDMdelversLRQAALW--------DEVKDKLKQSGL---------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 149 nkfvgGLPYGTQKQVELGRALALEPQLLLLDEPSAGMnseekqDMI--FWIKDIQDTLK--VTILLIEHDMKMVMDISDR 224
Cdd:PRK14243 151 -----SLSGGQQQRLCIARAIAVQPEVILMDEPCSAL------DPIstLRIEELMHELKeqYTIIIVTHNMQQAARVSDM 219
|
....*
gi 1308832087 225 VLVIN 229
Cdd:PRK14243 220 TAFFN 224
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
19-71 |
7.54e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 51.49 E-value: 7.54e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1308832087 19 LSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRR 71
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDL 69
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
19-258 |
1.36e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 52.15 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 19 LSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGiYRPSRGRIVFKDREIqgRRPDKVA-RMGIARTFQNIELFaHMSTME 97
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGSLKINGIEL--RELDPESwRKHLSWVGQNPQLP-HGTLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 98 NLMLGRHRymktglfrgafmwgrrsfAGKEEVAN---RKKVEEIIDLLD--LQSVRNKFVGGLPYGTQKQVELGRALALE 172
Cdd:PRK11174 442 NVLLGNPD------------------ASDEQLQQaleNAWVSEFLPLLPqgLDTPIGDQAAGLSVGQAQRLALARALLQP 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 173 PQLLLLDEPSAG--MNSEEKqdmifwikdIQDTLKV-----TILLIEHDMKMVMDIsDRVLVINFGSPIVEGTPEEVQRN 245
Cdd:PRK11174 504 CQLLLLDEPTASldAHSEQL---------VMQALNAasrrqTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQA 573
|
250
....*....|...
gi 1308832087 246 PEVLKAYLGEENA 258
Cdd:PRK11174 574 GGLFATLLAHRQE 586
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
20-73 |
1.80e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 50.19 E-value: 1.80e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1308832087 20 SNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPD 73
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE 71
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
4-62 |
1.82e-07 |
|
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: 49.84 E-value: 1.82e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1308832087 4 FKVEKLSIS--FGGLdALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVF 62
Cdd:cd03223 1 IELENLSLAtpDGRV-LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM 60
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
6-85 |
2.34e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 50.56 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 6 VEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGI--YRPSRGRIVFKDREIQGRRPDKVARMGIART 83
Cdd:PRK09580 4 IKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGEGIFMA 83
|
..
gi 1308832087 84 FQ 85
Cdd:PRK09580 84 FQ 85
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-246 |
2.65e-07 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 50.57 E-value: 2.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 1 MAFFKVEKLSISF----GGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGI----YRPSRGRIVFKDREI---QG 69
Cdd:PRK15093 1 MPLLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnWRVTADRMRFDDIDLlrlSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 70 RRPDKVARMGIARTFQNIE--LFAHMSTMENLMLGRHRYMKTGLFRGAFMWGRRsfagkeevanrkkveEIIDLLDLQSV 147
Cdd:PRK15093 81 RERRKLVGHNVSMIFQEPQscLDPSERVGRQLMQNIPGWTYKGRWWQRFGWRKR---------------RAIELLHRVGI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 148 RN--KFVGGLPY----GTQKQVELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDI 221
Cdd:PRK15093 146 KDhkDAMRSFPYelteGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQW 225
|
250 260
....*....|....*....|....*
gi 1308832087 222 SDRVLVINFGSPIVEGTPEEVQRNP 246
Cdd:PRK15093 226 ADKINVLYCGQTVETAPSKELVTTP 250
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-227 |
2.89e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 51.07 E-value: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 22 INFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARMGIA-----RTFQNIelFAHMSTM 96
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIMlcpedRKAEGI--IPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 97 ENLMLGRhrymktglfRGAFMWGRRSFAGKEEVANrkkVEEIIDLLDLQS-VRNKFVGGLPYGTQKQVELGRALALEPQL 175
Cdd:PRK11288 350 DNINISA---------RRHHLRAGCLINNRWEAEN---ADRFIRSLNIKTpSREQLIMNLSGGNQQKAILGRWLSEDMKV 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1308832087 176 LLLDEPSAGMNSEEKQDMIFWIKDIQDTlKVTILLIEHDMKMVMDISDRVLV 227
Cdd:PRK11288 418 ILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVV 468
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
21-231 |
3.64e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 50.70 E-value: 3.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 21 NINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYrPSR--GRIVFKDREIQGRRPDKVARMGIA-----RTFQNIELFahM 93
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLFGAY-PGRweGEIFIDGKPVKIRNPQQAIAQGIAmvpedRKRDGIVPV--M 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 94 STMENLMLGR-HRYMKTGLFRGAfmwgrrsfagkeevANRKKVEEIIDLLDLQSVRNKF-VGGLPYGTQKQVELGRALAL 171
Cdd:PRK13549 357 GVGKNITLAAlDRFTGGSRIDDA--------------AELKTILESIQRLKVKTASPELaIARLSGGNQQKAVLAKCLLL 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1308832087 172 EPQLLLLDEPSAGMNSEEKQDmIFwiKDIQDTLK--VTILLIEHDMKMVMDISDRVLVINFG 231
Cdd:PRK13549 423 NPKILILDEPTRGIDVGAKYE-IY--KLINQLVQqgVAIIVISSELPEVLGLSDRVLVMHEG 481
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
17-63 |
3.73e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 49.81 E-value: 3.73e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1308832087 17 DALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFK 63
Cdd:PRK11629 23 DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFN 69
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-261 |
3.90e-07 |
|
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: 50.55 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 27 QEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIvfkDREiqgrrPDKVArmgIARTFQNIELFAHMSTMENlmlgrhry 106
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDY---DEE-----PSWDE---VLKRFRGTELQDYFKKLAN-------- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 107 mktglfrgafmwGR--------------RSFAGK-----EEVANRKKVEEIIDLLDLQSVRNKFVGGLPYGTQKQVELGR 167
Cdd:COG1245 158 ------------GEikvahkpqyvdlipKVFKGTvrellEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 168 ALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKvTILLIEHDMkMVMD-ISDRVLVInFGSPIVEGtpeeVQRNP 246
Cdd:COG1245 226 ALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGK-YVLVVEHDL-AILDyLADYVHIL-YGEPGVYG----VVSKP 298
|
250 260
....*....|....*....|....
gi 1308832087 247 --------EVLKAYLGEENA-IRD 261
Cdd:COG1245 299 ksvrvginQYLDGYLPEENVrIRD 322
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-246 |
4.48e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 50.13 E-value: 4.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 1 MAFFKVEKLSISFGGLD----ALSNINFEVQEGQIFSIIGPNGAGKTTLFNCING-IYRPSR---GRIVFKDREIQgRRP 72
Cdd:PRK11022 1 MALLNVDKLSVHFGDESapfrAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGlIDYPGRvmaEKLEFNGQDLQ-RIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 73 DKVARM----GIARTFQNielfaHMSTMENLMLGRHRYMKtglfrgafmwgrrsfAGK-EEVANRK-KVEEIIDLL---- 142
Cdd:PRK11022 80 EKERRNlvgaEVAMIFQD-----PMTSLNPCYTVGFQIME---------------AIKvHQGGNKKtRRQRAIDLLnqvg 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 143 --DLQSVRNKFVGGLPYGTQKQVELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMD 220
Cdd:PRK11022 140 ipDPASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAE 219
|
250 260
....*....|....*....|....*.
gi 1308832087 221 ISDRVLVINFGSPIVEGTPEEVQRNP 246
Cdd:PRK11022 220 AAHKIIVMYAGQVVETGKAHDIFRAP 245
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
7-90 |
7.62e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 48.56 E-value: 7.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 7 EKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVaRMGIARTFQN 86
Cdd:PRK10247 11 QNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIY-RQQVSYCAQT 89
|
....
gi 1308832087 87 IELF 90
Cdd:PRK10247 90 PTLF 93
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
19-231 |
7.92e-07 |
|
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: 48.62 E-value: 7.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 19 LSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRpDKVARMGIARTFQNIELFAHmSTMEN 98
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYE-HKYLHSKVSLVGQEPVLFAR-SLQDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 99 LmlgrhrymktglfrgAFMWGRRSFAGKEEVANRKKVEEIIDLLDL---QSVRNKfvGGLPYGTQKQ-VELGRALALEPQ 174
Cdd:cd03248 108 I---------------AYGLQSCSFECVKEAAQKAHAHSFISELASgydTEVGEK--GSQLSGGQKQrVAIARALIRNPQ 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1308832087 175 LLLLDEPSAGMNSEEKQDMIFWIKDiqDTLKVTILLIEHDMKMVmDISDRVLVINFG 231
Cdd:cd03248 171 VLILDEATSALDAESEQQVQQALYD--WPERRTVLVIAHRLSTV-ERADQILVLDGG 224
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
22-67 |
1.12e-06 |
|
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: 49.03 E-value: 1.12e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1308832087 22 INFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREI 67
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV 396
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
5-247 |
1.17e-06 |
|
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: 49.30 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISF-----------GGLDALSNINFEVQEGQIFSIIGPNGAGKTTLfncinG--IYR--PSRGRIVFKDREIQG 69
Cdd:COG4172 277 EARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTL-----GlaLLRliPSEGEIRFDGQDLDG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 70 RRPDKV----ARMGIarTFQNIelFAHMS---TMENLM---LGRHRymkTGLfrgafmwgrrsfaGKEEVanRKKVEEIi 139
Cdd:COG4172 352 LSRRALrplrRRMQV--VFQDP--FGSLSprmTVGQIIaegLRVHG---PGL-------------SAAER--RARVAEA- 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 140 dlldLQSV------RNK----FVGGlpygtQKQ-VELGRALALEPQLLLLDEP-SAGMNSEEKQdMIFWIKDIQDTLKVT 207
Cdd:COG4172 409 ----LEEVgldpaaRHRypheFSGG-----QRQrIAIARALILEPKLLVLDEPtSALDVSVQAQ-ILDLLRDLQREHGLA 478
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1308832087 208 ILLIEHDMKMVMDISDRVLVINFGSpIVE-GTPEEVQRNPE 247
Cdd:COG4172 479 YLFISHDLAVVRALAHRVMVMKDGK-VVEqGPTEQVFDAPQ 518
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
179-259 |
1.37e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 49.44 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 179 DEPSAGMNSEEKQDMIFWIKDIQDTLKvTILLIEHDMKMVmDISDRVLVIN-----FGSPIV-EGTPEEVQRNPEVLKA- 251
Cdd:PRK00635 503 DEPSIGLHPQDTHKLINVIKKLRDQGN-TVLLVEHDEQMI-SLADRIIDIGpgagiFGGEVLfNGSPREFLAKSDSLTAk 580
|
....*...
gi 1308832087 252 YLGEENAI 259
Cdd:PRK00635 581 YLRQELTI 588
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
19-79 |
1.86e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 47.65 E-value: 1.86e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1308832087 19 LSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIY--RPSRGRIVFKDREIQGRRP--DKVARMG 79
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGREASliDAIGRKG 110
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-238 |
1.96e-06 |
|
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: 48.63 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 25 EVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDReiqgrrpdkvarmgIARTFQNIELFAHMSTMENLMLGRH 104
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK--------------ISYKPQYISPDYDGTVEEFLRSANT 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 105 RYMKTGLFrgafmwgrrsfagKEEVANRKKVEEIIDlldlQSVRNkFVGGlpygtqkqvELGR-----ALALEPQLLLLD 179
Cdd:COG1245 428 DDFGSSYY-------------KTEIIKPLGLEKLLD----KNVKD-LSGG---------ELQRvaiaaCLSRDADLYLLD 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1308832087 180 EPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINfGSPIVEGT 238
Cdd:COG1245 481 EPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMVFE-GEPGVHGH 538
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
18-62 |
2.06e-06 |
|
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: 47.08 E-value: 2.06e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1308832087 18 ALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVF 62
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV 64
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
19-51 |
2.23e-06 |
|
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: 46.78 E-value: 2.23e-06
10 20 30
....*....|....*....|....*....|...
gi 1308832087 19 LSNINFEVQEGQIFSIIGPNGAGKTTLFNCING 51
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAG 57
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-247 |
2.46e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 48.31 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 18 ALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVA--RMGIARTFQniELFAHM-- 93
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQalRRDIQFIFQ--DPYASLdp 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 94 ------STMENLMLgrhrymkTGLFRGAfmwgrrsfagkeevANRKKVEEIIDLLDLQSVR-----NKFVGGlpygtQKQ 162
Cdd:PRK10261 417 rqtvgdSIMEPLRV-------HGLLPGK--------------AAAARVAWLLERVGLLPEHawrypHEFSGG-----QRQ 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 163 -VELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSpIVEGTPEE 241
Cdd:PRK10261 471 rICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQ-IVEIGPRR 549
|
....*..
gi 1308832087 242 -VQRNPE 247
Cdd:PRK10261 550 aVFENPQ 556
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
18-93 |
2.64e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 48.04 E-value: 2.64e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1308832087 18 ALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVaRMGIARTFQNIELFAHM 93
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDY-RKLFSAVFTDFHLFDQL 412
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
3-246 |
3.29e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 47.27 E-value: 3.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 3 FFKVEKLsisfggLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQG--RRPDKVARMGI 80
Cdd:PRK11308 21 LFKPERL------VKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKadPEAQKLLRQKI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 81 ARTFQNIelFAHM-------STMENLMLgrhryMKTGLfrgafmwgrrsfaGKEEvaNRKKVEEIIDLLDLqsvRNKFVG 153
Cdd:PRK11308 95 QIVFQNP--YGSLnprkkvgQILEEPLL-----INTSL-------------SAAE--RREKALAMMAKVGL---RPEHYD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 154 GLPY---GTQKQ-VELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVIN 229
Cdd:PRK11308 150 RYPHmfsGGQRQrIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMY 229
|
250
....*....|....*..
gi 1308832087 230 FGSPIVEGTPEEVQRNP 246
Cdd:PRK11308 230 LGRCVEKGTKEQIFNNP 246
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-60 |
3.31e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.02 E-value: 3.31e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1308832087 4 FKVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRI 60
Cdd:PRK11147 320 FEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI 376
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
19-235 |
3.77e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.80 E-value: 3.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 19 LSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGiyRPSRGRIVFKDREIQGRRPDKvarmgiarTFQNIELFA-----HM 93
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTGVITGGDRLVNGRPLDS--------SFQRSIGYVqqqdlHL 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 94 STMEnlmlgrhryMKTGLFRGAFMwgRRSfagkEEVANRKK---VEEIIDLLDLQSVRNKFVG----GLPYGTQKQ---- 162
Cdd:TIGR00956 849 PTST---------VRESLRFSAYL--RQP----KSVSKSEKmeyVEEVIKLLEMESYADAVVGvpgeGLNVEQRKRltig 913
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1308832087 163 VELgraLALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSPIV 235
Cdd:TIGR00956 914 VEL---VAKPKLLLFLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSAILFEEFDRLLLLQKGGQTV 983
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-102 |
4.89e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 47.13 E-value: 4.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISFGGLD---------ALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQgRRPDKV 75
Cdd:PRK11160 333 AADQVSLTLNNVSftypdqpqpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIA-DYSEAA 411
|
90 100
....*....|....*....|....*..
gi 1308832087 76 ARMGIARTFQNIELFAHmSTMENLMLG 102
Cdd:PRK11160 412 LRQAISVVSQRVHLFSA-TLRDNLLLA 437
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
19-239 |
5.28e-06 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 46.60 E-value: 5.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 19 LSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQG--RRPDKVARMGIARTFQN-IELFAHMST 95
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlnRAQRKAFRRDIQMVFQDsISAVNPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 96 MENLMLGRHRYMkTGLfrgafmwgrrsfagkEEVANRKKVEEIIDLLDLQ-SVRNKFVGGLPYGTQKQVELGRALALEPQ 174
Cdd:PRK10419 108 VREIIREPLRHL-LSL---------------DKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPK 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1308832087 175 LLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSpIVEGTP 239
Cdd:PRK10419 172 LLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQ-IVETQP 235
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
17-103 |
5.75e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 47.01 E-value: 5.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 17 DALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVaRMGIARTFQNIELFAHmSTM 96
Cdd:PRK10789 329 PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSW-RSRLAVVSQTPFLFSD-TVA 406
|
....*..
gi 1308832087 97 ENLMLGR 103
Cdd:PRK10789 407 NNIALGR 413
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
25-238 |
8.06e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 46.73 E-value: 8.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 25 EVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDReiqgrrpdkvarmgIARTFQNIELFAHMSTMENLMlgrh 104
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK--------------ISYKPQYIKPDYDGTVEDLLR---- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 105 ryMKTGLFRGAFMWgrrsfagkeevanrkkvEEIIDLLDLQSVRNKFVGGLPYGTQKQVELGRALALEPQLLLLDEPSAG 184
Cdd:PRK13409 423 --SITDDLGSSYYK-----------------SEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAH 483
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1308832087 185 MNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINfGSPIVEGT 238
Cdd:PRK13409 484 LDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMVFE-GEPGKHGH 536
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
6-241 |
1.26e-05 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 45.86 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 6 VEKLSISF-GGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQgRRPDKVARMGIARTF 84
Cdd:PRK10790 343 IDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLS-SLSHSVLRQGVAMVQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 85 QNIELFAHmSTMENLMLGRHrymktglFRGAFMWgrrsfagkeevanrkKVEEIIDLLDLqsvrnkfVGGLPYGT----- 159
Cdd:PRK10790 422 QDPVVLAD-TFLANVTLGRD-------ISEEQVW---------------QALETVQLAEL-------ARSLPDGLytplg 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 160 ---------QKQ-VELGRALALEPQLLLLDEPSAGMNSEEKQdmifwikDIQDTLKV-----TILLIEHDMKMVMDiSDR 224
Cdd:PRK10790 472 eqgnnlsvgQKQlLALARVLVQTPQILILDEATANIDSGTEQ-------AIQQALAAvrehtTLVVIAHRLSTIVE-ADT 543
|
250
....*....|....*..
gi 1308832087 225 VLVINFGSPIVEGTPEE 241
Cdd:PRK10790 544 ILVLHRGQAVEQGTHQQ 560
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-261 |
1.45e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.96 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 26 VQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIvfkdreiqgrrPDKVARMGIARTFQNIELFAHmstMENLMLGRHR 105
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDY-----------EEEPSWDEVLKRFRGTELQNY---FKKLYNGEIK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 106 ------YMKTglfrgafmwGRRSFAGK-----EEVANRKKVEEIIDLLDLQSVRNKFVGGLPYGTQKQVELGRALALEPQ 174
Cdd:PRK13409 162 vvhkpqYVDL---------IPKVFKGKvrellKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDAD 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 175 LLLLDEPSAGMNSEEKQDMIFWIKDIQDtlKVTILLIEHDMkMVMD-ISDrVLVINFGSPIVEGtpeeVQRNP------- 246
Cdd:PRK13409 233 FYFFDEPTSYLDIRQRLNVARLIRELAE--GKYVLVVEHDL-AVLDyLAD-NVHIAYGEPGAYG----VVSKPkgvrvgi 304
|
250
....*....|....*..
gi 1308832087 247 -EVLKAYLGEENA-IRD 261
Cdd:PRK13409 305 nEYLKGYLPEENMrIRP 321
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
19-251 |
1.76e-05 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 45.48 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 19 LSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQG------RRpdKVARMGiartfQNIELFAH 92
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQydhhylHR--QVALVG-----QEPVLFSG 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 93 mSTMENLMLGRHRYMKTGLFRGAFMWGRRSFAGKEEVANRKKVEEiidlldlqsvrnkfVGGLPYGTQKQ-VELGRALAL 171
Cdd:TIGR00958 570 -SVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGE--------------KGSQLSGGQKQrIAIARALVR 634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 172 EPQLLLLDEPSAGMNSEEKQDMIFWiKDIQDTlkvTILLIEHDMKMVMDiSDRVLVINFGSPIVEGTPEEVQRNPEVLKA 251
Cdd:TIGR00958 635 KPRVLILDEATSALDAECEQLLQES-RSRASR---TVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQGCYKH 709
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
19-237 |
1.78e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 45.64 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 19 LSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPS--RGRIVfkdreIQGRRPDKVARMGIARTFQNIELFAHMSTM 96
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTIL-----ANNRKPTKQILKRTGFVTQDDILYPHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 97 ENLMLgrhrymkTGLFRGAfmwgrRSFAGKEEVanrKKVEEIIDLLDLQS-----VRNKFVGGLPYGTQKQVELGRALAL 171
Cdd:PLN03211 159 ETLVF-------CSLLRLP-----KSLTKQEKI---LVAESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLI 223
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1308832087 172 EPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSPIVEG 237
Cdd:PLN03211 224 NPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFG 289
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
5-74 |
2.16e-05 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 44.60 E-value: 2.16e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1308832087 5 KVEKLSIS-FGGLDALSnINFEVQEGqIFSIIGPNGAGKTTLFNCINGIYRPSRGRIV-FKDREIQGRRPDK 74
Cdd:COG3950 2 RIKSLTIEnFRGFEDLE-IDFDNPPR-LTVLVGENGSGKTTLLEAIALALSGLLSRLDdVKFRKLLIRNGEF 71
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
18-236 |
2.33e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.11 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 18 ALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARMGIArtfqnielfahMSTME 97
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHGFA-----------LVTEE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 98 NLMLGRHRYMKTGLfrGAFMWGRRSFAGKEEVANRKKVEE----IIDLLDLQSVRNK-FVGGLPYGTQKQVELGRALALE 172
Cdd:PRK10982 332 RRSTGIYAYLDIGF--NSLISNIRNYKNKVGLLDNSRMKSdtqwVIDSMRVKTPGHRtQIGSLSGGNQQKVIIGRWLLTQ 409
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1308832087 173 PQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKvTILLIEHDMKMVMDISDRVLVINFG--SPIVE 236
Cdd:PRK10982 410 PEILMLDEPTRGIDVGAKFEIYQLIAELAKKDK-GIIIISSEMPELLGITDRILVMSNGlvAGIVD 474
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
13-104 |
2.95e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 44.07 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 13 FGGLDalsninFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIvfkdrEIQGRRPDKVARMG-IARTFQNIELFA 91
Cdd:PRK13543 27 FGPLD------FHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQI-----QIDGKTATRGDRSRfMAYLGHLPGLKA 95
|
90
....*....|....*...
gi 1308832087 92 HMSTMENL-----MLGRH 104
Cdd:PRK13543 96 DLSTLENLhflcgLHGRR 113
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
197-247 |
3.20e-05 |
|
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: 44.68 E-value: 3.20e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1308832087 197 IKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSpIVE-GTPEEVQRNPE 247
Cdd:COG4172 199 LKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGE-IVEqGPTAELFAAPQ 249
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-246 |
3.50e-05 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 44.13 E-value: 3.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 1 MAFFKVEKLSISF----GGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPS----RGRIVFKDRE-----I 67
Cdd:COG4170 1 MPLLDIRNLTIEIdtpqGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtADRFRWNGIDllklsP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 68 QGRRpdKVARMGIARTFQniELFAHMSTMENLMLGRHRYMKTGLFRGAFmWGRRSFagkeevanRKKveEIIDLL----- 142
Cdd:COG4170 81 RERR--KIIGREIAMIFQ--EPSSCLDPSAKIGDQLIEAIPSWTFKGKW-WQRFKW--------RKK--RAIELLhrvgi 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 143 -DLQSVRNKFVGGLPYGTQKQVELGRALALEPQLLLLDEPSAGMNSEeKQDMIFWIKD-IQDTLKVTILLIEHDMKMVMD 220
Cdd:COG4170 146 kDHKDIMNSYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMEST-TQAQIFRLLArLNQLQGTSILLISHDLESISQ 224
|
250 260
....*....|....*....|....*.
gi 1308832087 221 ISDRVLVINFGSPIVEGTPEEVQRNP 246
Cdd:COG4170 225 WADTITVLYCGQTVESGPTEQILKSP 250
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
11-51 |
3.81e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 44.62 E-value: 3.81e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1308832087 11 ISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCING 51
Cdd:PRK10938 268 VSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG 308
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
19-62 |
4.09e-05 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 44.41 E-value: 4.09e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1308832087 19 LSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVF 62
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR 422
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
179-259 |
4.35e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 44.62 E-value: 4.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 179 DEPSAGMNSEEKQDMIFWIKDIQDtLKVTILLIEHDMKMvMDISDRVLVI-----NFGSPIV-EGTPEEVQRNPEVLK-A 251
Cdd:TIGR00630 515 DEPSIGLHQRDNRRLINTLKRLRD-LGNTLIVVEHDEDT-IRAADYVIDIgpgagEHGGEVVaSGTPEEILANPDSLTgQ 592
|
....*...
gi 1308832087 252 YLGEENAI 259
Cdd:TIGR00630 593 YLSGRKKI 600
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
16-217 |
4.98e-05 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 43.23 E-value: 4.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 16 LDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVARM---GIARTFQNIELFAH 92
Cdd:PRK10584 23 LSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLrakHVGFVFQSFMLIPT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 93 MSTMENLMLgrhrymkTGLFRgafmwgrrsfaGKEEVANRKKVEEIIDLLDLQSVRNKFVGGLPYGTQKQVELGRALALE 172
Cdd:PRK10584 103 LNALENVEL-------PALLR-----------GESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1308832087 173 PQLLLLDEPSAGMN---SEEKQDMIFWIKDIQDTlkvTILLIEHDMKM 217
Cdd:PRK10584 165 PDVLFADEPTGNLDrqtGDKIADLLFSLNREHGT---TLILVTHDLQL 209
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-60 |
5.26e-05 |
|
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: 44.52 E-value: 5.26e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1308832087 19 LSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRI 60
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI 483
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
19-60 |
6.01e-05 |
|
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: 43.31 E-value: 6.01e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1308832087 19 LSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRI 60
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI 94
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
5-246 |
9.31e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 43.16 E-value: 9.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISF---GGL--------DALSNINFEVQEGQIFSIIGPNGAGKTT----LFNCINgiyrpSRGRIVFKDREIQG 69
Cdd:PRK15134 277 DVEQLQVAFpirKGIlkrtvdhnVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 70 RRPDKV--ARMGIARTFQ--NIELFAHMSTMENLMLGR--HRYMKTGLFRGAfmwgrRSFAGKEEVAnrkkveeiidlLD 143
Cdd:PRK15134 352 LNRRQLlpVRHRIQVVFQdpNSSLNPRLNVLQIIEEGLrvHQPTLSAAQREQ-----QVIAVMEEVG-----------LD 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 144 LQSvRNKFVGGLPYGTQKQVELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISD 223
Cdd:PRK15134 416 PET-RHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCH 494
|
250 260
....*....|....*....|...
gi 1308832087 224 RVLVINFGSPIVEGTPEEVQRNP 246
Cdd:PRK15134 495 QVIVLRQGEVVEQGDCERVFAAP 517
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
19-254 |
1.06e-04 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 42.51 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 19 LSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPS--------RGRIVFKDREIQGRRPDKVARMGIARTFQNIELF 90
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 91 AhMSTMENLMLGRHRYmktglfrgafmwGRRsfAGKEEVANRKKVEEIIDLLDLQSVRNKFVGGLPYGTQKQVELGRA-- 168
Cdd:PRK13547 97 A-FSAREIVLLGRYPH------------ARR--AGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVla 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 169 -------LALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVINFGSPIVEGTPEE 241
Cdd:PRK13547 162 qlwpphdAAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPAD 241
|
250
....*....|...
gi 1308832087 242 VQRnPEVLKAYLG 254
Cdd:PRK13547 242 VLT-PAHIARCYG 253
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
5-49 |
1.48e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 41.92 E-value: 1.48e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1308832087 5 KVEKLSIS-FGGLDALSNINFEvqeGQIFSIIGPNGAGKTTLFNCI 49
Cdd:COG0419 1 KLLRLRLEnFRSYRDTETIDFD---DGLNLIVGPNGAGKSTILEAI 43
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-245 |
1.65e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 42.66 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 19 LSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREiqgrrpdkVARMGIARTFQNIELFAHMSTmen 98
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCD--------VAKFGLTDLRRVLSIIPQSPV--- 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 99 lmlgrhrymktgLFRGAFMWGRRSF-----AGKEEVANRKKVEEIIDL----LDLQSvrnkFVGGLPY--GTQKQVELGR 167
Cdd:PLN03232 1321 ------------LFSGTVRFNIDPFsehndADLWEALERAHIKDVIDRnpfgLDAEV----SEGGENFsvGQRQLLSLAR 1384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 168 ALALEPQLLLLDEPSAGMNSeeKQDMIfwikdIQDTLK-----VTILLIEHDMKMVMDiSDRVLVINFGSPIVEGTPEEV 242
Cdd:PLN03232 1385 ALLRRSKILVLDEATASVDV--RTDSL-----IQRTIReefksCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQEL 1456
|
...
gi 1308832087 243 QRN 245
Cdd:PLN03232 1457 LSR 1459
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
21-64 |
2.15e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 42.32 E-value: 2.15e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1308832087 21 NINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKD 64
Cdd:PTZ00265 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIND 446
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
18-60 |
2.37e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 41.73 E-value: 2.37e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1308832087 18 ALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRI 60
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV 81
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
21-49 |
2.68e-04 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 40.94 E-value: 2.68e-04
10 20
....*....|....*....|....*....
gi 1308832087 21 NINFEvqeGQIFSIIGPNGAGKTTLFNCI 49
Cdd:pfam13476 13 TIDFS---KGLTLITGPNGSGKTTILDAI 38
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
18-90 |
2.71e-04 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 41.93 E-value: 2.71e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1308832087 18 ALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVaRMGIARTFQNIELF 90
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASL-RNQVALVSQNVHLF 429
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
19-104 |
2.87e-04 |
|
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: 40.99 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 19 LSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVF-----KDREIQGRRpdkvARMGIARtfQNIELFAhM 93
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLdgvdiRDLNLRWLR----SQIGLVS--QEPVLFD-G 91
|
90
....*....|.
gi 1308832087 94 STMENLMLGRH 104
Cdd:cd03249 92 TIAENIRYGKP 102
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
6-228 |
3.49e-04 |
|
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: 40.99 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 6 VEKLSISF--GGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINgiyrpsrgRIVFKDREIQ--GRRPDKVARMGIA 81
Cdd:cd03289 5 VKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFL--------RLLNTEGDIQidGVSWNSVPLQKWR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 82 RTFQNI--ELFAHMSTMENLMLGRHRYMKTGLFRGAfmwgrrsfagkEEVANRKKVEEIIDLLDLQSVRNKFVggLPYGT 159
Cdd:cd03289 77 KAFGVIpqKVFIFSGTFRKNLDPYGKWSDEEIWKVA-----------EEVGLKSVIEQFPGQLDFVLVDGGCV--LSHGH 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1308832087 160 QKQVELGRALALEPQLLLLDEPSAGMNSeekqdmiFWIKDIQDTLK-----VTILLIEHDMKMVMDiSDRVLVI 228
Cdd:cd03289 144 KQLMCLARSVLSKAKILLLDEPSAHLDP-------ITYQVIRKTLKqafadCTVILSEHRIEAMLE-CQRFLVI 209
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
9-158 |
3.65e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 41.65 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 9 LSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRrpDKVARMGIARTFQNIE 88
Cdd:NF033858 272 LTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAG--DIATRRRVGYMSQAFS 349
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1308832087 89 LFAHMSTMENLMLgrH-RymktgLFRgafmwgrrsfAGKEEVANRkkVEEIIDLLDLQSVRNKFVGGLPYG 158
Cdd:NF033858 350 LYGELTVRQNLEL--HaR-----LFH----------LPAAEIAAR--VAEMLERFDLADVADALPDSLPLG 401
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
22-66 |
3.97e-04 |
|
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: 41.27 E-value: 3.97e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1308832087 22 INFEVQEGQIFSIIGPNGAGKTTLFNCINGIYrPSRGRIVFKDRE 66
Cdd:TIGR00954 471 LSFEVPSGNNLLICGPNGCGKSSLFRILGELW-PVYGGRLTKPAK 514
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
6-60 |
4.18e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 41.26 E-value: 4.18e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1308832087 6 VEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRI 60
Cdd:NF033858 4 LEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRV 58
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
26-243 |
4.42e-04 |
|
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: 41.54 E-value: 4.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 26 VQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGrivfkDREIQGrrpdKVARMGIARTFQNIELFAHMSTMENLMLGR-H 104
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSG-----DATVAG----KSILTNISDVHQNMGYCPQFDAIDDLLTGReH 2032
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 105 RYMKTGLfrgafmwgrRSFAGK--EEVANRKkveeiIDLLDLQSVRNKFVGGLPYGTQKQVELGRALALEPQLLLLDEPS 182
Cdd:TIGR01257 2033 LYLYARL---------RGVPAEeiEKVANWS-----IQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPT 2098
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1308832087 183 AGMNSEEKQDMIFWIKDIQDTLKvTILLIEHDMKMVMDISDRVLVINFGSPIVEGTPEEVQ 243
Cdd:TIGR01257 2099 TGMDPQARRMLWNTIVSIIREGR-AVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLK 2158
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
179-238 |
6.29e-04 |
|
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: 39.48 E-value: 6.29e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 179 DEPSAGMNSEEKQDMIFWIKDIQDTLKVTILLIEHDMKMVMDISDRVLVInFGSPIVEGT 238
Cdd:cd03222 96 DEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVF-EGEPGVYGI 154
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
18-194 |
6.47e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 39.85 E-value: 6.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 18 ALSNINFEVQEGQIFS------------IIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIqgrrpDKVARMGIARTFQ 85
Cdd:PRK13541 3 SLHQLQFNIEQKNLFDlsitflpsaityIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNI-----NNIAKPYCTYIGH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 86 NIELFAHMSTMENLMLGRHRYMKTGLFRGAFMWGRrsfagkeevanrkkveeIIDLLDlqsvrnKFVGGLPYGTQKQVEL 165
Cdd:PRK13541 78 NLGLKLEMTVFENLKFWSEIYNSAETLYAAIHYFK-----------------LHDLLD------EKCYSLSSGMQKIVAI 134
|
170 180
....*....|....*....|....*....
gi 1308832087 166 GRALALEPQLLLLDEPSAGMnSEEKQDMI 194
Cdd:PRK13541 135 ARLIACQSDLWLLDEVETNL-SKENRDLL 162
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
6-220 |
6.68e-04 |
|
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: 41.05 E-value: 6.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 6 VEKLSISF--GGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINgiyrpsrgRIVFKDREIQ--GRRPDKVARMGIA 81
Cdd:TIGR01271 1220 VQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL--------RLLSTEGEIQidGVSWNSVTLQTWR 1291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 82 RTFQNI--ELFAHMSTMENLMLGRHRYMKTGLFRGAfmwgrrsfagkEEVANRKKVEEIIDLLDLQSVRNKFVggLPYGT 159
Cdd:TIGR01271 1292 KAFGVIpqKVFIFSGTFRKNLDPYEQWSDEEIWKVA-----------EEVGLKSVIEQFPDKLDFVLVDGGYV--LSNGH 1358
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1308832087 160 QKQVELGRALALEPQLLLLDEPSAGMNSeekqdMIFWIkdIQDTLK-----VTILLIEHDMKMVMD 220
Cdd:TIGR01271 1359 KQLMCLARSILSKAKILLLDEPSAHLDP-----VTLQI--IRKTLKqsfsnCTVILSEHRVEALLE 1417
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
179-231 |
1.02e-03 |
|
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: 38.84 E-value: 1.02e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1308832087 179 DEPSAGMNSEEKQDMIFWIKDIQDtLKVTILLIEHDMKMvMDISDRvlVINFG 231
Cdd:cd03238 114 DEPSTGLHQQDINQLLEVIKGLID-LGNTVILIEHNLDV-LSSADW--IIDFG 162
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
5-239 |
1.10e-03 |
|
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: 39.32 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 5 KVEKLSISFGG--LDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKDREIQGRRPDKVaRMGIAR 82
Cdd:cd03369 8 EVENLSVRYAPdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL-RSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 83 TFQNIELFahMSTMenlmlgrhrymKTGLfrgafmwgrrsfagkeEVANRKKVEEIIDLLDLQSVRNKFVGGlpygtQKQ 162
Cdd:cd03369 87 IPQDPTLF--SGTI-----------RSNL----------------DPFDEYSDEEIYGALRVSEGGLNLSQG-----QRQ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 163 -VELGRALALEPQLLLLDEPSAGMNSEEKQdmifwikDIQDTL-----KVTILLIEHDMKMVMDIsDRVLVINFGSPIVE 236
Cdd:cd03369 133 lLCLARALLKRPRVLVLDEATASIDYATDA-------LIQKTIreeftNSTILTIAHRLRTIIDY-DKILVMDAGEVKEY 204
|
...
gi 1308832087 237 GTP 239
Cdd:cd03369 205 DHP 207
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
6-50 |
1.15e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 39.13 E-value: 1.15e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1308832087 6 VEKLSIS-FGGLDALSNINFEvqEGqIFSIIGPNGAGKTTLFNCIN 50
Cdd:cd03240 1 IDKLSIRnIRSFHERSEIEFF--SP-LTLIVGQNGAGKTTIIEALK 43
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
15-242 |
1.71e-03 |
|
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: 39.54 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 15 GLD-ALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVfkdreIQGRrpdKVARMGIARTFQNIELFAHM 93
Cdd:TIGR00957 1297 DLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEII-----IDGL---NIAKIGLHDLRFKITIIPQD 1368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 94 STmenlmlgrhrymktgLFRGAFMWGRRSFAGKEEvanrkkvEEIIDLLDLQSVRNkFVGGLPYGT-------------- 159
Cdd:TIGR00957 1369 PV---------------LFSGSLRMNLDPFSQYSD-------EEVWWALELAHLKT-FVSALPDKLdhecaeggenlsvg 1425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 160 QKQ-VELGRALALEPQLLLLDEPSAGMNSeEKQDMifwikdIQDTLKV-----TILLIEHDMKMVMDISdRVLVINFGSP 233
Cdd:TIGR00957 1426 QRQlVCLARALLRKTKILVLDEATAAVDL-ETDNL------IQSTIRTqfedcTVLTIAHRLNTIMDYT-RVIVLDKGEV 1497
|
....*....
gi 1308832087 234 IVEGTPEEV 242
Cdd:TIGR00957 1498 AEFGAPSNL 1506
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-214 |
2.04e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 39.16 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 1 MAFFKVEKLSISFGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVF-KD-----------REIQ 68
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYeQDlivarlqqdppRNVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 69 GRRPDKVARmGIARTFQNIELFAHMSTmenlmLGRHRYMKTGLFRGAFMWGRRSFAGKEEVANRkkVEEIIDLLDLQSvr 148
Cdd:PRK11147 81 GTVYDFVAE-GIEEQAEYLKRYHDISH-----LVETDPSEKNLNELAKLQEQLDHHNLWQLENR--INEVLAQLGLDP-- 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1308832087 149 NKFVGGLPYGTQKQVELGRALALEPQLLLLDEPSAGMNSeekqDMIFWIKDIQDTLKVTILLIEHD 214
Cdd:PRK11147 151 DAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDI----ETIEWLEGFLKTFQGSIIFISHD 212
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
5-49 |
2.41e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 38.02 E-value: 2.41e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1308832087 5 KVEKLSI-SFGGLDALSNINFE-VQEGQIFSIIGPNGAGKTTLFNCI 49
Cdd:cd03279 2 KPLKLELkNFGPFREEQVIDFTgLDNNGLFLICGPTGAGKSTILDAI 48
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
19-74 |
2.73e-03 |
|
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: 37.99 E-value: 2.73e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1308832087 19 LSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGiyRPSRGrIVFKDREIQGRRPDK 74
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAG-VITGEILINGRPLDK 75
|
|
| EutP |
COG4917 |
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport ... |
34-57 |
3.85e-03 |
|
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport and metabolism];
Pssm-ID: 443945 [Multi-domain] Cd Length: 145 Bit Score: 36.70 E-value: 3.85e-03
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
19-51 |
4.44e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 38.18 E-value: 4.44e-03
10 20 30
....*....|....*....|....*....|...
gi 1308832087 19 LSNINFEVQEGQIFSIIGPNGAGKTTLFNCING 51
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLG 665
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-64 |
5.04e-03 |
|
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: 36.58 E-value: 5.04e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1308832087 29 GQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFKD 64
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYID 37
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
13-60 |
7.07e-03 |
|
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: 36.86 E-value: 7.07e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1308832087 13 FGGLDALSNINFEVQEGQIFSIIGPNGAGKTTLFNCINGIyRPSRGRI 60
Cdd:cd03233 17 RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR-TEGNVSV 63
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
25-79 |
7.48e-03 |
|
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: 36.40 E-value: 7.48e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1308832087 25 EVQEGQIFSIIGPNGAGKTTLFNCINGIYRPSRGRIVFkDREIQGRRPDKVARMG 79
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW-DGITPVYKPQYIDLSG 74
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-231 |
8.85e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 37.38 E-value: 8.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 1 MAFFKVEKLSISF--GGLD--ALSNINFEVQEGQIFSIIGPNGAGK--TTLfncinGIYR--PS------RGRIVFK--- 63
Cdd:PRK15134 3 QPLLAIENLSVAFrqQQTVrtVVNDVSLQIEAGETLALVGESGSGKsvTAL-----SILRllPSppvvypSGDIRFHges 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 64 -----DREIQGRRPDKvarmgIARTFQniELFAHMSTMENL------MLGRHRYMKTGLFRGafmwgrrsfagkeevanr 132
Cdd:PRK15134 78 llhasEQTLRGVRGNK-----IAMIFQ--EPMVSLNPLHTLekqlyeVLSLHRGMRREAARG------------------ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832087 133 kkveEIIDLLDLQSVR------NKFVGGLPYGTQKQVELGRALALEPQLLLLDEPSAGMNSEEKQDMIFWIKDIQDTLKV 206
Cdd:PRK15134 133 ----EILNCLDRVGIRqaakrlTDYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNM 208
|
250 260
....*....|....*....|....*
gi 1308832087 207 TILLIEHDMKMVMDISDRVLVINFG 231
Cdd:PRK15134 209 GLLFITHNLSIVRKLADRVAVMQNG 233
|
|
| |
