|
Name |
Accession |
Description |
Interval |
E-value |
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
5-258 |
0e+00 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 531.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 5 TTPLLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIARLG 84
Cdd:PRK11300 2 SQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 85 VIRTFQHVRLFKEMTVIENLLVAQHQHLKSGIFSGLLKTPAFRRAESEALDNAVKWLERVDLLPFANRQAGNLAYGQQRR 164
Cdd:PRK11300 82 VVRTFQHVRLFREMTVIENLLVAQHQQLKTGLFSGLLKTPAFRRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 165 LEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPSEI 244
Cdd:PRK11300 162 LEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 241
|
250
....*....|....
gi 490378916 245 RQHPDVIKAYLGEA 258
Cdd:PRK11300 242 RNNPDVIKAYLGEA 255
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
5-259 |
2.01e-145 |
|
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: 407.12 E-value: 2.01e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 5 TTPLLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIARLG 84
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 85 VIRTFQHVRLFKEMTVIENLLVAQHQHLKSGIFSGLLKTPAFRRAESEALDNAVKWLERVDLLPFANRQAGNLAYGQQRR 164
Cdd:COG0411 81 IARTFQNPRLFPELTVLENVLVAAHARLGRGLLAALLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 165 LEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPSEI 244
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEV 240
|
250
....*....|....*
gi 490378916 245 RQHPDVIKAYLGEAY 259
Cdd:COG0411 241 RADPRVIEAYLGEEA 255
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
9-250 |
1.34e-117 |
|
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: 335.95 E-value: 1.34e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIARLGVIRT 88
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 89 FQHVRLFKEMTVIENLLVAQHQHLKSGIFSGllktpAFRRAESEALDNAVKWLERVDLLPFANRQAGNLAYGQQRRLEIA 168
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAQARTGSGLLLA-----RARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 169 RCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRtHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPSEIRQHP 248
Cdd:cd03219 156 RALATDPKLLLLDEPAAGLNPEETEELAELIRELR-ERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNP 234
|
..
gi 490378916 249 DV 250
Cdd:cd03219 235 RV 236
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-257 |
1.86e-76 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 231.93 E-value: 1.86e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 1 MSHITTPLLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAI 80
Cdd:COG4674 3 LDTMHGPILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 81 ARLGVIRTFQHVRLFKEMTVIENLLVAQHQHlkSGIFSGLlktpaFRRAESEALDNAVKWLERVDLLPFANRQAGNLAYG 160
Cdd:COG4674 83 ARLGIGRKFQKPTVFEELTVFENLELALKGD--RGVFASL-----FARLTAEERDRIEEVLETIGLTDKADRLAGLLSHG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 161 QQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHnvSILLIEHDMKLVMGISDRIYVVNQGTPLANGT 240
Cdd:COG4674 156 QKQWLEIGMLLAQDPKLLLLDEPVAGMTDAETERTAELLKSLAGKH--SVVVVEHDMEFVRQIARKVTVLHQGSVLAEGS 233
|
250
....*....|....*..
gi 490378916 241 PSEIRQHPDVIKAYLGE 257
Cdd:COG4674 234 LDEVQADPRVIEVYLGR 250
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
6-256 |
4.92e-64 |
|
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: 199.82 E-value: 4.92e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 6 TPLLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIARLGV 85
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 86 IrtfqHV----RLFKEMTVIENLLVAqhqhlksgifsgllktpAFRRAESEaldnAVKW-LERV-DLLP----FANRQAG 155
Cdd:COG0410 81 G----YVpegrRIFPSLTVEENLLLG-----------------AYARRDRA----EVRAdLERVyELFPrlkeRRRQRAG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 156 NLAYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRThHNVSILLIEHDMKLVMGISDRIYVVNQGTP 235
Cdd:COG0410 136 TLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNR-EGVTILLVEQNARFALEIADRAYVLERGRI 214
|
250 260
....*....|....*....|.
gi 490378916 236 LANGTPSEIRQHPDVIKAYLG 256
Cdd:COG0410 215 VLEGTAAELLADPEVREAYLG 235
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
9-258 |
5.12e-62 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 194.90 E-value: 5.12e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIARLGVIrt 88
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 89 FQHVRLFKEMTVIENLLVAqhqhlksGIFSGLLKTPAFRRAEsealdnavKWLERVDLLPFANRQAGNLAYGQQRRLEIA 168
Cdd:COG1131 79 PQEPALYPDLTVRENLRFF-------ARLYGLPRKEARERID--------ELLELFGLTDAADRKVGTLSGGMKQRLGLA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 169 RCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRtHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPSEIRQHP 248
Cdd:COG1131 144 LALLHDPELLILDEPTSGLDPEARRELWELLRELA-AEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL 222
|
250
....*....|..
gi 490378916 249 --DVIKAYLGEA 258
Cdd:COG1131 223 leDVFLELTGEE 234
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
7-257 |
1.35e-60 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 191.40 E-value: 1.35e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 7 PLLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILyrekhlegLTGQAI------ 80
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIF--------LDGEDIthlpmh 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 81 --ARLGVIRTFQHVRLFKEMTVIENLL-VAQHQHLksgifsgllkTPAFRRAESEALdnavkwLERVDLLPFANRQAGNL 157
Cdd:COG1137 74 krARLGIGYLPQEASIFRKLTVEDNILaVLELRKL----------SKKEREERLEEL------LEEFGITHLRKSKAYSL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 158 AYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRtHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLA 237
Cdd:COG1137 138 SGGERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLK-ERGIGVLITDHNVRETLGICDRAYIISEGKVLA 216
|
250 260
....*....|....*....|
gi 490378916 238 NGTPSEIRQHPDVIKAYLGE 257
Cdd:COG1137 217 EGTPEEILNNPLVRKVYLGE 236
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
9-256 |
1.79e-59 |
|
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: 188.14 E-value: 1.79e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIARLGVIRT 88
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 89 FQHVRLFKEMTVIENLLVAQHQHLKSGifsgllktpAFRRAESEALdnavkwLERVDLLPFANRQAGNLAYGQQRRLEIA 168
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSK---------KEREEKLEEL------LEEFHITHLRKSKASSLSGGERRRVEIA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 169 RCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRThHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPSEIRQHP 248
Cdd:cd03218 146 RALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKD-RGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
....*...
gi 490378916 249 DVIKAYLG 256
Cdd:cd03218 225 LVRKVYLG 232
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
5-255 |
8.97e-59 |
|
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: 186.72 E-value: 8.97e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 5 TTPLLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIARL- 83
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 84 ---GVIrtFQHVRLFKEMTVIENllVA----QHQHLKsgifsgllktpafrraESEALDNAVKWLERVDLLPFANRQAGN 156
Cdd:COG1127 82 rriGML--FQGGALFDSLTVFEN--VAfplrEHTDLS----------------EAEIRELVLEKLELVGLPGAADKMPSE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 157 LAYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPL 236
Cdd:COG1127 142 LSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKII 221
|
250 260
....*....|....*....|
gi 490378916 237 ANGTPSEIRQHPD-VIKAYL 255
Cdd:COG1127 222 AEGTPEELLASDDpWVRQFL 241
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
9-246 |
3.68e-58 |
|
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: 184.56 E-value: 3.68e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIARLGVIRT 88
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 89 FQHVRLFKEMTVIENLLVAqhqhlksgifsgllktpAFRRAESEaldnaVKW-LERV-DLLP----FANRQAGNLAYGQQ 162
Cdd:cd03224 81 PEGRRIFPELTVEENLLLG-----------------AYARRRAK-----RKArLERVyELFPrlkeRRKQLAGTLSGGEQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 163 RRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRtHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPS 242
Cdd:cd03224 139 QMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELR-DEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAA 217
|
....
gi 490378916 243 EIRQ 246
Cdd:cd03224 218 ELLA 221
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
9-249 |
1.64e-56 |
|
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: 180.78 E-value: 1.64e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGqaiARLGVIRT 88
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSE---AELYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 89 -----FQHVRLFKEMTVIENLLVAQHQHlksgifsgllktpaFRRAESEALDNAVKWLERVDLLPFANRQAGNLAYGQQR 163
Cdd:cd03261 78 rmgmlFQSGALFDSLTVFENVAFPLREH--------------TRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 164 RLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPSE 243
Cdd:cd03261 144 RVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEE 223
|
....*.
gi 490378916 244 IRQHPD 249
Cdd:cd03261 224 LRASDD 229
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
8-246 |
1.91e-55 |
|
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: 178.13 E-value: 1.91e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 8 LLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIARLGVIr 87
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 88 tFQHVRLFKEMTVIENLLVAqhqhlksGIFSGLLKTPAFRRAEsealdnavKWLERVDLLPFANRQAGNLAYGQQRRLEI 167
Cdd:COG4555 80 -PDERGLYDRLTVRENIRYF-------AELYGLFDEELKKRIE--------ELIELLGLEEFLDRRVGELSTGMKKKVAL 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490378916 168 ARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRThHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPSEIRQ 246
Cdd:COG4555 144 ARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKK-EGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELRE 221
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
5-254 |
2.52e-54 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 175.28 E-value: 2.52e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 5 TTPLLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLeGLTGQAIA--- 81
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP-RRARRRIGyvp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 82 -RLGVIRTFQhvrlfkeMTVIEnlLVAQHQHLKSGIFSGLlktpafRRAESEALDNAvkwLERVDLLPFANRQAGNLAYG 160
Cdd:COG1121 82 qRAEVDWDFP-------ITVRD--VVLMGRYGRRGLFRRP------SRADREAVDEA---LERVGLEDLADRPIGELSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 161 QQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRtHHNVSILLIEHDMKLVMGISDRIYVVNqGTPLANGT 240
Cdd:COG1121 144 QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELR-REGKTILVVTHDLGAVREYFDRVLLLN-RGLVAHGP 221
|
250
....*....|....
gi 490378916 241 PSEIRQHPDVIKAY 254
Cdd:COG1121 222 PEEVLTPENLSRAY 235
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
9-257 |
5.91e-54 |
|
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: 174.38 E-value: 5.91e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIARLGVIRT 88
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLGIGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 89 FQHVRLFKEMTVIENLL-VAQHQHlksgifsglLKTPAFRRAESEALdnavkwLERVDLLPFANRQAGNLAYGQQRRLEI 167
Cdd:TIGR04406 82 PQEASIFRKLTVEENIMaVLEIRK---------DLDRAEREERLEAL------LEEFQISHLRDNKAMSLSGGERRRVEI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 168 ARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRThHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPSEIRQH 247
Cdd:TIGR04406 147 ARALATNPKFILLDEPFAGVDPIAVGDIKKIIKHLKE-RGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVAN 225
|
250
....*....|
gi 490378916 248 PDVIKAYLGE 257
Cdd:TIGR04406 226 EKVRRVYLGE 235
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
9-253 |
3.39e-52 |
|
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: 169.44 E-value: 3.39e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRF-GGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIARL-GVI 86
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKvGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 87 rtFQHVR--LFkEMTVIENllVAqhqhlksgiFsGLLktpAFRRAESEALDNAVKWLERVDLLPFANRQAGNLAYGQQRR 164
Cdd:COG1122 81 --FQNPDdqLF-APTVEED--VA---------F-GPE---NLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 165 LEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRtHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPSEI 244
Cdd:COG1122 143 VAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLN-KEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
....*....
gi 490378916 245 RQHPDVIKA 253
Cdd:COG1122 222 FSDYELLEE 230
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
9-245 |
2.52e-50 |
|
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: 164.22 E-value: 2.52e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRFGGL--LAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIARLGVI 86
Cdd:cd03263 1 LQIRNLTKTYKKGtkPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 87 rtFQHVRLFKEMTVIENLLvaqhqhlksgiFSGLLKtpAFRRAESEALDNAVkwLERVDLLPFANRQAGNLAYGQQRRLE 166
Cdd:cd03263 81 --PQFDALFDELTVREHLR-----------FYARLK--GLPKSEIKEEVELL--LRVLGLTDKANKRARTLSGGMKRKLS 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490378916 167 IARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHnvSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPSEIR 245
Cdd:cd03263 144 LAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
9-244 |
1.91e-49 |
|
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: 162.74 E-value: 1.91e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRFG-GLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAI----ARL 83
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlrRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 84 GVIrtFQHVRLFKEMTVIENLLV---AQHQHLKSgifsgllktpAFRRAESEALDNAVKWLERVDLLPFANRQAGNLAYG 160
Cdd:cd03256 81 GMI--FQQFNLIERLSVLENVLSgrlGRRSTWRS----------LFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 161 QQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGT 240
Cdd:cd03256 149 QQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGP 228
|
....
gi 490378916 241 PSEI 244
Cdd:cd03256 229 PAEL 232
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
5-248 |
4.13e-48 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 162.57 E-value: 4.13e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 5 TTPLLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILyrekhlegLTGQAIARL- 83
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRIL--------LDGRDVTGLp 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 84 ------GVIrtFQHVRLFKEMTVIENllVAqhqhlksgiFSglLKTPAFRRAESEALdnAVKWLERVDLLPFANRQAGNL 157
Cdd:COG3842 74 pekrnvGMV--FQDYALFPHLTVAEN--VA---------FG--LRMRGVPKAEIRAR--VAELLELVGLEGLADRYPHQL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 158 AYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLA 237
Cdd:COG3842 137 SGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQ 216
|
250
....*....|.
gi 490378916 238 NGTPSEIRQHP 248
Cdd:COG3842 217 VGTPEEIYERP 227
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
7-244 |
8.99e-48 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 158.68 E-value: 8.99e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 7 PLLQVNGLTMRF-GGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAI----A 81
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALrrlrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 82 RLGVIrtFQHVRLFKEMTVIENLLV---AQHqhlksGIFSGLLKtpAFRRAEseaLDNAVKWLERVDLLPFANRQAGNLA 158
Cdd:COG3638 81 RIGMI--FQQFNLVPRLSVLTNVLAgrlGRT-----STWRSLLG--LFPPED---RERALEALERVGLADKAYQRADQLS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 159 YGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLAN 238
Cdd:COG3638 149 GGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFD 228
|
....*.
gi 490378916 239 GTPSEI 244
Cdd:COG3638 229 GPPAEL 234
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
9-245 |
1.26e-47 |
|
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: 157.53 E-value: 1.26e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGtilyrEKHLEGL-----TGQAIARL 83
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSG-----RATVAGHdvvrePREVRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 84 GVIrtFQHVRLFKEMTVIENLLvaqhqhlksgIFSGLLKTPAFRRAEsealdNAVKWLERVDLLPFANRQAGNLAYGQQR 163
Cdd:cd03265 76 GIV--FQDLSVDDELTGWENLY----------IHARLYGVPGAERRE-----RIDELLDFVGLLEAADRLVKTYSGGMRR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 164 RLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPSE 243
Cdd:cd03265 139 RLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
..
gi 490378916 244 IR 245
Cdd:cd03265 219 LK 220
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
9-233 |
2.54e-47 |
|
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: 154.86 E-value: 2.54e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIARLGVIrt 88
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 89 FQHVRLFKEMTVIENLlvaqhqhlksgIFSGllktpafrraesealdnavkwlervdllpfanrqagnlayGQQRRLEIA 168
Cdd:cd03230 79 PEEPSLYENLTVRENL-----------KLSG----------------------------------------GMKQRLALA 107
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490378916 169 RCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRtHHNVSILLIEHDMKLVMGISDRIYVVNQG 233
Cdd:cd03230 108 QALLHDPELLILDEPTSGLDPESRREFWELLRELK-KEGKTILLSSHILEEAERLCDRVAILNNG 171
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-248 |
4.72e-47 |
|
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: 163.54 E-value: 4.72e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 5 TTPLLQVNGLTMRF-----GGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQA 79
Cdd:COG1123 257 AEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRS 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 80 IARL----GVIrtFQHVR--LFKEMTVIENLLVAQHQHlksGIFSGllktpAFRRAESEALdnavkwLERVDLLP-FANR 152
Cdd:COG1123 337 LRELrrrvQMV--FQDPYssLNPRMTVGDIIAEPLRLH---GLLSR-----AERRERVAEL------LERVGLPPdLADR 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 153 QAGNLAYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQ 232
Cdd:COG1123 401 YPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYD 480
|
250
....*....|....*.
gi 490378916 233 GTPLANGTPSEIRQHP 248
Cdd:COG1123 481 GRIVEDGPTEEVFANP 496
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
10-233 |
7.74e-47 |
|
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: 155.00 E-value: 7.74e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 10 QVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEgLTGQAIA----RLGV 85
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE-KERKRIGyvpqRRSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 86 IRTFqhvrlfkEMTVIEnlLVAqhqhlkSGIFSGLLKTPAFRRAESEALDNAvkwLERVDLLPFANRQAGNLAYGQQRRL 165
Cdd:cd03235 80 DRDF-------PISVRD--VVL------MGLYGHKGLFRRLSKADKAKVDEA---LERVGLSELADRQIGELSGGQQQRV 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490378916 166 EIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRtHHNVSILLIEHDMKLVMGISDRIYVVNQG 233
Cdd:cd03235 142 LLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELR-REGMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
8-244 |
1.57e-46 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 155.59 E-value: 1.57e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 8 LLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIAR-LGVI 86
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARrIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 87 rtFQHVRLFKEMTVIENLLVAQHQHLKsgifsgllktpAFRRaESEALDNAVKW-LERVDLLPFANRQAGNLAYGQQRRL 165
Cdd:COG1120 81 --PQEPPAPFGLTVRELVALGRYPHLG-----------LFGR-PSAEDREAVEEaLERTGLEHLADRPVDELSGGERQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490378916 166 EIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPSEI 244
Cdd:COG1120 147 LIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
5-229 |
7.66e-46 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 159.80 E-value: 7.66e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 5 TTPLLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIARLG 84
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 85 VIRTFQHVRLFKEMTVIENLLVAQHQHLKsgifsGLLKTPAFRRAesealdnAVKWLERVDL-LPfANRQAGNLAYGQQR 163
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENIFLGREPRRG-----GLIDWRAMRRR-------ARELLARLGLdID-PDTPVGDLSVAQQQ 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490378916 164 RLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRThHNVSILLIEHDMKLVMGISDRIYV 229
Cdd:COG1129 148 LVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKA-QGVAIIYISHRLDEVFEIADRVTV 212
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
5-233 |
1.05e-45 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 159.81 E-value: 1.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 5 TTPLLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILY--REKHLEGlTGQAIAr 82
Cdd:COG3845 2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIdgKPVRIRS-PRDAIA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 83 LGVIRTFQHVRLFKEMTVIENLLVaqhqhlksgifsGLLKTPAFRRAESEALDNAVKWLER----VDLlpfaNRQAGNLA 158
Cdd:COG3845 80 LGIGMVHQHFMLVPNLTVAENIVL------------GLEPTKGGRLDRKAARARIRELSERygldVDP----DAKVEDLS 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490378916 159 YGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETndlDDLIAELR--THHNVSILLIEHDMKLVMGISDRIYVVNQG 233
Cdd:COG3845 144 VGEQQRVEILKALYRGARILILDEPTAVLTPQEA---DELFEILRrlAAEGKSIIFITHKLREVMAIADRVTVLRRG 217
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
9-229 |
3.71e-45 |
|
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: 151.09 E-value: 3.71e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRFGG----LLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTgqaiARLG 84
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG----PDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 85 VIrtFQHVRLFKEMTVIENLLVAqhqhLKsgifsgllktpAFRRAESEALDNAVKWLERVDLLPFANRQAGNLAYGQQRR 164
Cdd:cd03293 77 YV--FQQDALLPWLTVLDNVALG----LE-----------LQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQR 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490378916 165 LEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYV 229
Cdd:cd03293 140 VALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVV 204
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
9-239 |
1.49e-44 |
|
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: 149.21 E-value: 1.49e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILyrekhlegLTGQAIARLGVIRT 88
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEIL--------IDGRDVTGVPPERR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 89 -----FQHVRLFKEMTVIENLLvaqhqhlkSGIFSGLLKTPAFRRAESEALdnavkwlERVDLLPFANRQAGNLAYGQQR 163
Cdd:cd03259 73 nigmvFQDYALFPHLTVAENIA--------FGLKLRGVPKAEIRARVRELL-------ELVGLEGLLNRYPHELSGGQQQ 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490378916 164 RLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANG 239
Cdd:cd03259 138 RVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-229 |
1.92e-44 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 150.24 E-value: 1.92e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 1 MSHiTTPLLQVNGLTMRF----GGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLT 76
Cdd:COG1116 1 MSA-AAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 77 gqaiARLGVIrtFQHVRLFKEMTVIENLLVAqhqhLKsgiFSGLLKTPAFRRAEsealdnavKWLERVDLLPFANRQAGN 156
Cdd:COG1116 80 ----PDRGVV--FQEPALLPWLTVLDNVALG----LE---LRGVPKAERRERAR--------ELLELVGLAGFEDAYPHQ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490378916 157 LAYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMK--LVMgiSDRIYV 229
Cdd:COG1116 139 LSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDeaVFL--ADRVVV 211
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
8-248 |
5.10e-44 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 148.60 E-value: 5.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 8 LLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLeGLTGQAIARlgvIR 87
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDINK---LR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 88 T-----FQHVRLFKEMTVIENLLVAQHQHLKsgifsgllktpafrRAESEALDNAVKWLERVDLLPFANRQAGNLAYGQQ 162
Cdd:COG1126 77 RkvgmvFQQFNLFPHLTVLENVTLAPIKVKK--------------MSKAEAEERAMELLERVGLADKADAYPAQLSGGQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 163 RRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRtHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPS 242
Cdd:COG1126 143 QRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLA-KEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPE 221
|
....*.
gi 490378916 243 EIRQHP 248
Cdd:COG1126 222 EFFENP 227
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
9-246 |
6.35e-44 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 150.26 E-value: 6.35e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIARL----G 84
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRIGYLpeerG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 85 virtfqhvrLFKEMTVIENLL-VAQhqhLKsgifsGLLKtpafrraeSEALDNAVKWLERVDLLPFANRQAGNLAYGQQR 163
Cdd:COG4152 82 ---------LYPKMKVGEQLVyLAR---LK-----GLSK--------AEAKRRADEWLERLGLGDRANKKVEELSKGNQQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 164 RLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRtHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPSE 243
Cdd:COG4152 137 KVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELA-AKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDE 215
|
...
gi 490378916 244 IRQ 246
Cdd:COG4152 216 IRR 218
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
8-247 |
6.65e-44 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 148.60 E-value: 6.65e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 8 LLQVNGLTMRFG-GLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAI----AR 82
Cdd:TIGR02315 1 MLEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLrklrRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 83 LGVIrtFQHVRLFKEMTVIENLL---VAQHQHLKSGIFSgllktpaFRRAESE-ALDNavkwLERVDLLPFANRQAGNLA 158
Cdd:TIGR02315 81 IGMI--FQHYNLIERLTVLENVLhgrLGYKPTWRSLLGR-------FSEEDKErALSA----LERVGLADKAYQRADQLS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 159 YGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLAN 238
Cdd:TIGR02315 148 GGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFD 227
|
....*....
gi 490378916 239 GTPSEIRQH 247
Cdd:TIGR02315 228 GAPSELDDE 236
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
10-234 |
1.12e-43 |
|
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: 146.84 E-value: 1.12e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 10 QVNGLTMRFGGL--LAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIARL-GVI 86
Cdd:cd03225 1 ELKNLSFSYPDGarPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKvGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 87 rtFQHVR--LFKEmTVIENLlvaqhqhlksgIFS-GLLKTPafrraESEALDNAVKWLERVDLLPFANRQAGNLAYGQQR 163
Cdd:cd03225 81 --FQNPDdqFFGP-TVEEEV-----------AFGlENLGLP-----EEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490378916 164 RLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRtHHNVSILLIEHDMKLVMGISDRIYVVNQGT 234
Cdd:cd03225 142 RVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLK-AEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
24-185 |
1.74e-43 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 144.33 E-value: 1.74e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 24 VNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAI-ARLGVIrtFQHVRLFKEMTVIE 102
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLrKEIGYV--FQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 103 NLLVAQHqhlksgiFSGLLKTPAFRRAEsealdnavKWLERVDLLPFANR----QAGNLAYGQQRRLEIARCMVTRPEIL 178
Cdd:pfam00005 79 NLRLGLL-------LKGLSKREKDARAE--------EALEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLL 143
|
....*..
gi 490378916 179 MLDEPAA 185
Cdd:pfam00005 144 LLDEPTA 150
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
9-233 |
2.43e-43 |
|
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: 146.10 E-value: 2.43e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRFGG----LLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIARL- 83
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 84 ----GVIrtFQHVRLFKEMTVIENLLVAQHqhlksgiFSGLLKTPAFRRAEsealdnavKWLERVDLLPFANRQAGNLAY 159
Cdd:cd03255 81 rrhiGFV--FQSFNLLPDLTALENVELPLL-------LAGVPKKERRERAE--------ELLERVGLGDRLNHYPSELSG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490378916 160 GQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVmGISDRIYVVNQG 233
Cdd:cd03255 144 GQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDG 216
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
9-234 |
4.55e-43 |
|
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: 144.25 E-value: 4.55e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIA---RLGV 85
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPlrrRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 86 IrtFQHVRLFKEMTVIENLLVAqhqhlksgiFSGllktpafrraesealdnavkwlervdllpfanrqagnlayGQQRRL 165
Cdd:cd03229 81 V--FQDFALFPHLTVLENIALG---------LSG----------------------------------------GQQQRV 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490378916 166 EIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGT 234
Cdd:cd03229 110 ALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
9-248 |
7.61e-43 |
|
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: 145.46 E-value: 7.61e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLtgqAIARLGVIRT 88
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNL---PPHKRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 89 FQHVRLFKEMTVIENLLVAqhqhlksgifsglLKTPAFRRAESEAldnAVKW-LERVDLLPFANRQAGNLAYGQQRRLEI 167
Cdd:cd03300 78 FQNYALFPHLTVFENIAFG-------------LRLKKLPKAEIKE---RVAEaLDLVQLEGYANRKPSQLSGGQQQRVAI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 168 ARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPSEIRQH 247
Cdd:cd03300 142 ARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEE 221
|
.
gi 490378916 248 P 248
Cdd:cd03300 222 P 222
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
6-233 |
7.90e-43 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 145.19 E-value: 7.90e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 6 TPLLQVNGLTMRFG----GLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIA 81
Cdd:COG1136 2 SPLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 82 RL-----GVIrtFQHVRLFKEMTVIENLLVAQhqhlksgIFSGLLKTPAFRRAEsealdnavKWLERVDLLPFANRQAGN 156
Cdd:COG1136 82 RLrrrhiGFV--FQFFNLLPELTALENVALPL-------LLAGVSRKERRERAR--------ELLERVGLGDRLDHRPSQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490378916 157 LAYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLvMGISDRIYVVNQG 233
Cdd:COG1136 145 LSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPEL-AARADRVIRLRDG 220
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
9-248 |
8.87e-43 |
|
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: 145.56 E-value: 8.87e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYrekHLEGLTGQAIARLGVIRT 88
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILF---GGEDATDVPVQERNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 89 FQHVRLFKEMTVIENllVAqhqhlksgiFsGLLKTPAFRRAESEALDNAVK-WLERVDLLPFANRQAGNLAYGQQRRLEI 167
Cdd:cd03296 80 FQHYALFRHMTVFDN--VA---------F-GLRVKPRSERPPEAEIRAKVHeLLKLVQLDWLADRYPAQLSGGQRQRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 168 ARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPSEIRQH 247
Cdd:cd03296 148 ARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDH 227
|
.
gi 490378916 248 P 248
Cdd:cd03296 228 P 228
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
9-248 |
3.40e-42 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 146.83 E-value: 3.40e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLegLTGQAIARLGVIRT 88
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL--FTNLPPRERRVGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 89 FQHVRLFKEMTVIENllVAqhqhlksgiFsGLlktPAFRRAESEALDNAVKWLERVDLLPFANRQAGNLAYGQQRRLEIA 168
Cdd:COG1118 81 FQHYALFPHMTVAEN--IA---------F-GL---RVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 169 RCMVTRPEILMLDEPAAGLNPKETNDLDDliaELRTHH---NVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPSEIR 245
Cdd:COG1118 146 RALAVEPEVLLLDEPFGALDAKVRKELRR---WLRRLHdelGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVY 222
|
...
gi 490378916 246 QHP 248
Cdd:COG1118 223 DRP 225
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
9-233 |
2.84e-41 |
|
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: 140.74 E-value: 2.84e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGlTGQAIARL--GVI 86
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELrqKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 87 RTFQHVRLFKEMTVIENLLVAQHQHLKsgifsgllktpafrRAESEALDNAVKWLERVDLLPFANRQAGNLAYGQQRRLE 166
Cdd:cd03262 80 MVFQQFNLFPHLTVLENITLAPIKVKG--------------MSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490378916 167 IARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELrTHHNVSILLIEHDMKLVMGISDRIYVVNQG 233
Cdd:cd03262 146 IARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDL-AEEGMTMVVVTHEMGFAREVADRVIFMDDG 211
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
9-255 |
1.92e-40 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 139.20 E-value: 1.92e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIARLGVIRT 88
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 89 FQHVRLFKEMTVIENLLVaqhqhlksgifsGLlktPAFRRAESEALDnavkwlERVDLLP----FANRQAGNLAYGQQRR 164
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLT------------GL---AALPRRSRKIPD------EIYELFPvlkeMLGRRGGDLSGGQQQQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 165 LEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPSEI 244
Cdd:TIGR03410 140 LAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
250
....*....|.
gi 490378916 245 RQhpDVIKAYL 255
Cdd:TIGR03410 220 DE--DKVRRYL 228
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
10-239 |
1.27e-39 |
|
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: 135.64 E-value: 1.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 10 QVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIAR-LGVirt 88
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARkIAY--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 89 fqhvrlfkemtvienllVAQhqhlksgifsgllktpafrraesealdnavkWLERVDLLPFANRQAGNLAYGQQRRLEIA 168
Cdd:cd03214 78 -----------------VPQ-------------------------------ALELLGLAHLADRPFNELSGGERQRVLLA 109
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490378916 169 RCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANG 239
Cdd:cd03214 110 RALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
9-239 |
2.99e-39 |
|
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: 135.49 E-value: 2.99e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIARLGVIRT 88
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIGYLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 89 fqhvrLFKEMTVIENLL-VAQhqhLKsgifsGLLKTPAFRRAESealdnavkWLERVDLLPFANRQAGNLAYGQQRRLEI 167
Cdd:cd03269 81 -----LYPKMKVIDQLVyLAQ---LK-----GLKKEEARRRIDE--------WLERLELSEYANKRVEELSKGNQQKVQF 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490378916 168 ARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRThHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANG 239
Cdd:cd03269 140 IAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELAR-AGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
23-254 |
6.57e-39 |
|
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: 136.43 E-value: 6.57e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 23 AVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIARL----GVIrtFQ---HvRLF 95
Cdd:TIGR04521 20 ALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLrkkvGLV--FQfpeH-QLF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 96 KEmTVIE-------NLlvaqhqhlksgifsGLlktpafrrAESEALDNAVKWLERVDLLP-FANRQAGNLAYGQQRRLEI 167
Cdd:TIGR04521 97 EE-TVYKdiafgpkNL--------------GL--------SEEEAEERVKEALELVGLDEeYLERSPFELSGGQMRRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 168 ARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPSEIRQH 247
Cdd:TIGR04521 154 AGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSD 233
|
....*..
gi 490378916 248 PDVIKAY 254
Cdd:TIGR04521 234 VDELEKI 240
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
9-244 |
1.16e-38 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 134.62 E-value: 1.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYK-----PTSGTILYREKHLEGLTGQAIA-- 81
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDVLElr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 82 -RLGVIrtFQHVRLFkEMTVIENLLVAQHQHlksgifsgllktpafRRAESEALDNAVKW-LERVDLLPFANRQ--AGNL 157
Cdd:cd03260 81 rRVGMV--FQKPNPF-PGSIYDNVAYGLRLH---------------GIKLKEELDERVEEaLRKAALWDEVKDRlhALGL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 158 AYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRthHNVSILLIEHDMKLVMGISDRIYVVNQGTPLA 237
Cdd:cd03260 143 SGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELK--KEYTIVIVTHNMQQAARVADRTAFLLNGRLVE 220
|
....*..
gi 490378916 238 NGTPSEI 244
Cdd:cd03260 221 FGPTEQI 227
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
7-205 |
1.52e-38 |
|
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: 133.37 E-value: 1.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 7 PLLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIARLGVI 86
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 87 rtFQHVRLFKEMTVIENLLVAQHQHlksgifsGLlktpafrRAESEALDNAvkwLERVDLLPFANRQAGNLAYGQQRRLE 166
Cdd:COG4133 81 --GHADGLKPELTVRENLRFWAALY-------GL-------RADREAIDEA---LEAVGLAGLADLPVRQLSAGQKRRVA 141
|
170 180 190
....*....|....*....|....*....|....*....
gi 490378916 167 IARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTH 205
Cdd:COG4133 142 LARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLAR 180
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-248 |
1.86e-38 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 138.04 E-value: 1.86e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 3 HITTPLLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILyrekhlegLTGQAIAR 82
Cdd:PRK11607 14 KALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIM--------LDGVDLSH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 83 LGVIR-----TFQHVRLFKEMTVIENLLVAQHQHlksgifsgllktpafRRAESEALDNAVKWLERVDLLPFANRQAGNL 157
Cdd:PRK11607 86 VPPYQrpinmMFQSYALFPHMTVEQNIAFGLKQD---------------KLPKAEIASRVNEMLGLVHMQEFAKRKPHQL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 158 AYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLA 237
Cdd:PRK11607 151 SGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQ 230
|
250
....*....|.
gi 490378916 238 NGTPSEIRQHP 248
Cdd:PRK11607 231 IGEPEEIYEHP 241
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
7-249 |
2.70e-38 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 137.09 E-value: 2.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 7 PLLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILyrekhlegLTGQAIARL--- 83
Cdd:TIGR03265 3 PYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIY--------QGGRDITRLppq 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 84 ----GVIrtFQHVRLFKEMTVIENllvaqhqhlksgIFSGLLKTpafRRAESEALDNAVKWLERVDLLPFANRQAGNLAY 159
Cdd:TIGR03265 75 krdyGIV--FQSYALFPNLTVADN------------IAYGLKNR---GMGRAEVAERVAELLDLVGLPGSERKYPGQLSG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 160 GQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANG 239
Cdd:TIGR03265 138 GQQQRVALARALATSPGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVG 217
|
250
....*....|
gi 490378916 240 TPSEIRQHPD 249
Cdd:TIGR03265 218 TPQEIYRHPA 227
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
8-243 |
7.05e-38 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 133.32 E-value: 7.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 8 LLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIAR-LGVI 86
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARrRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 87 RtfQHVRL---FkemTVIEnlLVAQhqhlksgifsGLLKTPAFRRAESEALDNAvkwLERVDLLPFANRQAGNLAYGQQR 163
Cdd:COG4559 81 P--QHSSLafpF---TVEE--VVAL----------GRAPHGSSAAQDRQIVREA---LALVGLAHLAGRSYQTLSGGEQQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 164 RLEIARCMV-------TRPEILMLDEPAAGLNPKETNDLDDLIAELrTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPL 236
Cdd:COG4559 141 RVQLARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQL-ARRGGGVVAVLHDLNLAAQYADRILLLHQGRLV 219
|
....*..
gi 490378916 237 ANGTPSE 243
Cdd:COG4559 220 AQGTPEE 226
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
8-259 |
1.16e-37 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 132.32 E-value: 1.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 8 LLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIARLGVIR 87
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 88 TFQHVRLFKEMTVIENLLvaqhqhlksgifsGLLKTPAFRRAESEAlDNAVKWLERVDLLPFANRQAGNLAYGQQRRLEI 167
Cdd:PRK10895 83 LPQEASIFRRLSVYDNLM-------------AVLQIRDDLSAEQRE-DRANELMEEFHIEHLRDSMGQSLSGGERRRVEI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 168 ARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRThHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPSEIRQH 247
Cdd:PRK10895 149 ARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRD-SGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQD 227
|
250
....*....|..
gi 490378916 248 PDVIKAYLGEAY 259
Cdd:PRK10895 228 EHVKRVYLGEDF 239
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
9-239 |
1.36e-37 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 131.19 E-value: 1.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLeGLTGQAIARLGVIRT 88
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY-QKNIEALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 89 FQHvrLFKEMTVIENLLVAQHQHLksgifsgllktpaFRRAESEALdnavkwLERVDLLPFANRQAGNLAYGQQRRLEIA 168
Cdd:cd03268 80 APG--FYPNLTARENLRLLARLLG-------------IRKKRIDEV------LDVVGLKDSAKKKVKGFSLGMKQRLGIA 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490378916 169 RCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRThHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANG 239
Cdd:cd03268 139 LALLGNPDLLILDEPTNGLDPDGIKELRELILSLRD-QGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
9-257 |
1.96e-37 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 131.42 E-value: 1.96e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRFGGLLAvnNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREkhlEGLTGQAIARLGVIRT 88
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNG---QDLTALPPAERPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 89 FQHVRLFKEMTVIENLLVAQHQHLKsgifsgllktpaFRRAESEALDNAvkwLERVDLLPFANRQAGNLAYGQQRRLEIA 168
Cdd:COG3840 77 FQENNLFPHLTVAQNIGLGLRPGLK------------LTAEQRAQVEQA---LERVGLAGLLDRLPGQLSGGQRQRVALA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 169 RCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPSEI--RQ 246
Cdd:COG3840 142 RCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALldGE 221
|
250
....*....|.
gi 490378916 247 HPDVIKAYLGE 257
Cdd:COG3840 222 PPPALAAYLGI 232
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
6-215 |
3.53e-37 |
|
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: 131.36 E-value: 3.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 6 TPLLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSG---TILYREKHLEGLtgQAI-A 81
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLFGERRGGEDV--WELrK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 82 RLGVIRTFQHVRLFKEMTVIENLLvaqhqhlkSGIFS--GLlktpaFRRAESEALDNAVKWLERVDLLPFANRQAGNLAY 159
Cdd:COG1119 79 RIGLVSPALQLRFPRDETVLDVVL--------SGFFDsiGL-----YREPTDEQRERARELLELLGLAHLADRPFGTLSQ 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490378916 160 GQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEH 215
Cdd:COG1119 146 GEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTH 201
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
23-248 |
1.31e-36 |
|
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: 129.24 E-value: 1.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 23 AVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTG----QAIARLGVIrtFQHVRLFKEM 98
Cdd:cd03258 20 ALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGkelrKARRRIGMI--FQHFNLLSSR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 99 TVIENLLVAqhqhLKsgifsgLLKTP-AFRRAESEALdnavkwLERVDLLPFANRQAGNLAYGQQRRLEIARCMVTRPEI 177
Cdd:cd03258 98 TVFENVALP----LE------IAGVPkAEIEERVLEL------LELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490378916 178 LMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPSEIRQHP 248
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-253 |
1.74e-36 |
|
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: 135.03 E-value: 1.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 6 TPLLQVNGLTMRF--GGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPT---SGTILYREKHLEGLTGQAI 80
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 81 AR-LGVIrtFQHVrlfkeMTVIENLLVAQHqhlksgIFSGLLktpAFRRAESEALDNAVKWLERVDLLPFANRQAGNLAY 159
Cdd:COG1123 82 GRrIGMV--FQDP-----MTQLNPVTVGDQ------IAEALE---NLGLSRAEARARVLELLEAVGLERRLDRYPHQLSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 160 GQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANG 239
Cdd:COG1123 146 GQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDG 225
|
250
....*....|....
gi 490378916 240 TPSEIRQHPDVIKA 253
Cdd:COG1123 226 PPEEILAAPQALAA 239
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
8-233 |
1.94e-36 |
|
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: 128.78 E-value: 1.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 8 LLQVNGLTMRF----GGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIARL 83
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 84 GviRTFQHVrlFKE--------MTVIENLLVAQHQHLKsgifsgLLKTPAFRRAESEAldnavkwLERVDLLP-FANRQA 154
Cdd:cd03257 81 R--KEIQMV--FQDpmsslnprMTIGEQIAEPLRIHGK------LSKKEARKEAVLLL-------LVGVGLPEeVLNRYP 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490378916 155 GNLAYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQG 233
Cdd:cd03257 144 HELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAG 222
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
7-243 |
6.21e-36 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 128.35 E-value: 6.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 7 PLLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIA-RLGV 85
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELArRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 86 IRtfQHVRLFKEMTVIEnlLVAQhqhlksgifsGLLKTPAFRRAESEALDNAvkwLERVDLLPFANRQAGNLAYGQQRRL 165
Cdd:PRK13548 81 LP--QHSSLSFPFTVEE--VVAM----------GRAPHGLSRAEDDALVAAA---LAQVDLAHLAGRDYPQLSGGEQQRV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 166 EIARCMV------TRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANG 239
Cdd:PRK13548 144 QLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADG 223
|
....
gi 490378916 240 TPSE 243
Cdd:PRK13548 224 TPAE 227
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
9-258 |
1.63e-35 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 129.45 E-value: 1.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREkhlEGLTGQAIARLGVIRT 88
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDG---EDVTHRSIQQRDICMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 89 FQHVRLFKEMTVIENllvaqhqhlksgIFSGL--LKTPAFRRAE--SEALdnavkwlERVDLLPFANRQAGNLAYGQQRR 164
Cdd:PRK11432 84 FQSYALFPHMSLGEN------------VGYGLkmLGVPKEERKQrvKEAL-------ELVDLAGFEDRYVDQISGGQQQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 165 LEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPSEI 244
Cdd:PRK11432 145 VALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
250
....*....|....*.
gi 490378916 245 RQHPD--VIKAYLGEA 258
Cdd:PRK11432 225 YRQPAsrFMASFMGDA 240
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
9-234 |
1.71e-35 |
|
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: 124.46 E-value: 1.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIARLGvIRT 88
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAG-IAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 89 FqhvrlfkemtvienllvaqHQhlksgifsgllktpafrraesealdnavkwlervdllpfanrqagnLAYGQQRRLEIA 168
Cdd:cd03216 80 V-------------------YQ----------------------------------------------LSVGERQMVEIA 94
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490378916 169 RCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRThHNVSILLIEHDMKLVMGISDRIYVVNQGT 234
Cdd:cd03216 95 RALARNARLLILDEPTAALTPAEVERLFKVIRRLRA-QGVAVIFISHRLDEVFEIADRVTVLRDGR 159
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
5-256 |
2.35e-35 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 131.83 E-value: 2.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 5 TTPLLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIARLG 84
Cdd:PRK09700 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 85 VIRTFQHVRLFKEMTVIENLLVAQHQHLKsgIFSGLLKTPAFRRAESEALdnavkwLERVDLLPFANRQAGNLAYGQQRR 164
Cdd:PRK09700 82 IGIIYQELSVIDELTVLENLYIGRHLTKK--VCGVNIIDWREMRVRAAMM------LLRVGLKVDLDEKVANLSISHKQM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 165 LEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRThHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPSEI 244
Cdd:PRK09700 154 LEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRK-EGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
250
....*....|..
gi 490378916 245 rQHPDVIKAYLG 256
Cdd:PRK09700 233 -SNDDIVRLMVG 243
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
9-233 |
3.71e-35 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 125.16 E-value: 3.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRF-GGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIA----RL 83
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPylrrRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 84 GVIrtFQHVRLFKEMTVIENLLVAQHqhlksgifsgllktpAFRRAESEALDNAVKWLERVDLLPFANRQAGNLAYGQQR 163
Cdd:COG2884 82 GVV--FQDFRLLPDRTVYENVALPLR---------------VTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 164 RLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRtHHNVSILLIEHDMKLVMGISDRIYVVNQG 233
Cdd:COG2884 145 RVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEIN-RRGTTVLIATHDLELVDRMPKRVLELEDG 213
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
17-248 |
4.58e-35 |
|
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: 126.22 E-value: 4.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 17 RFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILyrekhlegLTGQAIA-----RLGVIR---- 87
Cdd:cd03294 33 KTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVL--------IDGQDIAamsrkELRELRrkki 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 88 --TFQHVRLFKEMTVIENL---LVAQHQhlksgifsgllktpafrrAESEALDNAVKWLERVDLLPFANRQAGNLAYGQQ 162
Cdd:cd03294 105 smVFQSFALLPHRTVLENVafgLEVQGV------------------PRAEREERAAEALELVGLEGWEHKYPDELSGGMQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 163 RRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPS 242
Cdd:cd03294 167 QRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPE 246
|
....*.
gi 490378916 243 EIRQHP 248
Cdd:cd03294 247 EILTNP 252
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
5-248 |
1.40e-34 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 127.76 E-value: 1.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 5 TTPLLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILyrekhlegLTGQAIARL- 83
Cdd:PRK09452 11 LSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIM--------LDGQDITHVp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 84 ----GVIRTFQHVRLFKEMTVIENllVAQHQHLKsgifsgllKTPA--FRRAESEAldnavkwLERVDLLPFANRQAGNL 157
Cdd:PRK09452 83 aenrHVNTVFQSYALFPHMTVFEN--VAFGLRMQ--------KTPAaeITPRVMEA-------LRMVQLEEFAQRKPHQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 158 AYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLA 237
Cdd:PRK09452 146 SGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQ 225
|
250
....*....|.
gi 490378916 238 NGTPSEIRQHP 248
Cdd:PRK09452 226 DGTPREIYEEP 236
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
7-256 |
2.22e-34 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 123.84 E-value: 2.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 7 PLLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIARLGVI 86
Cdd:PRK11614 4 VMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 87 RTFQHVRLFKEMTVIENLLVAqhqhlksGIFsgllktpafrrAESEALDNAVKWLerVDLLP--FANR--QAGNLAYGQQ 162
Cdd:PRK11614 84 IVPEGRRVFSRMTVEENLAMG-------GFF-----------AERDQFQERIKWV--YELFPrlHERRiqRAGTMSGGEQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 163 RRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRtHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPS 242
Cdd:PRK11614 144 QMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLR-EQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGD 222
|
250
....*....|....
gi 490378916 243 EIRQHPDVIKAYLG 256
Cdd:PRK11614 223 ALLANEAVRSAYLG 236
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
5-237 |
2.55e-34 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 128.89 E-value: 2.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 5 TTPLLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYkPT---SGTILYREKHLEGLTGQAIA 81
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIRDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 82 RLGVIRTFQHVRLFKEMTVIENllvaqhqhlksgIFSGLLKTPAFRRAESEALDNAVKWLERVDLLPFANRQAGNLAYGQ 161
Cdd:PRK13549 81 RAGIAIIHQELALVKELSVLEN------------IFLGNEITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490378916 162 QRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRtHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLA 237
Cdd:PRK13549 149 QQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLK-AHGIACIYISHKLNEVKAISDTICVIRDGRHIG 223
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
9-233 |
2.65e-34 |
|
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: 122.69 E-value: 2.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRFGGLLAVNNVELTINQGeIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIARLGVIRt 88
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLP- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 89 fQHVRLFKEMTVIEnllvaqhqHLKsgiFSGLLKTPAFRRAESEAlDNAvkwLERVDLLPFANRQAGNLAYGQQRRLEIA 168
Cdd:cd03264 79 -QEFGVYPNFTVRE--------FLD---YIAWLKGIPSKEVKARV-DEV---LELVNLGDRAKKKIGSLSGGMRRRVGIA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490378916 169 RCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRThhNVSILLIEHDMKLVMGISDRIYVVNQG 233
Cdd:cd03264 143 QALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKG 205
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
5-248 |
3.13e-34 |
|
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: 129.50 E-value: 3.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 5 TTPLLQVNGLTMRF--GGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAI-A 81
Cdd:COG4987 330 GGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLrR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 82 RLGVIrtFQHVRLFkEMTVIENLLVAQHQhlksgifsgllktpafrrAESEALDNAvkwLERVDLLPFANRQAGNLAY-- 159
Cdd:COG4987 410 RIAVV--PQRPHLF-DTTLRENLRLARPD------------------ATDEELWAA---LERVGLGDWLAALPDGLDTwl 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 160 ---------GQQRRLEIARCMVTRPEILMLDEPAAGLNPkETNdlDDLIAELRTH-HNVSILLIEHDMkLVMGISDRIYV 229
Cdd:COG4987 466 geggrrlsgGERRRLALARALLRDAPILLLDEPTEGLDA-ATE--QALLADLLEAlAGRTVLLITHRL-AGLERMDRILV 541
|
250
....*....|....*....
gi 490378916 230 VNQGTPLANGTPSEIRQHP 248
Cdd:COG4987 542 LEDGRIVEQGTHEELLAQN 560
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
9-248 |
5.54e-34 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 125.58 E-value: 5.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTIlyrekhleGLTGQAIARLG---- 84
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHI--------RFHGTDVSRLHardr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 85 -VIRTFQHVRLFKEMTVIENllvaqhqhlksgIFSGLLKTPAFRRAESEALDNAV-KWLERVDLLPFANRQAGNLAYGQQ 162
Cdd:PRK10851 75 kVGFVFQHYALFRHMTVFDN------------IAFGLTVLPRRERPNAAAIKAKVtQLLEMVQLAHLADRYPAQLSGGQK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 163 RRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPS 242
Cdd:PRK10851 143 QRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPD 222
|
....*.
gi 490378916 243 EIRQHP 248
Cdd:PRK10851 223 QVWREP 228
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
9-248 |
8.55e-34 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 124.80 E-value: 8.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLeglTGQAIARLGVIRT 88
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV---TDLPPKDRNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 89 FQHVRLFKEMTVIENLlvaqhqhlksgifsgllktpAF----RRAESEALDNAVKW-LERVDLLPFANRQAGNLAYGQQR 163
Cdd:COG3839 81 FQSYALYPHMTVYENI--------------------AFplklRKVPKAEIDRRVREaAELLGLEDLLDRKPKQLSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 164 RLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPSE 243
Cdd:COG3839 141 RVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEE 220
|
....*
gi 490378916 244 IRQHP 248
Cdd:COG3839 221 LYDRP 225
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
8-256 |
9.45e-34 |
|
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: 127.25 E-value: 9.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 8 LLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYK--PTSGTILYREKHLEGLTGQAIARLGV 85
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 86 IRTFQHVRLFKEMTVIENLLVAQHQHLKSGIFSGLLKTpafRRAesEALDNAVkwleRVDLLPFAnRQAGNLAYGQQRRL 165
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGNEITLPGGRMAYNAMY---LRA--KNLLREL----QLDADNVT-RPVGDYGGGQQQLV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 166 EIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRThHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANgTPSEIR 245
Cdd:TIGR02633 151 EIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKA-HGVACVYISHKLNEVKAVCDTICVIRDGQHVAT-KDMSTM 228
|
250
....*....|.
gi 490378916 246 QHPDVIKAYLG 256
Cdd:TIGR02633 229 SEDDIITMMVG 239
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
8-248 |
1.16e-33 |
|
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: 122.22 E-value: 1.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 8 LLQVNGLTMRFG----GLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIARl 83
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 84 GVIRTFQHVR--LFKEMTVIEnllvaqhqhlksgifsgLLKTP--AFRRAESEAldNAVKWLERVDLLP-FANRQAGNLA 158
Cdd:COG1124 80 RVQMVFQDPYasLHPRHTVDR-----------------ILAEPlrIHGLPDREE--RIAELLEQVGLPPsFLDRYPHQLS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 159 YGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLAN 238
Cdd:COG1124 141 GGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEE 220
|
250
....*....|
gi 490378916 239 GTPSEIRQHP 248
Cdd:COG1124 221 LTVADLLAGP 230
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
19-248 |
1.73e-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: 124.58 E-value: 1.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 19 GGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREkhlEGLTGQAIARLGVIR------TFQHV 92
Cdd:TIGR01186 4 GGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDG---ENIMKQSPVELREVRrkkigmVFQQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 93 RLFKEMTVIENLLVAQHqhlksgifsgLLKTPAFRRAEsealdNAVKWLERVDLLPFANRQAGNLAYGQQRRLEIARCMV 172
Cdd:TIGR01186 81 ALFPHMTILQNTSLGPE----------LLGWPEQERKE-----KALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490378916 173 TRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPSEIRQHP 248
Cdd:TIGR01186 146 AEPDILLMDEAFSALDPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNP 221
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
7-247 |
5.30e-33 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 126.03 E-value: 5.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 7 PLLQVNGLTMRF-GGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAI-ARLG 84
Cdd:COG4988 335 PSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWrRQIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 85 VIRtfQHVRLFKeMTVIENLLVAQHQhlksgifsgllktpafrrAESEALDNAvkwLERVDLLPFANR-----------Q 153
Cdd:COG4988 415 WVP--QNPYLFA-GTIRENLRLGRPD------------------ASDEELEAA---LEAAGLDEFVAAlpdgldtplgeG 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 154 AGNLAYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVsiLLIEHDMKLVMgISDRIYVVNQG 233
Cdd:COG4988 471 GRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTV--ILITHRLALLA-QADRILVLDDG 547
|
250
....*....|....
gi 490378916 234 TPLANGTPSEIRQH 247
Cdd:COG4988 548 RIVEQGTHEELLAK 561
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
14-257 |
7.74e-33 |
|
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: 119.71 E-value: 7.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 14 LTMRFGGL-LAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYRekhlegltGQAIARLGVIR----- 87
Cdd:cd03295 6 VTKRYGGGkKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFID--------GEDIREQDPVElrrki 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 88 --TFQHVRLFKEMTVIENLlvaqhqhlksGIFSGLLKTPAFRRAEsealdNAVKWLERVDLLP--FANRQAGNLAYGQQR 163
Cdd:cd03295 78 gyVIQQIGLFPHMTVEENI----------ALVPKLLKWPKEKIRE-----RADELLALVGLDPaeFADRYPHELSGGQQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 164 RLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPSE 243
Cdd:cd03295 143 RVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDE 222
|
250
....*....|....*.
gi 490378916 244 I--RQHPDVIKAYLGE 257
Cdd:cd03295 223 IlrSPANDFVAEFVGA 238
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
10-234 |
1.09e-32 |
|
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: 116.96 E-value: 1.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 10 QVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYRekhlegltGQAIARLGVIRTF 89
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILID--------GKDIAKLPLEELR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 90 QHVrlfkemtvienLLVAQhqhlksgiFSGllktpafrraesealdnavkwlervdllpfanrqagnlayGQQRRLEIAR 169
Cdd:cd00267 73 RRI-----------GYVPQ--------LSG----------------------------------------GQRQRVALAR 93
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490378916 170 CMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRThHNVSILLIEHDMKLVMGISDRIYVVNQGT 234
Cdd:cd00267 94 ALLLNPDLLLLDEPTSGLDPASRERLLELLRELAE-EGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
22-253 |
3.05e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 119.35 E-value: 3.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 22 LAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILY---------REKHLEGLTgqaiARLGVIRTFQHV 92
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitagkKNKKLKPLR----KKVGIVFQFPEH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 93 RLFKEmTVienllvaqhqhLKSGIFSGLlktpAFRRAESEALDNAVKWLERV----DLL---PFAnrqagnLAYGQQRRL 165
Cdd:PRK13634 97 QLFEE-TV-----------EKDICFGPM----NFGVSEEDAKQKAREMIELVglpeELLarsPFE------LSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 166 EIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPSEIR 245
Cdd:PRK13634 155 AIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIF 234
|
....*...
gi 490378916 246 QHPDVIKA 253
Cdd:PRK13634 235 ADPDELEA 242
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
23-233 |
8.81e-32 |
|
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: 114.79 E-value: 8.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 23 AVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAI-ARLGVIrtFQHVRLFKeMTVI 101
Cdd:cd03228 17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLrKNIAYV--PQDPFLFS-GTIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 102 ENLLvaqhqhlkSGifsgllktpafrraesealdnavkwlervdllpfanrqagnlayGQQRRLEIARCMVTRPEILMLD 181
Cdd:cd03228 94 ENIL--------SG--------------------------------------------GQRQRIAIARALLRDPPILILD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490378916 182 EPAAGLNPKETNDLDDLIAELRthHNVSILLIEHDMKLVMgISDRIYVVNQG 233
Cdd:cd03228 122 EATSALDPETEALILEALRALA--KGKTVIVIAHRLSTIR-DADRIIVLDDG 170
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
9-248 |
1.24e-31 |
|
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: 116.67 E-value: 1.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTmRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQaiaRLGVIRT 88
Cdd:cd03299 1 LKVENLS-KDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE---KRDISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 89 FQHVRLFKEMTVIENllvaqhqhlksgIFSGLLKTPAFRRAESEALDNAVKWLERVDLLpfaNRQAGNLAYGQQRRLEIA 168
Cdd:cd03299 77 PQNYALFPHMTVYKN------------IAYGLKKRKVDKKEIERKVLEIAEMLGIDHLL---NRKPETLSGGEQQRVAIA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 169 RCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPSEIRQHP 248
Cdd:cd03299 142 RALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKP 221
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
23-244 |
3.05e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 116.69 E-value: 3.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 23 AVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILyrekhlegLTGQAIARLGVirTFQHVRlfKEMTvie 102
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKII--------IDGVDITDKKV--KLSDIR--KKVG--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 103 nlLVAQ---HQHLKSGIFSGLLKTPAFRRAESEALDNAVK-WLERV--DLLPFANRQAGNLAYGQQRRLEIARCMVTRPE 176
Cdd:PRK13637 87 --LVFQypeYQLFEETIEKDIAFGPINLGLSEEEIENRVKrAMNIVglDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490378916 177 ILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPSEI 244
Cdd:PRK13637 165 ILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREV 232
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
9-247 |
3.06e-31 |
|
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: 121.48 E-value: 3.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRFGGL--LAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILY-----REKHLEGLTGQaia 81
Cdd:COG2274 474 IELENVSFRYPGDspPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIdgidlRQIDPASLRRQ--- 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 82 rLGVIrtFQHVRLFkEMTVIENLLVAQHQhlksgifsgllktpafrrAESEALDNAvkwLERVDLLPFANR--------- 152
Cdd:COG2274 551 -IGVV--LQDVFLF-SGTIRENITLGDPD------------------ATDEEIIEA---ARLAGLHDFIEAlpmgydtvv 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 153 --QAGNLAYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRthHNVSILLIEHDMKLVMgISDRIYVV 230
Cdd:COG2274 606 geGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLL--KGRTVIIIAHRLSTIR-LADRIIVL 682
|
250
....*....|....*..
gi 490378916 231 NQGTPLANGTPSEIRQH 247
Cdd:COG2274 683 DKGRIVEDGTHEELLAR 699
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-254 |
4.07e-31 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 116.83 E-value: 4.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 5 TTPLLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIARLG 84
Cdd:PRK13537 4 SVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 85 VIRTFQHvrLFKEMTVIENLLVAqhqhlksGIFSGLlkTPAFRRAESEALdnavkwLERVDLLPFANRQAGNLAYGQQRR 164
Cdd:PRK13537 84 VVPQFDN--LDPDFTVRENLLVF-------GRYFGL--SAAAARALVPPL------LEFAKLENKADAKVGELSGGMKRR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 165 LEIARCMVTRPEILMLDEPAAGLNPKETN----DLDDLIAELRThhnvsILLIEHDMKLVMGISDRIYVVNQGTPLANGT 240
Cdd:PRK13537 147 LTLARALVNDPDVLVLDEPTTGLDPQARHlmweRLRSLLARGKT-----ILLTTHFMEEAERLCDRLCVIEEGRKIAEGA 221
|
250
....*....|....*..
gi 490378916 241 PSEIRQHP---DVIKAY 254
Cdd:PRK13537 222 PHALIESEigcDVIEIY 238
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
9-248 |
4.74e-31 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 117.49 E-value: 4.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRF----GGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAI--AR 82
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELraAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 83 --LGVIrtFQHVRLFKEMTVIEN----LLVAqhqhlksgifsGLLKtpAFRRAESEALdnavkwLERVDLLPFANRQAGN 156
Cdd:COG1135 82 rkIGMI--FQHFNLLSSRTVAENvalpLEIA-----------GVPK--AEIRKRVAEL------LELVGLSDKADAYPSQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 157 LAYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPL 236
Cdd:COG1135 141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIV 220
|
250
....*....|..
gi 490378916 237 ANGTPSEIRQHP 248
Cdd:COG1135 221 EQGPVLDVFANP 232
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
8-239 |
2.26e-30 |
|
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: 112.85 E-value: 2.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 8 LLQVNGLTMRF----GGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILyrekhLEGLTG-----Q 78
Cdd:cd03266 1 MITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFAT-----VDGFDVvkepaE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 79 AIARLGVIrtFQHVRLFKEMTVIENLlvaqhqhlksGIFSGLLktpAFRRAESEAldnAVKWL-ERVDLLPFANRQAGNL 157
Cdd:cd03266 76 ARRRLGFV--SDSTGLYDRLTARENL----------EYFAGLY---GLKGDELTA---RLEELaDRLGMEELLDRRVGGF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 158 AYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNvSILLIEHDMKLVMGISDRIYVVNQGTPLA 237
Cdd:cd03266 138 STGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGK-CILFSTHIMQEVERLCDRVVVLHRGRVVY 216
|
..
gi 490378916 238 NG 239
Cdd:cd03266 217 EG 218
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
20-252 |
3.35e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 113.63 E-value: 3.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 20 GLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAI-ARLGVIRTFQHV--RLFK 96
Cdd:PRK13639 14 GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLeVRKTVGIVFQNPddQLFA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 97 EmTVIENllVAqhqhlksgiFSGL-LKTPafrraeSEALDNAVK-WLERVDLLPFANRQAGNLAYGQQRRLEIARCMVTR 174
Cdd:PRK13639 94 P-TVEED--VA---------FGPLnLGLS------KEEVEKRVKeALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490378916 175 PEILMLDEPAAGLNPKETNDLDDLIAELrTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPSEIRQHPDVIK 252
Cdd:PRK13639 156 PEIIVLDEPTSGLDPMGASQIMKLLYDL-NKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETIR 232
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
13-257 |
7.26e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 113.39 E-value: 7.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 13 GLTMRFGGLlavNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTG-QAIARL----GVIR 87
Cdd:PRK13641 15 GTPMEKKGL---DNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGnKNLKKLrkkvSLVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 88 TFQHVRLFKEmTVIENLLVAQHQhlksgifsgllktpaFRRAESEALDNAVKWLERVDLLP-FANRQAGNLAYGQQRRLE 166
Cdd:PRK13641 92 QFPEAQLFEN-TVLKDVEFGPKN---------------FGFSEDEAKEKALKWLKKVGLSEdLISKSPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 167 IARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAEL-RTHHNVsiLLIEHDMKLVMGISDRIYVVNQGTPLANGTPSEIR 245
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYqKAGHTV--ILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIF 233
|
250
....*....|...
gi 490378916 246 QHPD-VIKAYLGE 257
Cdd:PRK13641 234 SDKEwLKKHYLDE 246
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
23-239 |
8.52e-30 |
|
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: 111.66 E-value: 8.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 23 AVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILY--------REKHLegltgqaiARLGVIRTfQHVRL 94
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVaglvpwkrRKKFL--------RRIGVVFG-QKTQL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 95 FKEMTVIENLLVAQHqhlksgifsgllktpAFRRAESEALDNAVKWLERVDLLPFANRQAGNLAYGQQRRLEIARCMVTR 174
Cdd:cd03267 107 WWDLPVIDSFYLLAA---------------IYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490378916 175 PEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANG 239
Cdd:cd03267 172 PEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-249 |
1.63e-29 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 111.43 E-value: 1.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 1 MSHITTPLLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILY----------REK 70
Cdd:COG4598 1 MTDTAPPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVggeeirlkpdRDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 71 HLEGLTGQAIARlgvIRT-----FQHVRLFKEMTVIENLLVAQHQHLKsgifsgllktpafrRAESEALDNAVKWLERVD 145
Cdd:COG4598 81 ELVPADRRQLQR---IRTrlgmvFQSFNLWSHMTVLENVIEAPVHVLG--------------RPKAEAIERAEALLAKVG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 146 LLPFANRQAGNLAYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETND----LDDLIAELRThhnvsILLIEHDMKLVM 221
Cdd:COG4598 144 LADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEvlkvMRDLAEEGRT-----MLVVTHEMGFAR 218
|
250 260
....*....|....*....|....*...
gi 490378916 222 GISDRIYVVNQGTPLANGTPSEIRQHPD 249
Cdd:COG4598 219 DVSSHVVFLHQGRIEEQGPPAEVFGNPK 246
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
2-249 |
1.65e-29 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 111.78 E-value: 1.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 2 SHITTPLLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAI- 80
Cdd:PRK11831 1 EQSVANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 81 -ARLGVIRTFQHVRLFKEMTVIENLL--VAQHQHLKSGifsgLLKTPAFRRAESEALDNAVKwlervdLLPfanrqaGNL 157
Cdd:PRK11831 81 tVRKRMSMLFQSGALFTDMNVFDNVAypLREHTQLPAP----LLHSTVMMKLEAVGLRGAAK------LMP------SEL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 158 AYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLA 237
Cdd:PRK11831 145 SGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVA 224
|
250
....*....|..
gi 490378916 238 NGTPSEIRQHPD 249
Cdd:PRK11831 225 HGSAQALQANPD 236
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
8-252 |
2.98e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 111.48 E-value: 2.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 8 LLQVNGLTMRFG-GLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEgltgqaIARLGVI 86
Cdd:PRK13636 5 ILKVEELNYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID------YSRKGLM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 87 RTFQHVRLFKEMTVIENLLVAQHQHLKSGIFSglLKTPafrraESEALDNAVKWLERVDLLPFANRQAGNLAYGQQRRLE 166
Cdd:PRK13636 79 KLRESVGMVFQDPDNQLFSASVYQDVSFGAVN--LKLP-----EDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 167 IARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPSEIRQ 246
Cdd:PRK13636 152 IAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFA 231
|
....*.
gi 490378916 247 HPDVIK 252
Cdd:PRK13636 232 EKEMLR 237
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
7-216 |
3.78e-29 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 110.72 E-value: 3.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 7 PLLQVNGLTMRFGG----LLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILyrekhlegLTGQAI-- 80
Cdd:COG4525 2 SMLTVRHVSVRYPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEIT--------LDGVPVtg 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 81 --ARLGVIrtFQHVRLFKEMTVIENllVAqhqhlksgiFSglLKTPAFRRAESEALdnAVKWLERVDLLPFANRQAGNLA 158
Cdd:COG4525 74 pgADRGVV--FQKDALLPWLNVLDN--VA---------FG--LRLRGVPKAERRAR--AEELLALVGLADFARRRIWQLS 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490378916 159 YGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHD 216
Cdd:COG4525 137 GGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS 194
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
7-258 |
1.11e-28 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 112.24 E-value: 1.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 7 PLLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIARLgVI 86
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRR-VA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 87 RTFQHVRLFKEMTVIENLLVAQHQHLksGIFSGLlkTPAFRRAESEAldnavkwLERVDLLPFANRQAGNLAYGQQRRLE 166
Cdd:PRK09536 81 SVPQDTSLSFEFDVRQVVEMGRTPHR--SRFDTW--TETDRAAVERA-------MERTGVAQFADRPVTSLSGGERQRVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 167 IARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIeHDMKLVMGISDRIYVVNQGTPLANGTPSEIRQ 246
Cdd:PRK09536 150 LARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLADGRVRAAGPPADVLT 228
|
250
....*....|..
gi 490378916 247 HPDVIKAYLGEA 258
Cdd:PRK09536 229 ADTLRAAFDART 240
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
8-229 |
2.60e-28 |
|
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: 109.76 E-value: 2.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 8 LLQVNGLTMRF----GGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKP---TSGTILYREKHLEGLTGQAI 80
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 81 ARL-GviRTFQHVrlFKE--------MTV----IENLLVaqHQHLKsgifsgllktpafrraESEALDNAVKWLERVDLl 147
Cdd:COG0444 81 RKIrG--REIQMI--FQDpmtslnpvMTVgdqiAEPLRI--HGGLS----------------KAEARERAIELLERVGL- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 148 PFANRQAGnlAY------GQQRRLEIARCMVTRPEILMLDEPAAGLnpketndlD--------DLIAELRTHHNVSILLI 213
Cdd:COG0444 138 PDPERRLD--RYphelsgGMRQRVMIARALALEPKLLIADEPTTAL--------DvtiqaqilNLLKDLQRELGLAILFI 207
|
250
....*....|....*.
gi 490378916 214 EHDMKLVMGISDRIYV 229
Cdd:COG0444 208 THDLGVVAEIADRVAV 223
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
24-246 |
2.66e-28 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 107.55 E-value: 2.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 24 VNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILyrekhlegLTGQAIARLGVIR--TFQHVRLFKEMTVI 101
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVI--------LEGKQITEPGPDRmvVFQNYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 102 ENLLVAQHQHLksgifsgllktPAFRRAESEALDNavKWLERVDLLPFANRQAGNLAYGQQRRLEIARCMVTRPEILMLD 181
Cdd:TIGR01184 73 ENIALAVDRVL-----------PDLSKSERRAIVE--EHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLD 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490378916 182 EPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVvnqgtpLANGTPSEIRQ 246
Cdd:TIGR01184 140 EPFGALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVM------LTNGPAANIGQ 198
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
29-239 |
4.16e-28 |
|
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: 106.81 E-value: 4.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 29 LTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLeglTGQAIARLGVIRTFQHVRLFKEMTVIENLlvaq 108
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV---TAAPPADRPVSMLFQENNLFAHLTVEQNV---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 109 hqhlksgifsGLLKTPAFR-RAES-EALDNAvkwLERVDLLPFANRQAGNLAYGQQRRLEIARCMVTRPEILMLDEPAAG 186
Cdd:cd03298 92 ----------GLGLSPGLKlTAEDrQAIEVA---LARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490378916 187 LNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANG 239
Cdd:cd03298 159 LDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
28-233 |
4.56e-28 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 106.48 E-value: 4.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 28 ELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLeglTGQAIARLGVIRTFQHVRLFKEMTVIENLLVA 107
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSH---TGLAPYQRPVSMLFQENNLFAHLTVRQNIGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 108 QHQHLKsgiFSGLLKTPAFRRAESEALDNavkWLERvdlLPfanrqaGNLAYGQQRRLEIARCMVTRPEILMLDEPAAGL 187
Cdd:TIGR01277 95 LHPGLK---LNAEQQEKVVDAAQQVGIAD---YLDR---LP------EQLSGGQRQRVALARCLVRPNPILLLDEPFSAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490378916 188 NPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQG 233
Cdd:TIGR01277 160 DPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQG 205
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
39-257 |
5.81e-28 |
|
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: 109.12 E-value: 5.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 39 LIGPNGAGKTTIFNCLTGFYKPTSGTILYREkhlEGLTGQAIARLGVIRTFQHVRLFKEMTVIENLLVAqhqhlksgifs 118
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDG---EDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFG----------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 119 glLKTPAFRRAESEALDNAVkwLERVDLLPFANRQAGNLAYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKetndLDDL 198
Cdd:TIGR01187 67 --LKMRKVPRAEIKPRVLEA--LRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKK----LRDQ 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490378916 199 IA-ELRT-HHNVSI--LLIEHDMKLVMGISDRIYVVNQGTPLANGTPSEIRQHPD--VIKAYLGE 257
Cdd:TIGR01187 139 MQlELKTiQEQLGItfVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPAnlFVARFIGE 203
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
9-202 |
5.82e-28 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 107.02 E-value: 5.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGT--ILYREKHLEGLTG-QAIARL-- 83
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTlnIAGNHFDFSKTPSdKAIRELrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 84 GVIRTFQHVRLFKEMTVIENLLVAQHQHLksgifsGLlktpafrrAESEALDNAVKWLERVDLLPFANRQAGNLAYGQQR 163
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNLIEAPCRVL------GL--------SKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQ 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 490378916 164 RLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAEL 202
Cdd:PRK11124 149 RVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIREL 187
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
5-229 |
6.44e-28 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 108.67 E-value: 6.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 5 TTPLLQVNGLTMRF---GGLL--------AVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLE 73
Cdd:COG4608 4 AEPLLEVRDLKKHFpvrGGLFgrtvgvvkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDIT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 74 GLTGQAIARLGviRTFQHVrlFKE--------MTV---IENLLVAQHqhlksgifsglLKTPAFRRAESEALdnavkwLE 142
Cdd:COG4608 84 GLSGRELRPLR--RRMQMV--FQDpyaslnprMTVgdiIAEPLRIHG-----------LASKAERRERVAEL------LE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 143 RVDLLP-FANRQAGNLAYGQQRRLEIARCMVTRPEILMLDEP-AAglnpketndLD--------DLIAELRTHHNVSILL 212
Cdd:COG4608 143 LVGLRPeHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPvSA---------LDvsiqaqvlNLLEDLQDELGLTYLF 213
|
250
....*....|....*..
gi 490378916 213 IEHDMKLVMGISDRIYV 229
Cdd:COG4608 214 ISHDLSVVRHISDRVAV 230
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
9-248 |
1.03e-27 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 106.98 E-value: 1.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGL---TGQAIA---- 81
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkDGQLKVadkn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 82 RLGVIRT-----FQHVRLFKEMTVIENLLVAQHQHLksgifsGLLKtpafrraeSEALDNAVKWLERVDLLPFAN-RQAG 155
Cdd:PRK10619 86 QLRLLRTrltmvFQHFNLWSHMTVLENVMEAPIQVL------GLSK--------QEARERAVKYLAKVGIDERAQgKYPV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 156 NLAYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELrTHHNVSILLIEHDMKLVMGISDRIYVVNQGTP 235
Cdd:PRK10619 152 HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQL-AEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
250
....*....|...
gi 490378916 236 LANGTPSEIRQHP 248
Cdd:PRK10619 231 EEEGAPEQLFGNP 243
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
9-233 |
1.06e-27 |
|
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: 105.41 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLtgQAIARlGVIRT 88
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDL--PPKDR-DIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 89 FQHVRLFKEMTVIENLLVAqhqhLKSgifsgllktpafRRAESEALDNAVKWLERV----DLLpfaNRQAGNLAYGQQRR 164
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFG----LKL------------RKVPKDEIDERVREVAELlqieHLL---DRKPKQLSGGQRQR 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490378916 165 LEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQG 233
Cdd:cd03301 139 VALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDG 207
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
15-248 |
1.77e-27 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 105.56 E-value: 1.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 15 TMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILyrekhLEGLT---GQAIARLgvIR---- 87
Cdd:PRK09493 8 SKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLI-----VDGLKvndPKVDERL--IRqeag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 88 -TFQHVRLFKEMTVIENLLVaqhqhlksgifsGLLKTPAFRRAESEALdnAVKWLERVDLLPFANRQAGNLAYGQQRRLE 166
Cdd:PRK09493 81 mVFQQFYLFPHLTALENVMF------------GPLRVRGASKEEAEKQ--ARELLAKVGLAERAHHYPSELSGGQQQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 167 IARCMVTRPEILMLDEPAAGLNPketndlddliaELRthHNV------------SILLIEHDMKLVMGISDRIYVVNQGT 234
Cdd:PRK09493 147 IARALAVKPKLMLFDEPTSALDP-----------ELR--HEVlkvmqdlaeegmTMVIVTHEIGFAEKVASRLIFIDKGR 213
|
250
....*....|....
gi 490378916 235 PLANGTPSEIRQHP 248
Cdd:PRK09493 214 IAEDGDPQVLIKNP 227
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
23-247 |
2.12e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 107.48 E-value: 2.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 23 AVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILY--------REKHLegltgqaiARLGVI---RTfqh 91
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVlgyvpfkrRKEFA--------RRIGVVfgqRS--- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 92 vRLFKEMTVIENLLVAQHqhlksgIFSglLKTPAFRraesEALDNAVkwlERVDLLPFANRQAGNLAYGQQRRLEIARCM 171
Cdd:COG4586 106 -QLWWDLPAIDSFRLLKA------IYR--IPDAEYK----KRLDELV---ELLDLGELLDTPVRQLSLGQRMRCELAAAL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490378916 172 VTRPEILMLDEPAAGL--NPKETndLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPSEIRQH 247
Cdd:COG4586 170 LHRPKILFLDEPTIGLdvVSKEA--IREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKER 245
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
5-250 |
2.15e-27 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 109.62 E-value: 2.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 5 TTPLLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLE-GLTGQAIARl 83
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALAA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 84 GVIRTFQHVRLFKEMTVIENLLVAQHQHlKSGIF-SGLLKTPAfrRAESEALDnavkwlerVDLLPfaNRQAGNLAYGQQ 162
Cdd:PRK11288 80 GVAIIYQELHLVPEMTVAENLYLGQLPH-KGGIVnRRLLNYEA--REQLEHLG--------VDIDP--DTPLKYLSIGQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 163 RRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVsILLIEHDMKLVMGISDRIYVVNQGTplangtps 242
Cdd:PRK11288 147 QMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRV-ILYVSHRMEEIFALCDAITVFKDGR-------- 217
|
....*...
gi 490378916 243 EIRQHPDV 250
Cdd:PRK11288 218 YVATFDDM 225
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
3-233 |
2.30e-27 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 105.78 E-value: 2.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 3 HITTPLLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKH-----LEGLtG 77
Cdd:PRK11701 1 MMDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlrdLYAL-S 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 78 QAIARL------GVIRtfQHVRLFKEMTVI------ENLLVAQHQHlksgifsgllktpaFRRAESEALDnavkWLERVD 145
Cdd:PRK11701 80 EAERRRllrtewGFVH--QHPRDGLRMQVSaggnigERLMAVGARH--------------YGDIRATAGD----WLERVE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 146 LLPfaNR---QAGNLAYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMG 222
Cdd:PRK11701 140 IDA--ARiddLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARL 217
|
250
....*....|.
gi 490378916 223 ISDRIYVVNQG 233
Cdd:PRK11701 218 LAHRLLVMKQG 228
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
9-248 |
2.36e-27 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 105.48 E-value: 2.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHL---EGLTGQAIARL-- 83
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIRLLrq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 84 GVIRTFQHVRLFKEMTVIENLLVAQHQHLksgifsGLLKtpafrraeSEALDNAVKWLERVDLLPFANRQAGNLAYGQQR 163
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENLIEAPCKVL------GLSK--------EQAREKAMKLLARLRLTDKADRFPLHLSGGQQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 164 RLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELrTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTpSE 243
Cdd:COG4161 149 RVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIREL-SQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-AS 226
|
....*
gi 490378916 244 IRQHP 248
Cdd:COG4161 227 HFTQP 231
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-257 |
2.83e-27 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 107.22 E-value: 2.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 4 ITTPLLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIARL 83
Cdd:PRK13536 37 MSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 84 GVIRTFQhvRLFKEMTVIENLLV-----AQHQHLKSGIFSGLLKtpaFRRAESEaldnavkwlervdllpfANRQAGNLA 158
Cdd:PRK13536 117 GVVPQFD--NLDLEFTVRENLLVfgryfGMSTREIEAVIPSLLE---FARLESK-----------------ADARVSDLS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 159 YGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETN----DLDDLIAELRThhnvsILLIEHDMKLVMGISDRIYVVNQGT 234
Cdd:PRK13536 175 GGMKRRLTLARALINDPQLLILDEPTTGLDPHARHliweRLRSLLARGKT-----ILLTTHFMEEAERLCDRLCVLEAGR 249
|
250 260
....*....|....*....|....*.
gi 490378916 235 PLANGTPSE-IRQHP--DVIKAYLGE 257
Cdd:PRK13536 250 KIAEGRPHAlIDEHIgcQVIEIYGGD 275
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-248 |
5.26e-27 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 104.83 E-value: 5.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 1 MSHITtpllqVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEG---LTG 77
Cdd:PRK11264 1 MSAIE-----VKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTarsLSQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 78 QAiarlGVIR--------TFQHVRLFKEMTVIENllvaqhqhlksgIFSGLLKTPAFRRAESEALdnAVKWLERVDLLPF 149
Cdd:PRK11264 76 QK----GLIRqlrqhvgfVFQNFNLFPHRTVLEN------------IIEGPVIVKGEPKEEATAR--ARELLAKVGLAGK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 150 ANRQAGNLAYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELrTHHNVSILLIEHDMKLVMGISDRIYV 229
Cdd:PRK11264 138 ETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQL-AQEKRTMVIVTHEMSFARDVADRAIF 216
|
250
....*....|....*....
gi 490378916 230 VNQGTPLANGTPSEIRQHP 248
Cdd:PRK11264 217 MDQGRIVEQGPAKALFADP 235
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
9-206 |
6.28e-27 |
|
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: 103.21 E-value: 6.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHL---EGLTGQAIARLGv 85
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLaeqRDEPHENILYLG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 86 irtfqHVRLFK-EMTVIENLLVAQHQHlksgifsgllktpafrRAESEALDNAvkwLERVDLLPFANRQAGNLAYGQQRR 164
Cdd:TIGR01189 80 -----HLPGLKpELSALENLHFWAAIH----------------GGAQRTIEDA---LAAVGLTGFEDLPAAQLSAGQQRR 135
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490378916 165 LEIARCMVTRPEILMLDEPAAGLNPKEtndlDDLIAELRTHH 206
Cdd:TIGR01189 136 LALARLWLSRRPLWILDEPTTALDKAG----VALLAGLLRAH 173
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
8-251 |
7.27e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 106.09 E-value: 7.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 8 LLQVNGLTMRFGG-----LLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTI----LYREKHLEGLTGQ 78
Cdd:PRK13631 21 ILRVKNLYCVFDEkqeneLVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 79 AIARLGVIRTFQhvRLFKEMTVIenLLVAQHQHLKSGIFSGLLKTP-AFRRAESEALDNAVKWLERVDL-LPFANRQAGN 156
Cdd:PRK13631 101 TNPYSKKIKNFK--ELRRRVSMV--FQFPEYQLFKDTIEKDIMFGPvALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 157 LAYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRThHNVSILLIEHDMKLVMGISDRIYVVNQGTPL 236
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKA-NNKTVFVITHTMEHVLEVADEVIVMDKGKIL 255
|
250
....*....|....*
gi 490378916 237 ANGTPSEIRQHPDVI 251
Cdd:PRK13631 256 KTGTPYEIFTDQHII 270
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
11-216 |
9.37e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 107.84 E-value: 9.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 11 VNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKhlegltgqaiARLGVIRtfQ 90
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG----------LRIGYLP--Q 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 91 HVRLFKEMTVIENLLVAqhqhlksgiFSGLLKTPAFRRAESEALDNAVKWLERVDLL----------------------- 147
Cdd:COG0488 69 EPPLDDDLTVLDTVLDG---------DAELRALEAELEELEAKLAEPDEDLERLAELqeefealggweaearaeeilsgl 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490378916 148 ----PFANRQAGNLAYGQQRRLEIARCMVTRPEILMLDEPaaglnpkeTNDLD-DLIAELRTH---HNVSILLIEHD 216
Cdd:COG0488 140 gfpeEDLDRPVSELSGGWRRRVALARALLSEPDLLLLDEP--------TNHLDlESIEWLEEFlknYPGTVLVVSHD 208
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
19-248 |
9.57e-27 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 106.04 E-value: 9.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 19 GGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIARL----GVIrtFQHVRL 94
Cdd:PRK11153 16 RTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKArrqiGMI--FQHFNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 95 FKEMTVIENLLVAqhqhlksgifsglLKTPAFRRAESEALDNAVkwLERVDLLPFANRQAGNLAYGQQRRLEIARCMVTR 174
Cdd:PRK11153 94 LSSRTVFDNVALP-------------LELAGTPKAEIKARVTEL--LELVGLSDKADRYPAQLSGGQKQRVAIARALASN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490378916 175 PEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPSEIRQHP 248
Cdd:PRK11153 159 PKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHP 232
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
6-233 |
9.66e-27 |
|
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: 108.23 E-value: 9.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 6 TPLLQVNGLTMRF---GGLL--------AVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYkPTSGTILYREKHLEG 74
Cdd:COG4172 273 PPLLEARDLKVWFpikRGLFrrtvghvkAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 75 LTGQAIARLGviRTFQHV----------RLFKEMTVIENLLVaqHQhlksgifsgllktPAFRRAESEALdnAVKWLERV 144
Cdd:COG4172 352 LSRRALRPLR--RRMQVVfqdpfgslspRMTVGQIIAEGLRV--HG-------------PGLSAAERRAR--VAEALEEV 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 145 DLLP-FANRqagnlaY------GQQRRLEIARCMVTRPEILMLDEPaaglnpkeTNDLD--------DLIAELRTHHNVS 209
Cdd:COG4172 413 GLDPaARHR------YphefsgGQRQRIAIARALILEPKLLVLDEP--------TSALDvsvqaqilDLLRDLQREHGLA 478
|
250 260
....*....|....*....|....
gi 490378916 210 ILLIEHDMKLVMGISDRIYVVNQG 233
Cdd:COG4172 479 YLFISHDLAVVRALAHRVMVMKDG 502
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
6-234 |
1.03e-26 |
|
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: 103.28 E-value: 1.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 6 TPLLQVNGLTMRF-----GG--LLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYRekHLEGLT-- 76
Cdd:COG4778 2 TTLLEVENLSKTFtlhlqGGkrLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVR--HDGGWVdl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 77 GQAIAR--LGVIRTF-----QHVRLFKEMTVIEnlLVAQhqhlksgifsgllktPAFRR--AESEALDNAVKWLERVDL- 146
Cdd:COG4778 80 AQASPReiLALRRRTigyvsQFLRVIPRVSALD--VVAE---------------PLLERgvDREEARARARELLARLNLp 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 147 -----LP---FAnrqaGnlayGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRtHHNVSILLIEHDMK 218
Cdd:COG4778 143 erlwdLPpatFS----G----GEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAK-ARGTAIIGIFHDEE 213
|
250
....*....|....*.
gi 490378916 219 LVMGISDRIYVVNQGT 234
Cdd:COG4778 214 VREAVADRVVDVTPFS 229
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
7-247 |
1.12e-26 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 104.71 E-value: 1.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 7 PLLQVNGLTMRFGGL--LAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAI-ARL 83
Cdd:PRK13635 4 EIIRVEHISFRYPDAatYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVrRQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 84 GVIrtFQHV-RLFKEMTV-------IENllvaqhqhlksgifSGLLKTPAFRRaesealdnaVKW-LERVDLLPFANRQA 154
Cdd:PRK13635 84 GMV--FQNPdNQFVGATVqddvafgLEN--------------IGVPREEMVER---------VDQaLRQVGMEDFLNREP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 155 GNLAYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGiSDRIYVVNQGT 234
Cdd:PRK13635 139 HRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGE 217
|
250
....*....|...
gi 490378916 235 PLANGTPSEIRQH 247
Cdd:PRK13635 218 ILEEGTPEEIFKS 230
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
9-233 |
1.88e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 103.63 E-value: 1.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRFG-GL----LAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIARL 83
Cdd:COG1101 2 LELKNLSKTFNpGTvnekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 84 gVIRTFQHVRL--FKEMTVIENLLVAQHQHLKSGIFSGLLKTpafRRAESEALdnavkwLERVDL-LPfaNR---QAGNL 157
Cdd:COG1101 82 -IGRVFQDPMMgtAPSMTIEENLALAYRRGKRRGLRRGLTKK---RRELFREL------LATLGLgLE--NRldtKVGLL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490378916 158 AYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMK--LVMGisDRIYVVNQG 233
Cdd:COG1101 150 SGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEqaLDYG--NRLIMMHEG 225
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
9-249 |
2.64e-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: 105.18 E-value: 2.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNgLTMRFGGL-LavnNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHL-EGLTGQAIA----R 82
Cdd:COG4148 3 LEVD-FRLRRGGFtL---DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqDSARGIFLPphrrR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 83 LGVIrtFQHVRLFKEMTVIENLLVAQHqhlksgifsgllKTPAFRRAESeaLDNAVKWLERVDLLpfaNRQAGNLAYGQQ 162
Cdd:COG4148 79 IGYV--FQEARLFPHLSVRGNLLYGRK------------RAPRAERRIS--FDEVVELLGIGHLL---DRRPATLSGGER 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 163 RRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPS 242
Cdd:COG4148 140 QRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLA 219
|
....*..
gi 490378916 243 EIRQHPD 249
Cdd:COG4148 220 EVLSRPD 226
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-219 |
3.43e-26 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 102.13 E-value: 3.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 1 MSHITTPLLQVNGLTMRFGG----LLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLT 76
Cdd:COG4181 1 MSSSSAPIIELRGLTKTVGTgageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 77 GQAIARL-----GVIrtFQHVRLFKEMTVIENLLVaqhqhlksgifsgllktPAFRRAESEALDNAVKWLERVDLLPFAN 151
Cdd:COG4181 81 EDARARLrarhvGFV--FQSFQLLPTLTALENVML-----------------PLELAGRRDARARARALLERVGLGHRLD 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490378916 152 RQAGNLAYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKL 219
Cdd:COG4181 142 HYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPAL 209
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
8-240 |
6.08e-26 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 102.40 E-value: 6.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 8 LLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYK----PTS-----GTILYREKHLEGLTGQ 78
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksAGShiellGRTVQREGRLARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 79 AIARLGVIrtFQHVRLFKEMTVIENLLVAqhqhlksgifsGLLKTPAFRRAES----EALDNAVKWLERVDLLPFANRQA 154
Cdd:PRK09984 84 SRANTGYI--FQQFNLVNRLSVLENVLIG-----------ALGSTPFWRTCFSwftrEQKQRALQALTRVGMVHFAHQRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 155 GNLAYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGT 234
Cdd:PRK09984 151 STLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGH 230
|
....*.
gi 490378916 235 PLANGT 240
Cdd:PRK09984 231 VFYDGS 236
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
19-233 |
7.97e-26 |
|
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: 100.56 E-value: 7.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 19 GGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIARL----GVIrtFQHVRL 94
Cdd:cd03292 12 NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLrrkiGVV--FQDFRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 95 FKEMTVIENLLVAqhqhlksgifsgLLKTPAFRRAESEALDNAvkwLERVDLLPFANRQAGNLAYGQQRRLEIARCMVTR 174
Cdd:cd03292 90 LPDRNVYENVAFA------------LEVTGVPPREIRKRVPAA---LELVGLSHKHRALPAELSGGEQQRVAIARAIVNS 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490378916 175 PEILMLDEPAAGLNPKETNDLDDLIAELRThHNVSILLIEHDMKLVMGISDRIYVVNQG 233
Cdd:cd03292 155 PTILIADEPTGNLDPDTTWEIMNLLKKINK-AGTTVVVATHAKELVDTTRHRVIALERG 212
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
7-233 |
1.21e-25 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 99.43 E-value: 1.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 7 PLLQVNGLTMRfgglLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIARLGVi 86
Cdd:cd03215 3 PVLEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGI- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 87 rtfQHV---R----LFKEMTVIENLLVAQHqhlksgiFSGllktpafrraesealdnavkwlervdllpfanrqaGNlay 159
Cdd:cd03215 78 ---AYVpedRkregLVLDLSVAENIALSSL-------LSG-----------------------------------GN--- 109
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490378916 160 gQQRRLeIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRThHNVSILLIEHDMKLVMGISDRIYVVNQG 233
Cdd:cd03215 110 -QQKVV-LARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELAD-AGKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
4-244 |
1.22e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 101.61 E-value: 1.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 4 ITTPLLQVNGLTMRFGG--LLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILyrekhLEGLT----- 76
Cdd:PRK13632 3 NKSVMIKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIK-----IDGITisken 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 77 -GQAIARLGVIrtFQHV-RLFKEMTVienllvaqhqhlKSGIFSGLLKTPAFRRAESEALDNAVKwleRVDLLPFANRQA 154
Cdd:PRK13632 78 lKEIRKKIGII--FQNPdNQFIGATV------------EDDIAFGLENKKVPPKKMKDIIDDLAK---KVGMEDYLDKEP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 155 GNLAYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMgISDRIYVVNQGT 234
Cdd:PRK13632 141 QNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGK 219
|
250
....*....|
gi 490378916 235 PLANGTPSEI 244
Cdd:PRK13632 220 LIAQGKPKEI 229
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
23-254 |
1.37e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 101.73 E-value: 1.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 23 AVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQ-----AIARLGVIRTFQHVRLFKE 97
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQkeikpVRKKVGVVFQFPESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 98 mTVIENLLVAQHQhlksgifsgllktpaFRRAESEALDNAVKWLERVDLLP-FANRQAGNLAYGQQRRLEIARCMVTRPE 176
Cdd:PRK13643 101 -TVLKDVAFGPQN---------------FGIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490378916 177 ILMLDEPAAGLNPKETNDLDDLIAELRtHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPSEIRQHPDVIKAY 254
Cdd:PRK13643 165 VLVLDEPTAGLDPKARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVDFLKAH 241
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
13-246 |
1.42e-25 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 105.21 E-value: 1.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 13 GLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILyrekhlegLTGQAIARlGVIRTFQHV 92
Cdd:NF033858 271 GLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAW--------LFGQPVDA-GDIATRRRV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 93 -------RLFKEMTVIENLLVaqHQHLksgifsgllktpaFRRAESEALDNAVKWLERVDLLPFANRQAGNLAYGQQRRL 165
Cdd:NF033858 342 gymsqafSLYGELTVRQNLEL--HARL-------------FHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRL 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 166 EIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGiSDRIYVVNQGTPLANGTPSEIR 245
Cdd:NF033858 407 SLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEAER-CDRISLMHAGRVLASDTPAALV 485
|
.
gi 490378916 246 Q 246
Cdd:NF033858 486 A 486
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
21-244 |
1.99e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 101.70 E-value: 1.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 21 LLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTI--LYREKHLEGLTGQAIA----------------- 81
Cdd:PRK13651 20 LKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewIFKDEKNKKKTKEKEKvleklviqktrfkkikk 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 82 ------RLGVIRTFQHVRLFKEmtVIEnllvaqhqhlKSGIFSGLlktpAFRRAESEALDNAVKWLERVDL-LPFANRQA 154
Cdd:PRK13651 100 ikeirrRVGVVFQFAEYQLFEQ--TIE----------KDIIFGPV----SMGVSKEEAKKRAAKYIELVGLdESYLQRSP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 155 GNLAYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRThHNVSILLIEHDMKLVMGISDRIYVVNQGT 234
Cdd:PRK13651 164 FELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNK-QGKTIILVTHDLDNVLEWTKRTIFFKDGK 242
|
250
....*....|
gi 490378916 235 PLANGTPSEI 244
Cdd:PRK13651 243 IIKDGDTYDI 252
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
6-251 |
2.37e-25 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 100.19 E-value: 2.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 6 TPLLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTIlyreKHLEGLtgqaiaRLGV 85
Cdd:PRK09544 2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI----KRNGKL------RIGY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 86 IRtfQHVRLFKEMTvienLLVAQHQHLKSGIFSGLLkTPAFRRAESEALDNAvkwlervdllPFAnrqagNLAYGQQRRL 165
Cdd:PRK09544 72 VP--QKLYLDTTLP----LTVNRFLRLRPGTKKEDI-LPALKRVQAGHLIDA----------PMQ-----KLSGGETQRV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 166 EIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGTpLANGTPSEIR 245
Cdd:PRK09544 130 LLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNHHI-CCSGTPEVVS 208
|
....*.
gi 490378916 246 QHPDVI 251
Cdd:PRK09544 209 LHPEFI 214
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-233 |
2.64e-25 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 100.52 E-value: 2.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 6 TPLLqVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILyrekhlEGLTGQAIARLGV 85
Cdd:PRK11247 11 TPLL-LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL------AGTAPLAEAREDT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 86 IRTFQHVRLFKEMTVIENLlvaqhqhlksgifsGLLKTPAFRRAESEALDnAVKWLERVDLLPFAnrqagnLAYGQQRRL 165
Cdd:PRK11247 84 RLMFQDARLLPWKKVIDNV--------------GLGLKGQWRDAALQALA-AVGLADRANEWPAA------LSGGQKQRV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490378916 166 EIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQG 233
Cdd:PRK11247 143 ALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEG 210
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
20-241 |
2.96e-25 |
|
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: 104.71 E-value: 2.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 20 GLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEglTGQAIARLGVIRTFQHVRLFKEMT 99
Cdd:TIGR01257 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE--TNLDAVRQSLGMCPQHNILFHHLT 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 100 VIENLLvaqhqhlksgiFSGLLKTPAFRRA--ESEALdnavkwLERVDLLPFANRQAGNLAYGQQRRLEIARCMVTRPEI 177
Cdd:TIGR01257 1020 VAEHIL-----------FYAQLKGRSWEEAqlEMEAM------LEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKV 1082
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490378916 178 LMLDEPAAGLNPKETNDLDDLIAELRTHHnvSILLIEHDMKLVMGISDRIYVVNQGTPLANGTP 241
Cdd:TIGR01257 1083 VVLDEPTSGVDPYSRRSIWDLLLKYRSGR--TIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
22-249 |
5.44e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 99.83 E-value: 5.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 22 LAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREkhlegltgQAIARLGVIRTFQHVRLfkemtVI 101
Cdd:PRK13648 23 FTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNN--------QAITDDNFEKLRKHIGI-----VF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 102 ENllvAQHQHLKS--------GIFSGLLKTPAFRRAESEALdnavkwlERVDLLPFANRQAGNLAYGQQRRLEIARCMVT 173
Cdd:PRK13648 90 QN---PDNQFVGSivkydvafGLENHAVPYDEMHRRVSEAL-------KQVDMLERADYEPNALSGGQKQRVAIAGVLAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490378916 174 RPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGiSDRIYVVNQGTPLANGTPSEIRQHPD 249
Cdd:PRK13648 160 NPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAE 234
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
5-233 |
5.54e-25 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 99.34 E-value: 5.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 5 TTPLLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCL-------TGFYkpTSGTILYRekhlegltG 77
Cdd:COG1117 8 LEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndliPGAR--VEGEILLD--------G 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 78 QAI-----------ARLGVIrtFQHVRLFkEMTVIENllVA---QHQHLKSgifsgllktpafrRAEseaLDNAVKW-LE 142
Cdd:COG1117 78 EDIydpdvdvvelrRRVGMV--FQKPNPF-PKSIYDN--VAyglRLHGIKS-------------KSE---LDEIVEEsLR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 143 RVDL-------LpfaNRQAGNLAYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRthHNVSILLIEH 215
Cdd:COG1117 137 KAALwdevkdrL---KKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELK--KDYTIVIVTH 211
|
250
....*....|....*...
gi 490378916 216 DMKLVMGISDRIYVVNQG 233
Cdd:COG1117 212 NMQQAARVSDYTAFFYLG 229
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
9-244 |
1.24e-24 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 102.19 E-value: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGF--YKPTSGTILYR----EKHL---------- 72
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHvalcEKCGyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 73 --------------------EGLTGQAIARLGVI--RTFQhvrLFKEMTVIENLLVAQHQHLKSGifsgllktpafrrae 130
Cdd:TIGR03269 81 pcpvcggtlepeevdfwnlsDKLRRRIRKRIAIMlqRTFA---LYGDDTVLDNVLEALEEIGYEG--------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 131 SEALDNAVKWLERVDLLPFANRQAGNLAYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSI 210
Cdd:TIGR03269 143 KEAVGRAVDLIEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISM 222
|
250 260 270
....*....|....*....|....*....|....
gi 490378916 211 LLIEHDMKLVMGISDRIYVVNQGTPLANGTPSEI 244
Cdd:TIGR03269 223 VLTSHWPEVIEDLSDKAIWLENGEIKEEGTPDEV 256
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-233 |
2.64e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 100.86 E-value: 2.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 4 ITTPLLQVNGLTMRfgglLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLT-GQAI-A 81
Cdd:COG1129 252 PGEVVLEVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSpRDAIrA 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 82 RLGVI---RtfQHVRLFKEMTVIENL-LVAQHQHLKSGIFSgllktpafRRAESEAldnAVKWLERVDL-LPFANRQAGN 156
Cdd:COG1129 328 GIAYVpedR--KGEGLVLDLSIRENItLASLDRLSRGGLLD--------RRRERAL---AEEYIKRLRIkTPSPEQPVGN 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 157 LAYGQQRRLEIARCMVTRPEILMLDEPAAGlnpketndLD--------DLIAELrTHHNVSILLIEHDMKLVMGISDRIY 228
Cdd:COG1129 395 LSGGNQQKVVLAKWLATDPKVLILDEPTRG--------IDvgakaeiyRLIREL-AAEGKAVIVISSELPELLGLSDRIL 465
|
....*
gi 490378916 229 VVNQG 233
Cdd:COG1129 466 VMREG 470
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
19-246 |
3.15e-24 |
|
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: 96.91 E-value: 3.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 19 GGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAI-ARLGVIrtFQHVRLFKE 97
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLrSMIGVV--LQDTFLFSG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 98 mTVIENLlvaqhqhlksgifsgLLKTPAFRRAESEALDNAVKWLERVDLLP-----FANRQAGNLAYGQQRRLEIARCMV 172
Cdd:cd03254 92 -TIMENI---------------RLGRPNATDEEVIEAAKEAGAHDFIMKLPngydtVLGENGGNLSQGERQLLAIARAML 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490378916 173 TRPEILMLDEPAAGLNPKETNDLDDLIAELRthHNVSILLIEHDMKLVMGiSDRIYVVNQGTPLANGTPSEIRQ 246
Cdd:cd03254 156 RDPKILILDEATSNIDTETEKLIQEALEKLM--KGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELLA 226
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-259 |
3.55e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 97.29 E-value: 3.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKptsgtiLYREKHLEG---LTGQAIARLGV 85
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIE------LYPEARVSGevyLDGQDIFKMDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 86 IRTFQHVRL-FKEMTVIENLLVAQHQHLKSGIfSGLLKTPA--FRRAEsEALDNAVKWLERVDLLpfaNRQAGNLAYGQQ 162
Cdd:PRK14247 78 IELRRRVQMvFQIPNPIPNLSIFENVALGLKL-NRLVKSKKelQERVR-WALEKAQLWDEVKDRL---DAPAGKLSGGQQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 163 RRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRThhNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPS 242
Cdd:PRK14247 153 QRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKK--DMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTR 230
|
250
....*....|....*..
gi 490378916 243 EIRQHPdviKAYLGEAY 259
Cdd:PRK14247 231 EVFTNP---RHELTEKY 244
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
6-219 |
5.06e-24 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 96.42 E-value: 5.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 6 TPLLQVNGLTMRF--GGLLA--VNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIA 81
Cdd:PRK11629 3 KILLQCDNLCKRYqeGSVQTdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 82 -----RLGVIRTFQHvrLFKEMTVIEN----LLVAQhqhlksgifsgllKTPAfrraesEALDNAVKWLERVDLLPFANR 152
Cdd:PRK11629 83 elrnqKLGFIYQFHH--LLPDFTALENvampLLIGK-------------KKPA------EINSRALEMLAAVGLEHRANH 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490378916 153 QAGNLAYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKL 219
Cdd:PRK11629 142 RPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQL 208
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
8-217 |
5.14e-24 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 97.08 E-value: 5.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 8 LLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTgqaiARLGVIr 87
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG----AERGVV- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 88 tFQHVRLFKEMTVIENLLVAqhqhlksgifsglLKTPAFRRAESEALdnAVKWLERVDLLPFANRQAGNLAYGQQRRLEI 167
Cdd:PRK11248 76 -FQNEGLLPWRNVQDNVAFG-------------LQLAGVEKMQRLEI--AHQMLKKVGLEGAEKRYIWQLSGGQRQRVGI 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490378916 168 ARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDM 217
Cdd:PRK11248 140 ARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
4-226 |
5.55e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 96.77 E-value: 5.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 4 ITTPLLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLT--GFYKP---TSGTILYREKHLEGLTGQ 78
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPevtITGSIVYNGHNIYSPRTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 79 AIA-RLGVIRTFQHVRLFKeMTVIENLLVAQHqhlksgiFSGLLKTPAFRRAESEALDNAVKWLERVDLLpfaNRQAGNL 157
Cdd:PRK14239 81 TVDlRKEIGMVFQQPNPFP-MSIYENVVYGLR-------LKGIKDKQVLDEAVEKSLKGASIWDEVKDRL---HDSALGL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490378916 158 AYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRthHNVSILLIEHDMKLVMGISDR 226
Cdd:PRK14239 150 SGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLK--DDYTMLLVTRSMQQASRISDR 216
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
5-233 |
6.44e-24 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 100.08 E-value: 6.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 5 TTPLLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILY--REKHLEGLTGQAIAR 82
Cdd:PRK10762 1 MQALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYlgKEVTFNGPKSSQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 83 LGVIRtfQHVRLFKEMTVIENllvaqhqhlksgIFSGLLKTPAFRRAE-SEALDNAVKWLERVDLLPFANRQAGNLAYGQ 161
Cdd:PRK10762 81 IGIIH--QELNLIPQLTIAEN------------IFLGREFVNRFGRIDwKKMYAEADKLLARLNLRFSSDKLVGELSIGE 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490378916 162 QRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRThHNVSILLIEHDMKLVMGISDRIYVVNQG 233
Cdd:PRK10762 147 QQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKS-QGRGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
8-244 |
7.43e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 97.00 E-value: 7.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 8 LLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEgltgqaIARLGVIR 87
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD------YSKRGLLA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 88 TFQHVrlfkeMTVIENllvAQHQHLKSGIFSGL---LKTPAFRRAE-SEALDNAvkwLERVDLLPFANRQAGNLAYGQQR 163
Cdd:PRK13638 75 LRQQV-----ATVFQD---PEQQIFYTDIDSDIafsLRNLGVPEAEiTRRVDEA---LTLVDAQHFRHQPIQCLSHGQKK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 164 RLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNvSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPSE 243
Cdd:PRK13638 144 RVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGN-HVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGE 222
|
.
gi 490378916 244 I 244
Cdd:PRK13638 223 V 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-234 |
7.73e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 99.75 E-value: 7.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 7 PLLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTIlyrekhlegltgqaiaRLGV- 85
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV----------------KLGEt 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 86 --IRTF-QHVRLFK-EMTVIENLlvaqhQHLKSGifsgllKTPAFRRAesealdnavkWLERvdllpF------ANRQAG 155
Cdd:COG0488 378 vkIGYFdQHQEELDpDKTVLDEL-----RDGAPG------GTEQEVRG----------YLGR-----FlfsgddAFKPVG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 156 NLAYGQQRRLEIARCMVTRPEILMLDEPaaglnpkeTNDLD----DLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVN 231
Cdd:COG0488 432 VLSGGEKARLALAKLLLSPPNVLLLDEP--------TNHLDietlEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFE 503
|
...
gi 490378916 232 QGT 234
Cdd:COG0488 504 DGG 506
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
8-234 |
1.16e-23 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 99.09 E-value: 1.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 8 LLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYkPT---SGTILYREKHLEGLTGQAIARLG 84
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEVCRFKDIRDSEALG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 85 VIRTFQHVRLFKEMTVIENLLVAqHQHLKSGIFSgllktpafrraESEALDNAVKWLERVDLLPFANRQAGNLAYGQQRR 164
Cdd:NF040905 80 IVIIHQELALIPYLSIAENIFLG-NERAKRGVID-----------WNETNRRARELLAKVGLDESPDTLVTDIGVGKQQL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 165 LEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSIlLIEHDMKLVMGISDRIYVVNQGT 234
Cdd:NF040905 148 VEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSI-IISHKLNEIRRVADSITVLRDGR 216
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
22-248 |
1.17e-23 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 98.57 E-value: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 22 LAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTG---QAIARLGVIRTFQHVRLFKEM 98
Cdd:PRK10070 42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDaelREVRRKKIAMVFQSFALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 99 TVIENLLVAQHqhlksgifsgLLKTPAFRRAEsEALDNavkwLERVDLLPFANRQAGNLAYGQQRRLEIARCMVTRPEIL 178
Cdd:PRK10070 122 TVLDNTAFGME----------LAGINAEERRE-KALDA----LRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDIL 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 179 MLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPSEIRQHP 248
Cdd:PRK10070 187 LMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNP 256
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
7-206 |
1.17e-23 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 94.56 E-value: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 7 PLLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLE-GLTGQAIARLGv 85
Cdd:PRK13539 1 MMLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDdPDVAEACHYLG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 86 irtfqHVRLFK-EMTVIENLLVAQhqhlksgifsgllktpAFRRAESEALDNAvkwLERVDLLPFANRQAGNLAYGQQRR 164
Cdd:PRK13539 80 -----HRNAMKpALTVAENLEFWA----------------AFLGGEELDIAAA---LEAVGLAPLAHLPFGYLSAGQKRR 135
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490378916 165 LEIARCMVTRPEILMLDEPAAGLNpketNDLDDLIAELRTHH 206
Cdd:PRK13539 136 VALARLLVSNRPIWILDEPTAALD----AAAVALFAELIRAH 173
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
9-246 |
1.73e-23 |
|
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: 94.13 E-value: 1.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGF--YKPTSGTILYREKHLEGLTGQAIARLGVI 86
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERARLGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 87 RTFQHVRLFKEMTVIENLlvaqhQHLKSGiFSGllktpafrraesealdnavkwlervdllpfanrqagnlayGQQRRLE 166
Cdd:cd03217 81 LAFQYPPEIPGVKNADFL-----RYVNEG-FSG----------------------------------------GEKKRNE 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 167 IARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRThHNVSILLIEHDMKLVMGI-SDRIYVVNQGTPLANGTPSEIR 245
Cdd:cd03217 115 ILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLRE-EGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDKELAL 193
|
.
gi 490378916 246 Q 246
Cdd:cd03217 194 E 194
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
5-248 |
2.18e-23 |
|
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: 98.60 E-value: 2.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 5 TTPLLQVNGLTMRFGG----LLAVNNVELTINQGEIVSLIGPNGAGKT----TIFNCLTGFYKPTSGTILYREKHLEGLT 76
Cdd:COG4172 3 SMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 77 GQAI-----ARLGVIrtFQhvrlfkE-MT-----------VIENLLVaqHQHLksgifsgllktpafRRAESEALdnAVK 139
Cdd:COG4172 83 ERELrrirgNRIAMI--FQ------EpMTslnplhtigkqIAEVLRL--HRGL--------------SGAAARAR--ALE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 140 WLERVDLlPFANRQAGnlAY------GQQRRLEIARCMVTRPEILMLDEPaaglnpkeTNDLD--------DLIAELRTH 205
Cdd:COG4172 137 LLERVGI-PDPERRLD--AYphqlsgGQRQRVMIAMALANEPDLLIADEP--------TTALDvtvqaqilDLLKDLQRE 205
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 490378916 206 HNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPSEI---RQHP 248
Cdd:COG4172 206 LGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELfaaPQHP 251
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
23-251 |
2.67e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 95.64 E-value: 2.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 23 AVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYRekhlegltGQAIARLGVirtfQHVRLFKEMTVie 102
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIR--------GEPITKENI----REVRKFVGLVF-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 103 nllvaqhQHLKSGIFSGLLKT-----PAFRRAESEALDNAV-KWLERVDLLPFANRQAGNLAYGQQRRLEIARCMVTRPE 176
Cdd:PRK13652 85 -------QNPDDQIFSPTVEQdiafgPINLGLDEETVAHRVsSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490378916 177 ILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPSEIRQHPDVI 251
Cdd:PRK13652 158 VLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDLL 232
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
14-233 |
2.84e-23 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 94.26 E-value: 2.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 14 LTMRFggllavnnvELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTI-LYREKHleglTGQAIARLGVIRTFQHV 92
Cdd:PRK10771 14 LPMRF---------DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLtLNGQDH----TTTPPSRRPVSMLFQEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 93 RLFKEMTVIENLLVaqhqhlksGIFSGLlKTPAFRRAESEALdnavkwLERVDLLPFANRQAGNLAYGQQRRLEIARCMV 172
Cdd:PRK10771 81 NLFSHLTVAQNIGL--------GLNPGL-KLNAAQREKLHAI------ARQMGIEDLLARLPGQLSGGQRQRVALARCLV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490378916 173 TRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQG 233
Cdd:PRK10771 146 REQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADG 206
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-253 |
4.20e-23 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 97.81 E-value: 4.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 5 TTPLLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIARLG 84
Cdd:PRK15439 8 APPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 85 VIRTFQHVRLFKEMTVIENLLVaqhqhlksgifsGLLKTPafrrAESEALDNAVKWLE-RVDLlpfaNRQAGNLAYGQQR 163
Cdd:PRK15439 88 IYLVPQEPLLFPNLSVKENILF------------GLPKRQ----ASMQKMKQLLAALGcQLDL----DSSAGSLEVADRQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 164 RLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRThHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPSE 243
Cdd:PRK15439 148 IVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLA-QGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTAD 226
|
250
....*....|
gi 490378916 244 IRqHPDVIKA 253
Cdd:PRK15439 227 LS-TDDIIQA 235
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
9-230 |
5.36e-23 |
|
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: 97.36 E-value: 5.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRFGG-LLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTgQAIARLGVIR 87
Cdd:TIGR02857 322 LEFSGVSVAYPGrRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADAD-ADSWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 88 TFQHVRLFkEMTVIENLLVAQhqhlksgifsgllktpafRRAESEALDNAvkwLERVDLLPFA-------NRQAGN---- 156
Cdd:TIGR02857 401 VPQHPFLF-AGTIAENIRLAR------------------PDASDAEIREA---LERAGLDEFVaalpqglDTPIGEggag 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490378916 157 LAYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVsiLLIEHDMKLvMGISDRIYVV 230
Cdd:TIGR02857 459 LSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTV--LLVTHRLAL-AALADRIVVL 529
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
26-239 |
6.95e-23 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 92.74 E-value: 6.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 26 NVELTINqGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTI-----LYREKHLEGLTGQAIARLGVIrtFQHVRLFKEMTV 100
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngtVLFDSRKKINLPPQQRKIGLV--FQQYALFPHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 101 IENLLVAqhqhlksgifsglLKtpafRRAESEALDNAVKWLERVDLLPFANRQAGNLAYGQQRRLEIARCMVTRPEILML 180
Cdd:cd03297 93 RENLAFG-------------LK----RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490378916 181 DEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANG 239
Cdd:cd03297 156 DEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
19-227 |
1.89e-22 |
|
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: 91.55 E-value: 1.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 19 GGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLegltgQAIARLGVIR-TFQHVR--LF 95
Cdd:cd03226 11 KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI-----KAKERRKSIGyVMQDVDyqLF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 96 KEmTVIENLLVAqhqhlksgifsglLKTPAFRRAESEALdnavkwLERVDLLPFANRQAGNLAYGQQRRLEIARCMVTRP 175
Cdd:cd03226 86 TD-SVREELLLG-------------LKELDAGNEQAETV------LKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGK 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490378916 176 EILMLDEPAAGLNPKETNDLDDLIAELRThHNVSILLIEHDMKLVMGISDRI 227
Cdd:cd03226 146 DLLIFDEPTSGLDYKNMERVGELIRELAA-QGKAVIVITHDYEFLAKVCDRV 196
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
5-225 |
7.68e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 91.38 E-value: 7.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 5 TTPLLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNC-------LTGFYkpTSGTILYREKHLEGLTG 77
Cdd:PRK14243 7 TETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrlndlIPGFR--VEGKVTFHGKNLYAPDV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 78 QAIA---RLGVIrtFQHVRLFKEmTVIENLLVAQHQHLKSGIFSGLLKTpafrraeseALDNAVKWLERVDLLpfanRQA 154
Cdd:PRK14243 85 DPVEvrrRIGMV--FQKPNPFPK-SIYDNIAYGARINGYKGDMDELVER---------SLRQAALWDEVKDKL----KQS 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490378916 155 G-NLAYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHnvSILLIEHDMKLVMGISD 225
Cdd:PRK14243 149 GlSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSD 218
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
23-252 |
8.16e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 91.34 E-value: 8.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 23 AVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLT-----GQAIARLGVIRTFQHVRLFKE 97
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdiKQIRKKVGLVFQFPESQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 98 mTVIENLLVAQHQHlksgifsGLLKTPAFRRA-ESEALDNAVKwlERVDLLPFanrqagNLAYGQQRRLEIARCMVTRPE 176
Cdd:PRK13649 102 -TVLKDVAFGPQNF-------GVSQEEAEALArEKLALVGISE--SLFEKNPF------ELSGGQMRRVAIAGILAMEPK 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490378916 177 ILMLDEPAAGLNPKETNDLDDLIAELrtHHN-VSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPSEIRQHPDVIK 252
Cdd:PRK13649 166 ILVLDEPTAGLDPKGRKELMTLFKKL--HQSgMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQDVDFLE 240
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
23-244 |
9.13e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 91.38 E-value: 9.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 23 AVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILY---------REKHLEgltgQAIARLGVIRTFQHVR 93
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVdditithktKDKYIR----PVRKRIGMVFQFPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 94 LFKEMTVIENLLVAQH-----QHLKSGIFSgLLKTPAFRRaesealdnavkwlERVDLLPFanrqagNLAYGQQRRLEIA 168
Cdd:PRK13646 98 LFEDTVEREIIFGPKNfkmnlDEVKNYAHR-LLMDLGFSR-------------DVMSQSPF------QMSGGQMRKIAIV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490378916 169 RCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPSEI 244
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
7-244 |
1.07e-21 |
|
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: 93.71 E-value: 1.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 7 PLLQVNGLTMRF-----GGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYR--------EKHLE 73
Cdd:TIGR03269 278 PIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgdewvdmTKPGP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 74 GLTGQAIARLGVIrtFQHVRLFKEMTVIENLLVA-------QHQHLKSGIfsgLLKTPAFRRAESEALdnavkwlervdl 146
Cdd:TIGR03269 358 DGRGRAKRYIGIL--HQEYDLYPHRTVLDNLTEAiglelpdELARMKAVI---TLKMVGFDEEKAEEI------------ 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 147 lpfANRQAGNLAYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDR 226
Cdd:TIGR03269 421 ---LDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDR 497
|
250
....*....|....*...
gi 490378916 227 IYVVNQGTPLANGTPSEI 244
Cdd:TIGR03269 498 AALMRDGKIVKIGDPEEI 515
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-242 |
3.94e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 89.41 E-value: 3.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 1 MSHIttplLQVNGLTMRF-GGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSG--TILYREKHLEglTG 77
Cdd:PRK13647 1 MDNI----IEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGrvKVMGREVNAE--NE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 78 QAI-ARLGVIrtFQHV--RLFKeMTVIENLLVAQhqhlksgIFSGLLKTPAFRRAEsEALDnavkwleRVDLLPFANRQA 154
Cdd:PRK13647 75 KWVrSKVGLV--FQDPddQVFS-STVWDDVAFGP-------VNMGLDKDEVERRVE-EALK-------AVRMWDFRDKPP 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 155 GNLAYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELrthHN--VSILLIEHDMKLVMGISDRIYVVNQ 232
Cdd:PRK13647 137 YHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRL---HNqgKTVIVATHDVDLAAEWADQVIVLKE 213
|
250
....*....|
gi 490378916 233 GTPLANGTPS 242
Cdd:PRK13647 214 GRVLAEGDKS 223
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
10-256 |
4.84e-21 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 89.08 E-value: 4.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 10 QVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIARlGVIRTF 89
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFAR-KVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 90 QHVRLFKEMTVIEnlLVAQHQHLKSGIFSgllktpAFRRAESEALDNAVKWlerVDLLPFANRQAGNLAYGQQRRLEIAR 169
Cdd:PRK10575 92 QQLPAAEGMTVRE--LVAIGRYPWHGALG------RFGAADREKVEEAISL---VGLKPLAHRLVDSLSGGERQRAWIAM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 170 CMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPSEIRQhPD 249
Cdd:PRK10575 161 LVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMR-GE 239
|
....*..
gi 490378916 250 VIKAYLG 256
Cdd:PRK10575 240 TLEQIYG 246
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
9-188 |
6.04e-21 |
|
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: 87.55 E-value: 6.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHL---EGLTGQAIARLGv 85
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLdfqRDSIARGLLYLG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 86 irtfqHVRLFK-EMTVIENLLVAQHQHLKSGIFsgllktpafrraesEALDnavkwleRVDLLPFANRQAGNLAYGQQRR 164
Cdd:cd03231 80 -----HAPGIKtTLSVLENLRFWHADHSDEQVE--------------EALA-------RVGLNGFEDRPVAQLSAGQQRR 133
|
170 180
....*....|....*....|....
gi 490378916 165 LEIARCMVTRPEILMLDEPAAGLN 188
Cdd:cd03231 134 VALARLLLSGRPLWILDEPTTALD 157
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
18-233 |
8.85e-21 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 90.94 E-value: 8.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 18 FGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIARLGVIRTFQHVRLFKE 97
Cdd:PRK10982 8 FPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQELNLVLQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 98 MTVIENLLVAQHQhlKSGIFSGLLKTPAFRRAESEALDnavkwlerVDLLPfaNRQAGNLAYGQQRRLEIARCMVTRPEI 177
Cdd:PRK10982 88 RSVMDNMWLGRYP--TKGMFVDQDKMYRDTKAIFDELD--------IDIDP--RAKVATLSVSQMQMIEIAKAFSYNAKI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490378916 178 LMLDEPAAGLNPKETNDLDDLIAELRtHHNVSILLIEHDMKLVMGISDRIYVVNQG 233
Cdd:PRK10982 156 VIMDEPTSSLTEKEVNHLFTIIRKLK-ERGCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
10-253 |
1.02e-20 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 87.83 E-value: 1.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 10 QVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIAR-LGVIRT 88
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKrLAILRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 89 FQHV--RLfkemTVIEnlLVA-----QHQhlksgifsGLLkTPAFRRAESEALDnavkwleRVDLLPFANRQAGNLAYGQ 161
Cdd:COG4604 83 ENHInsRL----TVRE--LVAfgrfpYSK--------GRL-TAEDREIIDEAIA-------YLDLEDLADRYLDELSGGQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 162 QRRLEIArcMV----TrpEILMLDEPaaglnpkeTNDLD-----DLIAELR---THHNVSILLIEHDMKLVMGISDRIYV 229
Cdd:COG4604 141 RQRAFIA--MVlaqdT--DYVLLDEP--------LNNLDmkhsvQMMKLLRrlaDELGKTVVIVLHDINFASCYADHIVA 208
|
250 260
....*....|....*....|....
gi 490378916 230 VNQGTPLANGTPSEIRQhPDVIKA 253
Cdd:COG4604 209 MKDGRVVAQGTPEEIIT-PEVLSD 231
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
8-247 |
1.10e-20 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 90.93 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 8 LLQVNGLTMRFGG--LLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIaRLGV 85
Cdd:TIGR02203 330 DVEFRNVTFRYPGrdRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASL-RRQV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 86 IRTFQHVRLFKEmTVIENLLVAqhqhlksgifsgllKTPAFRRAESEALDNAVKWLERVDLLPFANRQ-----AGNLAYG 160
Cdd:TIGR02203 409 ALVSQDVVLFND-TIANNIAYG--------------RTEQADRAEIERALAAAYAQDFVDKLPLGLDTpigenGVLLSGG 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 161 QQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRthHNVSILLIEHDMKLVMGiSDRIYVVNQGTPLANGT 240
Cdd:TIGR02203 474 QRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLM--QGRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERGT 550
|
....*..
gi 490378916 241 PSEIRQH 247
Cdd:TIGR02203 551 HNELLAR 557
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
22-253 |
1.48e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 88.22 E-value: 1.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 22 LAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTIlyrekHLEGLTGQAIARLGVIRT-----FQH----- 91
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKV-----YVDGLDTSDEENLWDIRNkagmvFQNpdnqi 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 92 VRLFKEMTVI---ENLLVAQHQhlksgifsgllktpaFRraesEALDNAvkwLERVDLLPFANRQAGNLAYGQQRRLEIA 168
Cdd:PRK13633 99 VATIVEEDVAfgpENLGIPPEE---------------IR----ERVDES---LKKVGMYEYRRHAPHLLSGGQKQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 169 RCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGiSDRIYVVNQGTPLANGTPSEIRQHP 248
Cdd:PRK13633 157 GILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKEV 235
|
....*
gi 490378916 249 DVIKA 253
Cdd:PRK13633 236 EMMKK 240
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
9-244 |
2.37e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 86.99 E-value: 2.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIARLGVIRT 88
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 89 FQHvrLFKE-MTVIEnlLVA--QHQHLKsgiFSGLLKTpafrraESEALdnaVKW-LERVDLLPFANRQAGNLAYGQQRR 164
Cdd:PRK11231 83 QHH--LTPEgITVRE--LVAygRSPWLS---LWGRLSA------EDNAR---VNQaMEQTRINHLADRRLTDLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 165 LEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIeHDMKLVMGISDRIYVVNQGTPLANGTPSEI 244
Cdd:PRK11231 147 AFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVL-HDLNQASRYCDHLVVLANGHVMAQGTPEEV 225
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
9-234 |
3.91e-20 |
|
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: 83.65 E-value: 3.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTIlyrekhlegltgqaiarlgvirt 88
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 89 fqhvrlfkemTVIENLLVAQHQHLkSGifsgllktpafrraesealdnavkwlervdllpfanrqagnlayGQQRRLEIA 168
Cdd:cd03221 58 ----------TWGSTVKIGYFEQL-SG--------------------------------------------GEKMRLALA 82
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490378916 169 RCMVTRPEILMLDEPaaglnpkeTNDLDD-----LIAELRTHHNvSILLIEHDMKLVMGISDRIYVVNQGT 234
Cdd:cd03221 83 KLLLENPNLLLLDEP--------TNHLDLesieaLEEALKEYPG-TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
23-244 |
4.23e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 86.99 E-value: 4.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 23 AVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSG-TILYREKHLEGLTG-QAIARL----GVIRTFQHVRLFK 96
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqTIVGDYAIPANLKKiKEVKRLrkeiGLVFQFPEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 97 EmtVIENLLVAQHQHLksgifsGLLKTPAFRRAEsealdnavkwlERVDL--LP--FANRQAGNLAYGQQRRLEIARCMV 172
Cdd:PRK13645 106 E--TIEKDIAFGPVNL------GENKQEAYKKVP-----------ELLKLvqLPedYVKRSPFELSGGQKRRVALAGIIA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490378916 173 TRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPSEI 244
Cdd:PRK13645 167 MDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEI 238
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-225 |
4.34e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 86.63 E-value: 4.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 7 PLLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKptsgtiLYREKHLEG---LTGQAI--- 80
Cdd:PRK14258 6 PAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE------LESEVRVEGrveFFNQNIyer 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 81 ------ARLGVIRTFQHVRLFKeMTVIENL-----LVAQHQHLKsgiFSGLLKTpafrraeseALDNAVKWLERVDLLpf 149
Cdd:PRK14258 80 rvnlnrLRRQVSMVHPKPNLFP-MSVYDNVaygvkIVGWRPKLE---IDDIVES---------ALKDADLWDEIKHKI-- 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490378916 150 aNRQAGNLAYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISD 225
Cdd:PRK14258 145 -HKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSD 219
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
8-210 |
6.61e-20 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 84.86 E-value: 6.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 8 LLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYRekhlegltGQAIARLGVir 87
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQ--------GEPIRRQRD-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 88 TFQHVRLF--------KEMTVIENLLVAQHQHlksgifsgllktpafRRAESEALDNAvkwLERVDLLPFANRQAGNLAY 159
Cdd:PRK13538 71 EYHQDLLYlghqpgikTELTALENLRFYQRLH---------------GPGDDEALWEA---LAQVGLAGFEDVPVRQLSA 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 160 GQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAE---------LRTHHNVSI 210
Cdd:PRK13538 133 GQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQhaeqggmviLTTHQDLPV 192
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
9-256 |
1.63e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 85.04 E-value: 1.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIAR-LGVIR 87
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARrIGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 88 tfQHVRLFKEMTVIEnlLVAQHQHLKSGIFSgllktpAFRRAESEALDNAVKWLERVDLlpfANRQAGNLAYGQQRRLEI 167
Cdd:PRK10253 88 --QNATTPGDITVQE--LVARGRYPHQPLFT------RWRKEDEEAVTKAMQATGITHL---ADQSVDTLSGGQRQRAWI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 168 ARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPSEIRQh 247
Cdd:PRK10253 155 AMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVT- 233
|
....*....
gi 490378916 248 PDVIKAYLG 256
Cdd:PRK10253 234 AELIERIYG 242
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
23-243 |
1.67e-19 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 87.53 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 23 AVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAI-ARLGVIrtFQHVRLFkEMTVI 101
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLrRQIGVV--PQDTFLF-SGTIR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 102 ENLLVAQHQhlksgifsgllktpafrrAESEALDNAVKW---LERVDLLP-----FANRQAGNLAYGQQRRLEIARCMVT 173
Cdd:COG1132 432 ENIRYGRPD------------------ATDEEVEEAAKAaqaHEFIEALPdgydtVVGERGVNLSGGQRQRIAIARALLK 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490378916 174 RPEILMLDEPAAGLNPkET-----NDLDDLIAElRThhnvsILLIEHDMKLVMGiSDRIYVVNQGTPLANGTPSE 243
Cdd:COG1132 494 DPPILILDEATSALDT-ETealiqEALERLMKG-RT-----TIVIAHRLSTIRN-ADRILVLDDGRIVEQGTHEE 560
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
7-206 |
1.95e-19 |
|
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: 87.03 E-value: 1.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 7 PLLQVNGLTMRF-GGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIARlgV 85
Cdd:TIGR02868 333 PTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRR--R 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 86 IRTF-QHVRLFkEMTVIENLLVAQhqhlksgifsgllktpafrraeSEALDNAVKW-LERVDLLPFANRQAGNLAY---- 159
Cdd:TIGR02868 411 VSVCaQDAHLF-DTTVRENLRLAR----------------------PDATDEELWAaLERVGLADWLRALPDGLDTvlge 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490378916 160 -------GQQRRLEIARCMVTRPEILMLDEPAAGLNPKETND-LDDLIAELR-------THH 206
Cdd:TIGR02868 468 ggarlsgGERQRLALARALLADAPILLLDEPTEHLDAETADElLEDLLAALSgrtvvliTHH 529
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
7-233 |
1.98e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 87.00 E-value: 1.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 7 PLLQVNGLTMR-FGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIARLGV 85
Cdd:COG3845 256 VVLEVENLSVRdDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGV 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 86 --I---RtfQHVRLFKEMTVIENLLVAQHqhlKSGIFS--GLLKTPAFRRaesealdNAVKWLERVDL-LPFANRQAGNL 157
Cdd:COG3845 336 ayIpedR--LGRGLVPDMSVAENLILGRY---RRPPFSrgGFLDRKAIRA-------FAEELIEEFDVrTPGPDTPARSL 403
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490378916 158 AYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRThHNVSILLIEHDMKLVMGISDRIYVVNQG 233
Cdd:COG3845 404 SGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRD-AGAAVLLISEDLDEILALSDRIAVMYEG 478
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
9-233 |
2.36e-19 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 86.60 E-value: 2.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMrfgglLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHL------EGLTgQAIAR 82
Cdd:PRK10762 258 LKVDNLSG-----PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvtrspqDGLA-NGIVY 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 83 LGVIRtfQHVRLFKEMTVIENLLVAQHQHLKSGifSGLLKtpafRRAESEALDNAVKwLERVDLlPFANRQAGNLAYGQQ 162
Cdd:PRK10762 332 ISEDR--KRDGLVLGMSVKENMSLTALRYFSRA--GGSLK----HADEQQAVSDFIR-LFNIKT-PSMEQAIGLLSGGNQ 401
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490378916 163 RRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRThHNVSILLIEHDMKLVMGISDRIYVVNQG 233
Cdd:PRK10762 402 QKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKA-EGLSIILVSSEMPEVLGMSDRILVMHEG 471
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
4-243 |
2.46e-19 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 84.55 E-value: 2.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 4 ITTPLLQVNGLTMRF-GGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYrekhLEGLTGQAIAR 82
Cdd:PRK15056 2 MQQAGIVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISI----LGQPTRQALQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 83 --LGVIRTFQHVRLFKEMTVIENLLVAQHQHLksgifsGLLKTPAFRraESEALDNAvkwLERVDLLPFANRQAGNLAYG 160
Cdd:PRK15056 78 nlVAYVPQSEEVDWSFPVLVEDVVMMGRYGHM------GWLRRAKKR--DRQIVTAA---LARVDMVEFRHRQIGELSGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 161 QQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRThHNVSILLIEHDMKLVMGISDRIYVVnQGTPLANGt 240
Cdd:PRK15056 147 QKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRD-EGKTMLVSTHNLGSVTEFCDYTVMV-KGTVLASG- 223
|
...
gi 490378916 241 PSE 243
Cdd:PRK15056 224 PTE 226
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
5-248 |
2.67e-19 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 85.55 E-value: 2.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 5 TTPLLQVNGLTMRF----GGLLAVNNVELTINQGEIVSLIGPNGAGKT-TIFnCLTGFYKP---TSGTILYREKHLEGLT 76
Cdd:PRK09473 9 ADALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAF-ALMGLLAAngrIGGSATFNGREILNLP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 77 GQAIARLgviRTFQHVRLFKE--------MTVIENLLVAQHQHlksgifSGLLKTPAFrrAESEALDNAVKWLE---RVD 145
Cdd:PRK09473 88 EKELNKL---RAEQISMIFQDpmtslnpyMRVGEQLMEVLMLH------KGMSKAEAF--EESVRMLDAVKMPEarkRMK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 146 LLP--FANrqagnlayGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGI 223
Cdd:PRK09473 157 MYPheFSG--------GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGI 228
|
250 260
....*....|....*....|....*
gi 490378916 224 SDRIYVVNQGTPLANGTPSEIRQHP 248
Cdd:PRK09473 229 CDKVLVMYAGRTMEYGNARDVFYQP 253
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
8-244 |
3.77e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 84.37 E-value: 3.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 8 LLQVNGLTMRF---GGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTIlyrEKHLEGLTGQAI--AR 82
Cdd:PRK13642 4 ILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKV---KIDGELLTAENVwnLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 83 LGVIRTFQHV-RLFKEMTVIENLLVAQHQHlksgifsGLLKTPAFRRAESEALdnavkwleRVDLLPFANRQAGNLAYGQ 161
Cdd:PRK13642 81 RKIGMVFQNPdNQFVGATVEDDVAFGMENQ-------GIPREEMIKRVDEALL--------AVNMLDFKTREPARLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 162 QRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGiSDRIYVVNQGTPLANGTP 241
Cdd:PRK13642 146 KQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAP 224
|
...
gi 490378916 242 SEI 244
Cdd:PRK13642 225 SEL 227
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
6-233 |
6.10e-19 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 83.58 E-value: 6.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 6 TPLLQVNGLTMRF--GGLLA-------VNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLT 76
Cdd:PRK10419 1 MTLLNVSGLSHHYahGGLSGkhqhqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 77 GQAIA--RLGVIRTFQH-VRLFKEMTVIENLLVAQHQHLKSgifsgllKTPAFRRAESEALdnavkwLERVDLLP-FANR 152
Cdd:PRK10419 81 RAQRKafRRDIQMVFQDsISAVNPRKTVREIIREPLRHLLS-------LDKAERLARASEM------LRAVDLDDsVLDK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 153 QAGNLAYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQ 232
Cdd:PRK10419 148 RPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDN 227
|
.
gi 490378916 233 G 233
Cdd:PRK10419 228 G 228
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
23-252 |
6.51e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 83.70 E-value: 6.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 23 AVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKP-----TSGTILYREkhlegLTGQAI----ARLGVIrtFQHV- 92
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnpnSKITVDGIT-----LTAKTVwdirEKVGIV--FQNPd 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 93 RLFKEMTVIENLLVAqhqhlksgifsglLKTPAFRRAESEALDNAVkwLERVDLLPFANRQAGNLAYGQQRRLEIARCMV 172
Cdd:PRK13640 95 NQFVGATVGDDVAFG-------------LENRAVPRPEMIKIVRDV--LADVGMLDYIDSEPANLSGGQKQRVAIAGILA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 173 TRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGiSDRIYVVNQGTPLANGTPSEIRQHPDVIK 252
Cdd:PRK13640 160 VEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEIFSKVEMLK 238
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
18-248 |
9.47e-19 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 84.31 E-value: 9.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 18 FGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLtgqAIARLGVIRTFQHVRLFKE 97
Cdd:PRK11000 13 YGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDV---PPAERGVGMVFQSYALYPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 98 MTVIENLLVAqhqhLKsgiFSGLLKTPAFRRAEsealdNAVKWLERVDLLpfaNRQAGNLAYGQQRRLEIARCMVTRPEI 177
Cdd:PRK11000 90 LSVAENMSFG----LK---LAGAKKEEINQRVN-----QVAEVLQLAHLL---DRKPKALSGGQRQRVAIGRTLVAEPSV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 178 LMLDEPaaglnpketndLDDLIAELRTHHNVSI-----------LLIEHDMKLVMGISDRIYVVNQGTPLANGTPSEIRQ 246
Cdd:PRK11000 155 FLLDEP-----------LSNLDAALRVQMRIEIsrlhkrlgrtmIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYH 223
|
..
gi 490378916 247 HP 248
Cdd:PRK11000 224 YP 225
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
23-239 |
1.27e-18 |
|
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: 81.48 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 23 AVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILyrekhLEGLTgqaiarlgvIRTFQHVRLFKEMTvie 102
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVL-----LDGTD---------IRQLDPADLRRNIG--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 103 nlLVAQHQHLksgiFSGLLK---TPAFRRAESEALDNAVkwlERVDLLPFANRQAG-----------NLAYGQQRRLEIA 168
Cdd:cd03245 82 --YVPQDVTL----FYGTLRdniTLGAPLADDERILRAA---ELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490378916 169 RCMVTRPEILMLDEPAAGLnpketndldDLIAELRTHHNVS-------ILLIEHDMKLvMGISDRIYVVNQGTPLANG 239
Cdd:cd03245 153 RALLNDPPILLLDEPTSAM---------DMNSEERLKERLRqllgdktLIIITHRPSL-LDLVDRIIVMDSGRIVADG 220
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
23-243 |
1.50e-18 |
|
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: 81.89 E-value: 1.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 23 AVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIAR-LGVIRtfQHVRLFKEmTVI 101
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRqIGLVS--QDVFLFND-TVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 102 ENLLVAqhqhlksgifsgllkTPAFRRAESEALDNAVKWLERVDLLP-----FANRQAGNLAYGQQRRLEIARCMVTRPE 176
Cdd:cd03251 94 ENIAYG---------------RPGATREEVEEAARAANAHEFIMELPegydtVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 177 ILMLDEPAAGLNPKETNDLDDLIAEL---RThhnvsILLIEHDMKLVMGiSDRIYVVNQGTPLANGTPSE 243
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLmknRT-----TFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEE 222
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-248 |
2.33e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 82.07 E-value: 2.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 7 PLLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGtilYREKHLEGLTGQAI------ 80
Cdd:PRK14271 20 PAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSG---YRYSGDVLLGGRSIfnyrdv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 81 ----ARLGVIrtFQHVRLFKeMTVIENLL--VAQHQHLKSGIFSGLLKTpafrRAESEALDNAVKwlERVDLLPFanrqa 154
Cdd:PRK14271 97 lefrRRVGML--FQRPNPFP-MSIMDNVLagVRAHKLVPRKEFRGVAQA----RLTEVGLWDAVK--DRLSDSPF----- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 155 gNLAYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHhnVSILLIEHDMKLVMGISDRIYVVNQGT 234
Cdd:PRK14271 163 -RLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGR 239
|
250
....*....|....
gi 490378916 235 PLANGTPSEIRQHP 248
Cdd:PRK14271 240 LVEEGPTEQLFSSP 253
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
9-241 |
2.56e-18 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 80.62 E-value: 2.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRF--GGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYrekhleglTGQAIARLGVi 86
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILI--------DGVDISKIGL- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 87 rtfqHvRLFKEMTVIenllvAQHQHLksgiFSGLLKT---PaFRRAESEALDNAvkwLERVDLLPFANRQAG-------- 155
Cdd:cd03244 74 ----H-DLRSRISII-----PQDPVL----FSGTIRSnldP-FGEYSDEELWQA---LERVGLKEFVESLPGgldtvvee 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 156 ---NLAYGQQRRLEIARCMVTRPEILMLDEPAAGLNPkETndlDDLIAE-LRTH-HNVSILLIEHDMKLVMGiSDRIYVV 230
Cdd:cd03244 136 ggeNLSVGQRQLLCLARALLRKSKILVLDEATASVDP-ET---DALIQKtIREAfKDCTVLTIAHRLDTIID-SDRILVL 210
|
250
....*....|.
gi 490378916 231 NQGTPLANGTP 241
Cdd:cd03244 211 DKGRVVEFDSP 221
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-259 |
2.93e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 81.63 E-value: 2.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 24 VNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYK------PTSGTILYREKHLEGLTGQAIaRLGVIRTFQHVRLFKE 97
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKL-RKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 98 MTVIENLLVAQHQHlksgifsGLLKTPAFRRAESEALDNAVKWLERVDLLpfaNRQAGNLAYGQQRRLEIARCMVTRPEI 177
Cdd:PRK14246 105 LSIYDNIAYPLKSH-------GIKEKREIKKIVEECLRKVGLWKEVYDRL---NSPASQLSGGQQQRLTIARALALKPKV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 178 LMLDEPAAGLNPKETNDLDDLIAELRthHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPSEIRQHPdviKAYLGE 257
Cdd:PRK14246 175 LLMDEPTSMIDIVNSQAIEKLITELK--NEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSP---KNELTE 249
|
..
gi 490378916 258 AY 259
Cdd:PRK14246 250 KY 251
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
9-244 |
3.03e-18 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 81.04 E-value: 3.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRfGGLLAVNnveLTINQGEIVSLIGPNGAGKTTIFNCLTGFYkPTSGTILYREKHLEGLTGQAIARLgviRT 88
Cdd:COG4138 1 LQLNDVAVA-GRLGPIS---AQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARH---RA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 89 F--QHVRLFKEMTVIENLlvAQHQHLKsgifsgllktpafrrAESEALDNAVKWL-ERVDLLPFANRQAGNLAYGQQRRL 165
Cdd:COG4138 73 YlsQQQSPPFAMPVFQYL--ALHQPAG---------------ASSEAVEQLLAQLaEALGLEDKLSRPLTQLSGGEWQRV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 166 EIAR-CMVTRPEI------LMLDEPAAGLNPKETNDLDDLIAELrTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLAN 238
Cdd:COG4138 136 RLAAvLLQVWPTInpegqlLLLDEPMNSLDVAQQAALDRLLREL-CQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVAS 214
|
....*.
gi 490378916 239 GTPSEI 244
Cdd:COG4138 215 GETAEV 220
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
18-233 |
3.40e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 80.69 E-value: 3.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 18 FGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIA----RLGVIrtFQHVR 93
Cdd:PRK10908 12 LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPflrrQIGMI--FQDHH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 94 LFKEMTVIENLLVAQhqhlksgIFSGLlKTPAFRRAESEALDnavkwleRVDLLPFANRQAGNLAYGQQRRLEIARCMVT 173
Cdd:PRK10908 90 LLMDRTVYDNVAIPL-------IIAGA-SGDDIRRRVSAALD-------KVGLLDKAKNFPIQLSGGEQQRVGIARAVVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 174 RPEILMLDEPAAGLNPKETNDLDDLIAELrTHHNVSILLIEHDMKLVMGISDRIYVVNQG 233
Cdd:PRK10908 155 KPAVLLADEPTGNLDDALSEGILRLFEEF-NRVGVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
7-248 |
4.46e-18 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 82.06 E-value: 4.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 7 PLLQVNGLTMRFG-------------GLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLE 73
Cdd:PRK15079 7 VLLEVADLKVHFDikdgkqwfwqppkTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 74 GLTGQAI--ARLGVIRTFQH--VRLFKEMTVIEnllvaqhqhlksgIFSGLLKT--PAFRRAESEalDNAVKWLERVDLL 147
Cdd:PRK15079 87 GMKDDEWraVRSDIQMIFQDplASLNPRMTIGE-------------IIAEPLRTyhPKLSRQEVK--DRVKAMMLKVGLL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 148 P-FANRQAGNLAYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDR 226
Cdd:PRK15079 152 PnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDR 231
|
250 260
....*....|....*....|..
gi 490378916 227 IYVVNQGTPLANGTPSEIRQHP 248
Cdd:PRK15079 232 VLVMYLGHAVELGTYDEVYHNP 253
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
24-244 |
7.42e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 80.55 E-value: 7.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 24 VNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILyrekhlegLTGQAIARLGV--IR-----TFQHV-RLF 95
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQII--------IDGDLLTEENVwdIRhkigmVFQNPdNQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 96 KEMTV-------IENLLVAqHQHLKSGIfsgllktpafrraeSEALdnavkwlERVDLLPFANRQAGNLAYGQQRRLEIA 168
Cdd:PRK13650 95 VGATVeddvafgLENKGIP-HEEMKERV--------------NEAL-------ELVGMQDFKEREPARLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490378916 169 RCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVmGISDRIYVVNQGTPLANGTPSEI 244
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPREL 227
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
23-255 |
1.12e-17 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 79.36 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 23 AVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKH---LEgltgqaiarLGVIrtFQHvrlfkEMT 99
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVsalLE---------LGAG--FHP-----ELT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 100 VIENLlvaqhqhlksgIFSGLLKtpAFRRAESEALdnavkwLERV----DLLPFANRQAGNLAYGQQRRLEIARCMVTRP 175
Cdd:COG1134 105 GRENI-----------YLNGRLL--GLSRKEIDEK------FDEIvefaELGDFIDQPVKTYSSGMRARLAFAVATAVDP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 176 EILMLDEP-AAGlnpketnDLD------DLIAELRtHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPSEirqhp 248
Cdd:COG1134 166 DILLVDEVlAVG-------DAAfqkkclARIRELR-ESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEE----- 232
|
....*..
gi 490378916 249 dVIKAYL 255
Cdd:COG1134 233 -VIAAYE 238
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
6-246 |
1.90e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 81.31 E-value: 1.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 6 TPLLQVNGLTMRF----GGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIA 81
Cdd:PRK10535 2 TALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 82 RL-----GVIrtFQHVRLFKEMTVIENLLVaqhqhlkSGIFSGLLKTPafRRAESEALdnavkwLERVDLLPFANRQAGN 156
Cdd:PRK10535 82 QLrrehfGFI--FQRYHLLSHLTAAQNVEV-------PAVYAGLERKQ--RLLRAQEL------LQRLGLEDRVEYQPSQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 157 LAYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTH-HNVSIllIEHDmKLVMGISDRIYVVNQGTP 235
Cdd:PRK10535 145 LSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRgHTVII--VTHD-PQVAAQAERVIEIRDGEI 221
|
250
....*....|.
gi 490378916 236 LANGTPSEIRQ 246
Cdd:PRK10535 222 VRNPPAQEKVN 232
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
9-233 |
5.02e-17 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 76.20 E-value: 5.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRFGG--LLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIARLGVI 86
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 87 RtfQHVRLFkEMTVIENLlvaqhqhlksGI-FSGllktpafrraesealdnavkwlervdllpfanrqagnlayGQQRRL 165
Cdd:cd03247 81 N--QRPYLF-DTTLRNNL----------GRrFSG----------------------------------------GERQRL 107
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490378916 166 EIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAE-LRthhNVSILLIEHDMKlvmGIS--DRIYVVNQG 233
Cdd:cd03247 108 ALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEvLK---DKTLIWITHHLT---GIEhmDKILFLENG 172
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
22-233 |
5.15e-17 |
|
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: 77.51 E-value: 5.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 22 LAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKhlegltgqaiarlgVIRTFQHVRLFKEMTVI 101
Cdd:cd03248 28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGK--------------PISQYEHKYLHSKVSLV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 102 ENLLVAQHQHLKSGIFSGLLKTPAFRRAESEALDNAVKWLERVDLLPF--ANRQAGNLAYGQQRRLEIARCMVTRPEILM 179
Cdd:cd03248 94 GQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDteVGEKGSQLSGGQKQRVAIARALIRNPQVLI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490378916 180 LDEPAAGLNPKETNDLDDLIAElrTHHNVSILLIEHDMKLVMGiSDRIYVVNQG 233
Cdd:cd03248 174 LDEATSALDAESEQQVQQALYD--WPERRTVLVIAHRLSTVER-ADQILVLDGG 224
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-249 |
5.49e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 77.96 E-value: 5.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTI---FNCLTGfykptsgtiLYREKHLEG---LTGQAI-- 80
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLlrtFNRLLE---------LNEEARVEGevrLFGRNIys 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 81 -------ARLGVIRTFQHVRLFKEMTVIENLLVAqhqhLKsgiFSGLLKTPAFRRAESE-ALDNAVKWLERVDLLpfaNR 152
Cdd:PRK14267 76 pdvdpieVRREVGMVFQYPNPFPHLTIYDNVAIG----VK---LNGLVKSKKELDERVEwALKKAALWDEVKDRL---ND 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 153 QAGNLAYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHnvSILLIEHDMKLVMGISDRIYVVNQ 232
Cdd:PRK14267 146 YPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYL 223
|
250
....*....|....*..
gi 490378916 233 GTPLANGTPSEIRQHPD 249
Cdd:PRK14267 224 GKLIEVGPTRKVFENPE 240
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
26-253 |
5.92e-17 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 80.15 E-value: 5.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 26 NVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILyrekhlegLTGQAiarlgvIRTFQHVRLFKEMTvienlL 105
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVL--------LDGVP------LVQYDHHYLHRQVA-----L 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 106 VAQHQHLKSG-----IFSGLLKTPafrraESEALDNAVKWLERVDLLPFANR------QAGN-LAYGQQRRLEIARCMVT 173
Cdd:TIGR00958 560 VGQEPVLFSGsvrenIAYGLTDTP-----DEEIMAAAKAANAHDFIMEFPNGydtevgEKGSqLSGGQKQRIAIARALVR 634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 174 RPEILMLDEPAAGLNPKetndLDDLIAELRTHHNVSILLIEHDMKLVMGiSDRIYVVNQGTPLANGTPSEIRQHPDVIKA 253
Cdd:TIGR00958 635 KPRVLILDEATSALDAE----CEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQGCYKH 709
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
9-233 |
9.91e-17 |
|
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: 75.33 E-value: 9.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRFGGL--LAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILyrekhlegLTGQAIARLGV- 85
Cdd:cd03246 1 LEVENVSFRYPGAepPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVR--------LDGADISQWDPn 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 86 -IRTF-----QHVRLFkEMTVIENllvaqhqhlksgIFSGllktpafrraesealdnavkwlervdllpfanrqagnlay 159
Cdd:cd03246 73 eLGDHvgylpQDDELF-SGSIAEN------------ILSG---------------------------------------- 99
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490378916 160 GQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRThHNVSILLIEHDMKLVmGISDRIYVVNQG 233
Cdd:cd03246 100 GQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKA-AGATRIVIAHRPETL-ASADRILVLEDG 171
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-243 |
1.20e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 79.10 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 3 HITTPLLQVNGLTMRF--GGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAI 80
Cdd:PRK11160 333 AADQVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 81 -ARLGVIRtfQHVRLFKEmTVIENLLVAQHQhlksgifsgllktpafrrAESEALDNAvkwLERVDLLPFANRQAG---- 155
Cdd:PRK11160 413 rQAISVVS--QRVHLFSA-TLRDNLLLAAPN------------------ASDEALIEV---LQQVGLEKLLEDDKGlnaw 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 156 ------NLAYGQQRRLEIARCMVTRPEILMLDEPAAGLNpKETndlDDLIAELRTHH--NVSILLIEHDMKLvMGISDRI 227
Cdd:PRK11160 469 lgeggrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLD-AET---ERQILELLAEHaqNKTVLMITHRLTG-LEQFDRI 543
|
250
....*....|....*.
gi 490378916 228 YVVNQGTPLANGTPSE 243
Cdd:PRK11160 544 CVMDNGQIIEQGTHQE 559
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
7-248 |
1.31e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 79.13 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 7 PLLQVNGLTMRF---GGLL--------AVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGL 75
Cdd:PRK10261 312 PILQVRNLVTRFplrSGLLnrvtrevhAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 76 TGQAIA--RLGVIRTFQ--HVRLFKEMTVIENLLVAQHQHlksgifsGLLktpafrraESEALDNAVKWL-ERVDLLP-F 149
Cdd:PRK10261 392 SPGKLQalRRDIQFIFQdpYASLDPRQTVGDSIMEPLRVH-------GLL--------PGKAAAARVAWLlERVGLLPeH 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 150 ANRQAGNLAYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYV 229
Cdd:PRK10261 457 AWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAV 536
|
250 260
....*....|....*....|..
gi 490378916 230 VNQGTPLANGTPS---EIRQHP 248
Cdd:PRK10261 537 MYLGQIVEIGPRRavfENPQHP 558
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6-259 |
1.36e-16 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 79.29 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 6 TPLLQVNGLTMRFGGLL--AVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTilyrekhlEGLTGQAIARl 83
Cdd:TIGR01257 1935 TDILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGD--------ATVAGKSILT- 2005
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 84 GVIRTFQHVRLFKEMTVIENLLVAQhQHLKsgIFSGLLKTPAfrraesEALDNAVKW-LERVDLLPFANRQAGNLAYGQQ 162
Cdd:TIGR01257 2006 NISDVHQNMGYCPQFDAIDDLLTGR-EHLY--LYARLRGVPA------EEIEKVANWsIQSLGLSLYADRLAGTYSGGNK 2076
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 163 RRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELrTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPs 242
Cdd:TIGR01257 2077 RKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSI-IREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTI- 2154
|
250
....*....|....*..
gi 490378916 243 eirQHpdvIKAYLGEAY 259
Cdd:TIGR01257 2155 ---QH---LKSKFGDGY 2165
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
5-233 |
1.40e-16 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 76.60 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 5 TTPLLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGF--YKPTSGTILYREKHLEGLTGQAIAR 82
Cdd:CHL00131 4 NKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPEERAH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 83 LGVIRTFQHVRLFKEMTVIENLLVAQHQHLKsgiFSGLLKTPAFrraesEALDNAVKWLERVDLLP-FANRQAGN-LAYG 160
Cdd:CHL00131 84 LGIFLAFQYPIEIPGVSNADFLRLAYNSKRK---FQGLPELDPL-----EFLEIINEKLKLVGMDPsFLSRNVNEgFSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 161 QQRRLEIARCMVTRPEILMLDEPAAGLnpketnDLDDL--IAE----LRTHHNvSILLIEHDMKLVMGIS-DRIYVVNQG 233
Cdd:CHL00131 156 EKKRNEILQMALLDSELAILDETDSGL------DIDALkiIAEginkLMTSEN-SIILITHYQRLLDYIKpDYVHVMQNG 228
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
21-202 |
1.46e-16 |
|
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: 76.16 E-value: 1.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 21 LLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTG---FYKPTSGTILYRekhlegltGQAIARLGVIRTFQHVRLFKe 97
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFN--------GQPRKPDQFQKCVAYVRQDD- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 98 mTVIENLLVAQHQHlksgiFSGLLKTPA-FRRAESEALDnAVKWLERVDLLPFANRQAGNLAYGQQRRLEIARCMVTRPE 176
Cdd:cd03234 91 -ILLPGLTVRETLT-----YTAILRLPRkSSDAIRKKRV-EDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPK 163
|
170 180
....*....|....*....|....*.
gi 490378916 177 ILMLDEPAAGLNPKETNDLDDLIAEL 202
Cdd:cd03234 164 VLILDEPTSGLDSFTALNLVSTLSQL 189
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
8-258 |
3.18e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 75.98 E-value: 3.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 8 LLQVNGLTMRF---GGLL------AVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEglTGQ 78
Cdd:PRK15112 4 LLEVRNLSKTFryrTGWFrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH--FGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 79 AIARLGVIRTfqhvrLFKEMTVIENLLVAQHQHLKsgiFSGLLKTPAFRRAESEALDNAvkwLERVDLLP-FANRQAGNL 157
Cdd:PRK15112 82 YSYRSQRIRM-----IFQDPSTSLNPRQRISQILD---FPLRLNTDLEPEQREKQIIET---LRQVGLLPdHASYYPHML 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 158 AYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLA 237
Cdd:PRK15112 151 APGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVE 230
|
250 260
....*....|....*....|....*..
gi 490378916 238 NGTPSEIRQHP------DVIKAYLGEA 258
Cdd:PRK15112 231 RGSTADVLASPlheltkRLIAGHFGEA 257
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
8-231 |
5.47e-16 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 74.82 E-value: 5.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 8 LLQVNGLTMRFGG----LLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIARL 83
Cdd:PRK10584 6 IVEVHHLKKSVGQgeheLSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 84 ---GVIRTFQHVRLFKEMTVIENLlvaqhqhlksgifsgllKTPAFRRAESE--ALDNAVKWLERVDLLPFANRQAGNLA 158
Cdd:PRK10584 86 rakHVGFVFQSFMLIPTLNALENV-----------------ELPALLRGESSrqSRNGAKALLEQLGLGKRLDHLPAQLS 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490378916 159 YGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVN 231
Cdd:PRK10584 149 GGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVN 221
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
5-233 |
5.76e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 77.05 E-value: 5.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 5 TTPLLQVNGLTMRF--GGLL--AVNNVELTINQGEIVSLIGPNGAGKT-TIFNCLTGFYKP----TSGTILYR------- 68
Cdd:PRK15134 2 TQPLLAIENLSVAFrqQQTVrtVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHgesllha 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 69 -EKHLEGLTGQAIARLgvirtfqhvrlFKEMTVIENLLvaqhQHLKSGIFSGLLKTPAFRR--AESEALDnavkWLERVD 145
Cdd:PRK15134 82 sEQTLRGVRGNKIAMI-----------FQEPMVSLNPL----HTLEKQLYEVLSLHRGMRReaARGEILN----CLDRVG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 146 LLPFANRQAG---NLAYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMG 222
Cdd:PRK15134 143 IRQAAKRLTDyphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRK 222
|
250
....*....|.
gi 490378916 223 ISDRIYVVNQG 233
Cdd:PRK15134 223 LADRVAVMQNG 233
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
6-233 |
6.19e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 76.63 E-value: 6.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 6 TPLLQVNGLTMRfggllAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIARLGV 85
Cdd:PRK15439 266 APVLTVEDLTGE-----GFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 86 I-----RtfQHVRLFKEMTVIENLLVAQHQHLksgifsGLLKTPAFRRAESEALDNA--VKWLErvdllpfANRQAGNLA 158
Cdd:PRK15439 341 VylpedR--QSSGLYLDAPLAWNVCALTHNRR------GFWIKPARENAVLERYRRAlnIKFNH-------AEQAARTLS 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490378916 159 YGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELrTHHNVSILLIEHDMKLVMGISDRIYVVNQG 233
Cdd:PRK15439 406 GGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSI-AAQNVAVLFISSDLEEIEQMADRVLVMHQG 479
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
30-244 |
6.85e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 74.58 E-value: 6.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 30 TINQGEIVSLIGPNGAGKTTIFNCLTGFYkPTSGTILYREKHLEGLTGQAIARlgvIRTF--QHVRLFKEMTVIENLlvA 107
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELAR---HRAYlsQQQTPPFAMPVFQYL--T 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 108 QHQHLKsgifsgllktpafrrAESEALDNAVKWL-ERVDLLPFANRQAGNLAYGQ-QR-RLeIARCMVTRPEI------L 178
Cdd:PRK03695 92 LHQPDK---------------TRTEAVASALNEVaEALGLDDKLGRSVNQLSGGEwQRvRL-AAVVLQVWPDInpagqlL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490378916 179 MLDEPAAGLNPKETNDLDDLIAELrTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPSEI 244
Cdd:PRK03695 156 LLDEPMNSLDVAQQAALDRLLSEL-CQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEV 220
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
24-233 |
1.01e-15 |
|
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: 76.02 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 24 VNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPT-SGTILYREKHLEGLTGQAIARLGVIRTFQHVR---LFKEMT 99
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQAIRAGIAMVPEDRKrhgIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 100 VIENLLVAQhqhLKSgiFSGLLKTPAfrRAESEALDNAVKWLERVDLLPFAnrQAGNLAYGQQRRLEIARCMVTRPEILM 179
Cdd:TIGR02633 356 VGKNITLSV---LKS--FCFKMRIDA--AAELQIIGSAIQRLKVKTASPFL--PIGRLSGGNQQKAVLAKMLLTNPRVLI 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490378916 180 LDEPAAGLNPKETNDLDDLIAELrTHHNVSILLIEHDMKLVMGISDRIYVVNQG 233
Cdd:TIGR02633 427 LDEPTRGVDVGAKYEIYKLINQL-AQEGVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
23-233 |
1.01e-15 |
|
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: 73.72 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 23 AVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILyrekhlegLTGQAIARLGVIRTFQhvrlfKEMTVIE 102
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT--------VRGRVSSLLGLGGGFN-----PELTGRE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 103 NLlvaqhqhlksgIFSGLLKtpAFRRAESEALDNAVkwLERVDLLPFANRQAGNLAYGQQRRLEIARCMVTRPEILMLDE 182
Cdd:cd03220 104 NI-----------YLNGRLL--GLSRKEIDEKIDEI--IEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 183 P-AAGlnpketndlD--------DLIAELRThHNVSILLIEHDMKLVMGISDRIYVVNQG 233
Cdd:cd03220 169 VlAVG---------DaafqekcqRRLRELLK-QGKTVILVSHDPSSIKRLCDRALVLEKG 218
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
23-248 |
1.29e-15 |
|
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: 73.56 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 23 AVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKP----TSGTILYREKHLEGLtgqAIARLGVIRTFQHvrlfkEM 98
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGRPLLPL---SIRGRHIATIMQN-----PR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 99 TVIENLLVAQHQHLKSGIFSGLLKTPAFRRA----ESEALDNAVKWLErvdLLPFanrqagNLAYGQQRRLEIARCMVTR 174
Cdd:TIGR02770 73 TAFNPLFTMGNHAIETLRSLGKLSKQARALIlealEAVGLPDPEEVLK---KYPF------QLSGGMLQRVMIALALLLE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 175 PEILMLDEPaaglnpkeTNDLD--------DLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPSEIRQ 246
Cdd:TIGR02770 144 PPFLIADEP--------TTDLDvvnqarvlKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFY 215
|
..
gi 490378916 247 HP 248
Cdd:TIGR02770 216 NP 217
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
9-245 |
3.47e-15 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 74.00 E-value: 3.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAG--KTTIFNCLTGfykPTSGTILYRekhlegLTGQAIARLGVI 86
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRRPWR------F*TWCANRRALR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 87 RTfqhvrlfkemtvienllVAQHQHLKSG---IFSGLLKTPAFRR----AESEALDNAVKWLERVDLLPFANRQAGNLAY 159
Cdd:NF000106 85 RT-----------------IG*HRPVR*GrreSFSGRENLYMIGR*ldlSRKDARARADELLERFSLTEAAGRAAAKYSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 160 GQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELrTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANG 239
Cdd:NF000106 148 GMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSM-VRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADG 226
|
....*.
gi 490378916 240 TPSEIR 245
Cdd:NF000106 227 KVDELK 232
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
24-239 |
3.51e-15 |
|
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: 71.81 E-value: 3.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 24 VNNVELTINQGEIVSLIGPNGAGKTTIFNCLTG--FYKPTSGTILYREKHLEGLTGQAIarLGVIRtfQHVRLFKEMTVI 101
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLDKRSFRKI--IGYVP--QDDILHPTLTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 102 ENLLVAqhQHLKSgiFSGllktpafrraesealdnavkwlervdllpfanrqagnlayGQQRRLEIARCMVTRPEILMLD 181
Cdd:cd03213 101 ETLMFA--AKLRG--LSG----------------------------------------GERKRVSIALELVSNPSLLFLD 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490378916 182 EPAAGLNPKETNDLDDLIAELRtHHNVSILLIEHDMK-LVMGISDRIYVVNQGTPLANG 239
Cdd:cd03213 137 EPTSGLDSSSALQVMSLLRRLA-DTGRTIICSIHQPSsEIFELFDKLLLLSQGRVIYFG 194
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
24-256 |
4.08e-15 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 72.94 E-value: 4.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 24 VNNVELTINQGEIVSLIGPNGAGKTTIFNCLTG-FYKPT-------SGTILYREKHLEGLTGQAIARLGVIRTFQHVRLF 95
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGaprgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 96 KeMTVIENLLVAQHQHlksgifsgllktpAFRRAESEALDNAVKW--LERVDLLPFANRQAGNLAYGQQRRLEIARCM-- 171
Cdd:PRK13547 97 A-FSAREIVLLGRYPH-------------ARRAGALTHRDGEIAWqaLALAGATALVGRDVTTLSGGELARVQFARVLaq 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 172 -------VTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPSEI 244
Cdd:PRK13547 163 lwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
|
250
....*....|..
gi 490378916 245 RQhPDVIKAYLG 256
Cdd:PRK13547 243 LT-PAHIARCYG 253
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
6-216 |
1.12e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 70.90 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 6 TPLLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIaRLGV 85
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIY-RQQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 86 IRTFQHVRLFKEmTVIENLlvaqhqhlksgIFsgllktPAFRRAESEALDNAVKWLERVDL-LPFANRQAGNLAYGQQRR 164
Cdd:PRK10247 84 SYCAQTPTLFGD-TVYDNL-----------IF------PWQIRNQQPDPAIFLDDLERFALpDTILTKNIAELSGGEKQR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490378916 165 LEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHD 216
Cdd:PRK10247 146 ISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
5-248 |
2.14e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 72.43 E-value: 2.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 5 TTPLLQVNGLTMRF---GGLL--------AVNNVELTINQGEIVSLIGPNGAGKTTifnclTGF----YKPTSGTILYRE 69
Cdd:PRK15134 272 ASPLLDVEQLQVAFpirKGILkrtvdhnvVVKNISFTLRPGETLGLVGESGSGKST-----TGLallrLINSQGEIWFDG 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 70 KHLEGLTGQAIarLGVIRTFQHV----------RLFKEMTVIENLLVaqHQhlksgifsgllktPAFRRAESEAldNAVK 139
Cdd:PRK15134 347 QPLHNLNRRQL--LPVRHRIQVVfqdpnsslnpRLNVLQIIEEGLRV--HQ-------------PTLSAAQREQ--QVIA 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 140 WLERVDLLPFA-NRQAGNLAYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMK 218
Cdd:PRK15134 408 VMEEVGLDPETrHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLH 487
|
250 260 270
....*....|....*....|....*....|
gi 490378916 219 LVMGISDRIYVVNQGTPLANGTPSEIRQHP 248
Cdd:PRK15134 488 VVRALCHQVIVLRQGEVVEQGDCERVFAAP 517
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-242 |
3.92e-14 |
|
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: 69.74 E-value: 3.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 30 TINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILyrekhlegltgqaIARLGVIRTFQHVRLFKEMTVienllvaqh 109
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIE-------------IELDTVSYKPQYIKADYEGTV--------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 110 QHLKSGIFSGLLKTPAFRraeSEALdnavKWLERVDLLpfaNRQAGNLAYGQQRRLEIARCMVTRPEILMLDEPAAGLNP 189
Cdd:cd03237 79 RDLLSSITKDFYTHPYFK---TEIA----KPLQIEQIL---DREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490378916 190 KETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIyVVNQGTPLANGTPS 242
Cdd:cd03237 149 EQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRL-IVFEGEPSVNGVAN 200
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
8-233 |
4.15e-14 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 71.30 E-value: 4.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 8 LLQVNGLTMRfgGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIARLGVIR 87
Cdd:PRK10982 250 ILEVRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHGFAL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 88 TFQHVR---LFKEMTVIENLLVAQHQHLKSGIfsGLLKTpafRRAESEaldnaVKWLerVDLL----PFANRQAGNLAYG 160
Cdd:PRK10982 328 VTEERRstgIYAYLDIGFNSLISNIRNYKNKV--GLLDN---SRMKSD-----TQWV--IDSMrvktPGHRTQIGSLSGG 395
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490378916 161 QQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELrTHHNVSILLIEHDMKLVMGISDRIYVVNQG 233
Cdd:PRK10982 396 NQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAEL-AKKDKGIIIISSEMPELLGITDRILVMSNG 467
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
25-243 |
6.25e-14 |
|
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: 69.18 E-value: 6.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 25 NNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIAR-LGVIRtfQHVRLFKEmTVIEN 103
Cdd:cd03253 18 KDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRaIGVVP--QDTVLFND-TIGYN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 104 LlvaqhqhlksgifsgllktpAFRR--AESEALDNAVKWL---ERVDLLPFA-NRQAGN----LAYGQQRRLEIARCMVT 173
Cdd:cd03253 95 I--------------------RYGRpdATDEEVIEAAKAAqihDKIMRFPDGyDTIVGErglkLSGGEKQRVAIARAILK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490378916 174 RPEILMLDEPAAGLN-PKETNDLDDLIAELRthhNVSILLIEHDMKLVMGiSDRIYVVNQGTPLANGTPSE 243
Cdd:cd03253 155 NPPILLLDEATSALDtHTEREIQAALRDVSK---GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEE 221
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
8-248 |
6.98e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 71.04 E-value: 6.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 8 LLQVNGLTMRF----GGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTI-----LYREKHLE--GLT 76
Cdd:PRK10261 12 VLAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmLLRRRSRQviELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 77 GQAIARLGVIRTFQHVRLFKE-MTVIENLLVAQHQHLKS-GIFSGLlktpafrrAESEALDNAVKWLERVDLlPFA---- 150
Cdd:PRK10261 92 EQSAAQMRHVRGADMAMIFQEpMTSLNPVFTVGEQIAESiRLHQGA--------SREEAMVEAKRMLDQVRI-PEAqtil 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 151 NRQAGNLAYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVV 230
Cdd:PRK10261 163 SRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVM 242
|
250 260
....*....|....*....|.
gi 490378916 231 NQGTPLANGTPSEI---RQHP 248
Cdd:PRK10261 243 YQGEAVETGSVEQIfhaPQHP 263
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
25-243 |
7.94e-14 |
|
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: 68.72 E-value: 7.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 25 NNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILY-----REKHLEGLTGQaiarLGVIRtfQHVRLFkEMT 99
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLdgvdiRDLNLRWLRSQ----IGLVS--QEPVLF-DGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 100 VIENLLVaqhqhlksGIFSGLLKTPAFRRAESEALDNAVKWLERVDLLpfANRQAGNLAYGQQRRLEIARCMVTRPEILM 179
Cdd:cd03249 93 IAENIRY--------GKPDATDEEVEEAAKKANIHDFIMSLPDGYDTL--VGERGSQLSGGQKQRIAIARALLRNPKILL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490378916 180 LDEPAAGL---NPKETNDLDDLIAELRThhnvsILLIEHDMKLVMGiSDRIYVVNQGTPLANGTPSE 243
Cdd:cd03249 163 LDEATSALdaeSEKLVQEALDRAMKGRT-----TIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDE 223
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
13-244 |
9.83e-14 |
|
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: 68.67 E-value: 9.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 13 GLTMRFG--GLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYrEKHLEGLTGQAIARLGVIRTFQ 90
Cdd:cd03252 5 HVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLV-DGHDLALADPAWLRRQVGVVLQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 91 HVRLFKEmTVIENLLVAQHQHLKSGIF--SGLLKTPAFRRAESEALDNAVkwlervdllpfaNRQAGNLAYGQQRRLEIA 168
Cdd:cd03252 84 ENVLFNR-SIRDNIALADPGMSMERVIeaAKLAGAHDFISELPEGYDTIV------------GEQGAGLSGGQRQRIAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 169 RCMVTRPEILMLDEPAAGLnpketnDLDDLIAELRTHHNVS----ILLIEHDMKLVMGiSDRIYVVNQGTPLANGTPSEI 244
Cdd:cd03252 151 RALIHNPRILIFDEATSAL------DYESEHAIMRNMHDICagrtVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDEL 223
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
24-233 |
2.33e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.19 E-value: 2.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 24 VNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYK-PTSGTILYREKHLEGLT-GQAIA-----------RLGVIrtfq 90
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNpQQAIAqgiamvpedrkRDGIV---- 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 91 hvrlfKEMTVIENLLVAQhqhLKSGIFSGLLKTPAfrraESEALDNAVKWLERVDLLPFAnrQAGNLAYGQQRRLEIARC 170
Cdd:PRK13549 354 -----PVMGVGKNITLAA---LDRFTGGSRIDDAA----ELKTILESIQRLKVKTASPEL--AIARLSGGNQQKAVLAKC 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490378916 171 MVTRPEILMLDEPAAGLNPKETNDLDDLIAELrTHHNVSILLIEHDMKLVMGISDRIYVVNQG 233
Cdd:PRK13549 420 LLLNPKILILDEPTRGIDVGAKYEIYKLINQL-VQQGVAIIVISSELPEVLGLSDRVLVMHEG 481
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
22-244 |
2.82e-13 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 68.89 E-value: 2.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 22 LAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILY-----REKHLEGLTGQaiarlgVIRTFQHVRLFK 96
Cdd:PRK11176 357 PALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLdghdlRDYTLASLRNQ------VALVSQNVHLFN 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 97 EmTVIENLLVAQHQHlksgifsgllktpaFRRAESEA---LDNAVKWLERVD--LLPFANRQAGNLAYGQQRRLEIARCM 171
Cdd:PRK11176 431 D-TIANNIAYARTEQ--------------YSREQIEEaarMAYAMDFINKMDngLDTVIGENGVLLSGGQRQRIAIARAL 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490378916 172 VTRPEILMLDEPAAGLNPKETNDLDDLIAELRThhNVSILLIEHDMKLVMGiSDRIYVVNQGTPLANGTPSEI 244
Cdd:PRK11176 496 LRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAEL 565
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
9-241 |
3.18e-13 |
|
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: 66.67 E-value: 3.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRFGGLL--AVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILyrekhlegLTGQAIARLGVi 86
Cdd:cd03369 7 IEVENLSVRYAPDLppVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIE--------IDGIDISTIPL- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 87 rtfqhVRLFKEMTVIenllvAQHQHLksgiFSGLLKT--PAFRRAESEALDNAVKWLERVDllpfanrqagNLAYGQQRR 164
Cdd:cd03369 78 -----EDLRSSLTII-----PQDPTL----FSGTIRSnlDPFDEYSDEEIYGALRVSEGGL----------NLSQGQRQL 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490378916 165 LEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRThhNVSILLIEHDMKLVMGIsDRIYVVNQGTPLANGTP 241
Cdd:cd03369 134 LCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFT--NSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDHP 207
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
23-247 |
4.21e-13 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 68.45 E-value: 4.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 23 AVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIAR-LGVIrtFQHVRLFKEmTVI 101
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRnIAVV--FQDAGLFNR-SIE 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 102 ENLLV----AQHQHLKSgifsgllktpAFRRAesEALDNAVKWLERVDLLpfANRQAGNLAYGQQRRLEIARCMVTRPEI 177
Cdd:PRK13657 427 DNIRVgrpdATDEEMRA----------AAERA--QAHDFIERKPDGYDTV--VGERGRQLSGGERQRLAIARALLKDPPI 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 178 LMLDEPAAGLNPKETNDLDDLIAELRthHNVSILLIEHDMKLVMGiSDRIYVVNQGTPLANGTPSEIRQH 247
Cdd:PRK13657 493 LILDEATSALDVETEAKVKAALDELM--KGRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGSFDELVAR 559
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-257 |
5.24e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 68.33 E-value: 5.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 20 GLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYkPTSGTILYREKHLEGLT----GQAIARLGvirtfQHVRLF 95
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDpeswRKHLSWVG-----QNPQLP 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 96 KEmTVIENLLVAQHQhlksgifsgllktpafrrAESEALDNAvkwLERVDLLPFANR-----------QAGNLAYGQQRR 164
Cdd:PRK11174 436 HG-TLRDNVLLGNPD------------------ASDEQLQQA---LENAWVSEFLPLlpqgldtpigdQAAGLSVGQAQR 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 165 LEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHnvSILLIEH---DMKLVmgisDRIYVVNQGTPLANGTP 241
Cdd:PRK11174 494 LALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQ--TTLMVTHqleDLAQW----DQIWVMQDGQIVQQGDY 567
|
250
....*....|....*.
gi 490378916 242 SEIRQHPDVIKAYLGE 257
Cdd:PRK11174 568 AELSQAGGLFATLLAH 583
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
19-248 |
6.05e-13 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 67.56 E-value: 6.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 19 GGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILyrekhlegLTGQAIARL-----GVIRTFQHVR 93
Cdd:PRK11650 15 GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIW--------IGGRVVNELepadrDIAMVFQNYA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 94 LFKEMTVIENLLVAqhqhlksgifsglLKTPAFRRAESEA-LDNAVKWLErvdLLPFANRQAGNLAYGQQRRLEIARCMV 172
Cdd:PRK11650 87 LYPHMSVRENMAYG-------------LKIRGMPKAEIEErVAEAARILE---LEPLLDRKPRELSGGQRQRVAMGRAIV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 173 TRPEILMLDEPaaglnpketndLDDLIAELRTHHNVSI-----------LLIEHDMKLVMGISDRIYVVNQGTPLANGTP 241
Cdd:PRK11650 151 REPAVFLFDEP-----------LSNLDAKLRVQMRLEIqrlhrrlkttsLYVTHDQVEAMTLADRVVVMNGGVAEQIGTP 219
|
....*..
gi 490378916 242 SEIRQHP 248
Cdd:PRK11650 220 VEVYEKP 226
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
9-244 |
1.67e-12 |
|
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: 66.70 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRFGG--LLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILyrekhLEGLT---------G 77
Cdd:COG4618 331 LSVENLTVVPPGskRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVR-----LDGADlsqwdreelG 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 78 QAIARLGvirtfQHVRLFkEMTVIENllVAQhqhlksgifsgllktpaFRRAESEALDNAVKwleRVDL------LPFA- 150
Cdd:COG4618 406 RHIGYLP-----QDVELF-DGTIAEN--IAR-----------------FGDADPEKVVAAAK---LAGVhemilrLPDGy 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 151 ----NRQAGNLAYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRThHNVSILLIEHDMKLvMGISDR 226
Cdd:COG4618 458 dtriGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKA-RGATVVVITHRPSL-LAAVDK 535
|
250
....*....|....*...
gi 490378916 227 IYVVNQGTPLANGTPSEI 244
Cdd:COG4618 536 LLVLRDGRVQAFGPRDEV 553
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
23-189 |
1.68e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 66.53 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 23 AVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILyrekhlegLTGQAIArlgvirtfqhvrlfkemtvIE 102
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEIL--------LDGKPVT-------------------AE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 103 NLlvAQHQHLKSGIFSGL-----LKTPAFRRAESEALDnavKWLERVDL---LPFANRQAGN--LAYGQQRRLEIARCMV 172
Cdd:PRK10522 391 QP--EDYRKLFSAVFTDFhlfdqLLGPEGKPANPALVE---KWLERLKMahkLELEDGRISNlkLSKGQKKRLALLLALA 465
|
170
....*....|....*..
gi 490378916 173 TRPEILMLDEPAAGLNP 189
Cdd:PRK10522 466 EERDILLLDEWAADQDP 482
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
9-65 |
1.92e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 66.50 E-value: 1.92e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 490378916 9 LQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTI 65
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI 379
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
25-243 |
4.34e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 65.45 E-value: 4.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 25 NNVELTINQGEIVSLIGPNGAGKTTIFNCLTgFYKPT----SGTILyrekhlegLTGQAIAR--LGVIRTF--QHVRLFK 96
Cdd:TIGR00955 42 KNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVL--------LNGMPIDAkeMRAISAYvqQDDLFIP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 97 EMTVIENLlvaqhqhlksgIFSGLLKTPafRRAESEALDNAVK-WLERVDLLPFANRQAG------NLAYGQQRRLEIAR 169
Cdd:TIGR00955 113 TLTVREHL-----------MFQAHLRMP--RRVTKKEKRERVDeVLQALGLRKCANTRIGvpgrvkGLSGGERKRLAFAS 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490378916 170 CMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTPSE 243
Cdd:TIGR00955 180 ELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQ 253
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
9-65 |
5.73e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 65.14 E-value: 5.73e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 490378916 9 LQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTI 65
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI 381
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
20-256 |
8.26e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 63.47 E-value: 8.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 20 GLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYRekhleGLTGQAIARLGVIR-----TFQHVRL 94
Cdd:PRK13644 14 GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVS-----GIDTGDFSKLQGIRklvgiVFQNPET 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 95 -FKEMTVIENLLVAQHQhlksgifsgLLKTPAFRRaesEALDNAvkwLERVDLLPFANRQAGNLAYGQQRRLEIARCMVT 173
Cdd:PRK13644 89 qFVGRTVEEDLAFGPEN---------LCLPPIEIR---KRVDRA---LAEIGLEKYRHRSPKTLSGGQGQCVALAGILTM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 174 RPEILMLDEPAAGLNPKETNDLDDLIAELRtHHNVSILLIEHDMKlVMGISDRIYVVNQGTPLANGTPSEIRQHPDVikA 253
Cdd:PRK13644 154 EPECLIFDEVTSMLDPDSGIAVLERIKKLH-EKGKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVLSDVSL--Q 229
|
...
gi 490378916 254 YLG 256
Cdd:PRK13644 230 TLG 232
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
34-245 |
8.35e-12 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 63.54 E-value: 8.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 34 GEIVSLIGPNGAGKTTIFNCLTGFYKPTSG---------TIL----------YREKHLEGltgqaiaRLGVIRTFQHVrl 94
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGkfddppdwdEILdefrgselqnYFTKLLEG-------DVKVIVKPQYV-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 95 fkemtvieNLLVAQHQhlksGIFSGLLKtpafRRAESEALDNAVKWLErvdLLPFANRQAGNLAYGQQRRLEIARCMVTR 174
Cdd:cd03236 97 --------DLIPKAVK----GKVGELLK----KKDERGKLDELVDQLE---LRHVLDRNIDQLSGGELQRVAIAAALARD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490378916 175 PEILMLDEPAAGLNPKETNDLDDLIAELRTHHNvSILLIEHDMKLVMGISDRIYVVnQGTPLANGT---PSEIR 245
Cdd:cd03236 158 ADFYFFDEPSSYLDIKQRLNAARLIRELAEDDN-YVLVVEHDLAVLDYLSDYIHCL-YGEPGAYGVvtlPKSVR 229
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
6-206 |
1.49e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 63.88 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 6 TPLLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYkPTSGT---ILYREKHLEGLTGQAIAR 82
Cdd:PRK10938 258 EPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDH-PQGYSndlTLFGRRRGSGETIWDIKK 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 83 -LGVIRTFQHVRlFKEMTVIENLlvaqhqhlksgIFSGLLKTPAFRRAESEALDN-AVKWLervDLLPFANRQAG----N 156
Cdd:PRK10938 337 hIGYVSSSLHLD-YRVSTSVRNV-----------ILSGFFDSIGIYQAVSDRQQKlAQQWL---DILGIDKRTADapfhS 401
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490378916 157 LAYGQQRRLEIARCMVTRPEILMLDEPAAGLNPkeTND------LDDLIAELRT------HH 206
Cdd:PRK10938 402 LSWGQQRLALIVRALVKHPTLLILDEPLQGLDP--LNRqlvrrfVDVLISEGETqllfvsHH 461
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
25-236 |
1.56e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 62.28 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 25 NNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYK--PTSGTILYREKHLEgltgqaiarlgvirtfqhvrlfKEMTVIE 102
Cdd:COG2401 47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFG----------------------REASLID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 103 NLLVAQHQHLKSGIFS--GLLKTPAFRRaesealdnavkwlervdllPFAnrqagNLAYGQQRRLEIARCMVTRPEILML 180
Cdd:COG2401 105 AIGRKGDFKDAVELLNavGLSDAVLWLR-------------------RFK-----ELSTGQKFRFRLALLLAERPKLLVI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490378916 181 DEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGIS-DRIYVVNQGTPL 236
Cdd:COG2401 161 DEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDVIDDLQpDLLIFVGYGGVP 217
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
5-248 |
2.92e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 62.29 E-value: 2.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 5 TTPLLQVNGLTMRF---GGLL-------AVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEG 74
Cdd:PRK11308 2 QQPLLQAIDLKKHYpvkRGLFkperlvkALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 75 LTGQAIARLGviRTFQHV----------RLFKEMTVIENLLvaqhqhlksgIFSGLlkTPAFRRAESEALdnavkwLERV 144
Cdd:PRK11308 82 ADPEAQKLLR--QKIQIVfqnpygslnpRKKVGQILEEPLL----------INTSL--SAAERREKALAM------MAKV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 145 DLLP-FANRQAGNLAYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGI 223
Cdd:PRK11308 142 GLRPeHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHI 221
|
250 260
....*....|....*....|....*
gi 490378916 224 SDRIYVVNQGTPLANGTPSEIRQHP 248
Cdd:PRK11308 222 ADEVMVMYLGRCVEKGTKEQIFNNP 246
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
9-227 |
3.80e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 62.60 E-value: 3.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQaiarlgvirt 88
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQ---------- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 89 fQHVRLFKE-MTVIEnlLVAQHQHLKSGifsgllktpafrraesealDNAVK-WLERvdlLPF----ANRQAGNLAYGQQ 162
Cdd:PRK15064 390 -DHAYDFENdLTLFD--WMSQWRQEGDD-------------------EQAVRgTLGR---LLFsqddIKKSVKVLSGGEK 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490378916 163 RRLEIARCMVTRPEILMLDEPaaglnpkeTNDLD-DLIAELRT---HHNVSILLIEHDMKLVMGISDRI 227
Cdd:PRK15064 445 GRMLFGKLMMQKPNVLVMDEP--------TNHMDmESIESLNMaleKYEGTLIFVSHDREFVSSLATRI 505
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-245 |
3.81e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.52 E-value: 3.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 30 TINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKhlegltgqaiarlgVIRTFQHVRLFKEMTVIENLlvaqh 109
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK--------------ISYKPQYIKPDYDGTVEDLL----- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 110 qhlksgifsgllktpafrRAESEALDNAVKWLE---RVDLLPFANRQAGNLAYGQQRRLEIARCMVTRPEILMLDEPAAG 186
Cdd:PRK13409 422 ------------------RSITDDLGSSYYKSEiikPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAH 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490378916 187 LNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIyVVNQGTPLANGT---PSEIR 245
Cdd:PRK13409 484 LDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRL-MVFEGEPGKHGHasgPMDMR 544
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
7-248 |
4.39e-11 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 61.85 E-value: 4.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 7 PLLQVNGLTMRF----GGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKP----TSGTILYREKHLEGLTGQ 78
Cdd:COG4170 2 PLLDIRNLTIEIdtpqGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 79 AiaRLGVIRtfqhvrlfKEMTVIenllvAQH------------QHLKSGIFSGLLKTPAFRRAeSEALDNAVKWLERV-- 144
Cdd:COG4170 82 E--RRKIIG--------REIAMI-----FQEpsscldpsakigDQLIEAIPSWTFKGKWWQRF-KWRKKRAIELLHRVgi 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 145 -------DLLPFanrqagNLAYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDM 217
Cdd:COG4170 146 kdhkdimNSYPH------ELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDL 219
|
250 260 270
....*....|....*....|....*....|.
gi 490378916 218 KLVMGISDRIYVVNQGTPLANGTPSEIRQHP 248
Cdd:COG4170 220 ESISQWADTITVLYCGQTVESGPTEQILKSP 250
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
24-188 |
4.72e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 62.59 E-value: 4.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 24 VNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTS--GTILYREKHlegLTGQAIARLGVIRtfQHVRLFKEMTVI 101
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRK---PTKQILKRTGFVT--QDDILYPHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 102 ENLlvaqhqhlksgIFSGLLKTP-AFRRAESEALDNAVkwLERVDLLPFANRQAGN-----LAYGQQRRLEIARCMVTRP 175
Cdd:PLN03211 159 ETL-----------VFCSLLRLPkSLTKQEKILVAESV--ISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINP 225
|
170
....*....|...
gi 490378916 176 EILMLDEPAAGLN 188
Cdd:PLN03211 226 SLLILDEPTSGLD 238
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
19-233 |
4.82e-11 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 62.57 E-value: 4.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 19 GGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTI---------LYREKHLEGLTGQAIARLGVIRTF 89
Cdd:PLN03073 520 GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVfrsakvrmaVFSQHHVDGLDLSSNPLLYMMRCF 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 90 QhvrlfkemTVIENLLVAqhqHLKS-GIFSGLLKTPAFrraesealdnavkwlervdllpfanrqagNLAYGQQRRLEIA 168
Cdd:PLN03073 600 P--------GVPEQKLRA---HLGSfGVTGNLALQPMY-----------------------------TLSGGQKSRVAFA 639
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490378916 169 RCMVTRPEILMLDEPAAGLnpketnDLD---DLIAELRTHHNvSILLIEHDMKLVMGISDRIYVVNQG 233
Cdd:PLN03073 640 KITFKKPHILLLDEPSNHL------DLDaveALIQGLVLFQG-GVLMVSHDEHLISGSVDELWVVSEG 700
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
5-245 |
5.83e-11 |
|
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: 62.11 E-value: 5.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 5 TTPLLQVNGLTMRFGGL-LAVNnvELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKhlegltgqaiarl 83
Cdd:COG1245 338 EETLVEYPDLTKSYGGFsLEVE--GGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK------------- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 84 gVIRTFQHVRLFKEMTVIENLlvaqHQHLKSGIFSGLLKTPAFRRAEsealdnavkwLERvdLLpfaNRQAGNLAYGQQR 163
Cdd:COG1245 403 -ISYKPQYISPDYDGTVEEFL----RSANTDDFGSSYYKTEIIKPLG----------LEK--LL---DKNVKDLSGGELQ 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 164 RLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNqGTPLANGT--- 240
Cdd:COG1245 463 RVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMVFE-GEPGVHGHasg 541
|
....*
gi 490378916 241 PSEIR 245
Cdd:COG1245 542 PMDMR 546
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
10-247 |
5.93e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 62.06 E-value: 5.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 10 QVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTI------LYREKHLEGLTGQaIAR- 82
Cdd:NF033858 3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVevlggdMADARHRRAVCPR-IAYm 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 83 ---LGvirtfqhvR-LFKEMTVIENLLvaqhqhlksgiFSGLL--KTPAFRRAESEALdnavkwLERVDLLPFANRQAGN 156
Cdd:NF033858 82 pqgLG--------KnLYPTLSVFENLD-----------FFGRLfgQDAAERRRRIDEL------LRATGLAPFADRPAGK 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 157 LAYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHH-NVSILLIEHDMK-------LVMgisdriy 228
Cdd:NF033858 137 LSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERpGMSVLVATAYMEeaerfdwLVA------- 209
|
250
....*....|....*....
gi 490378916 229 vVNQGTPLANGTPSEIRQH 247
Cdd:NF033858 210 -MDAGRVLATGTPAELLAR 227
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
9-185 |
1.22e-10 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 60.97 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRF-----GGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILyrekhlegLTGQAIARl 83
Cdd:COG4615 328 LELRGVTYRYpgedgDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEIL--------LDGQPVTA- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 84 gvirtfqhvrlfkemtviENLlvAQHQHLKSGIFSG--LlktpaFRR---AESEALDNAV-KWLERVDL---LPFANRQA 154
Cdd:COG4615 399 ------------------DNR--EAYRQLFSAVFSDfhL-----FDRllgLDGEADPARArELLERLELdhkVSVEDGRF 453
|
170 180 190
....*....|....*....|....*....|....*...
gi 490378916 155 GNLAY--GQQRRLeiArcMVT-----RPeILMLDEPAA 185
Cdd:COG4615 454 STTDLsqGQRKRL--A--LLValledRP-ILVFDEWAA 486
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
27-233 |
1.41e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 60.70 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 27 VELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLE-GLTGQAIaRLGVI-----RTFQ---HVRlfke 97
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDiRSPRDAI-RAGIMlcpedRKAEgiiPVH---- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 98 mTVIENL-LVAQHQHLKSGIFSGllktpafRRAESEaldNAVKWLERVDL-LPFANRQAGNLAYGQQRRLEIARCMVTRP 175
Cdd:PRK11288 347 -SVADNInISARRHHLRAGCLIN-------NRWEAE---NADRFIRSLNIkTPSREQLIMNLSGGNQQKAILGRWLSEDM 415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490378916 176 EILMLDEPAAGLNPKETNDLDDLIAELrTHHNVSILLIEHDMKLVMGISDRIYVVNQG 233
Cdd:PRK11288 416 KVILLDEPTRGIDVGAKHEIYNVIYEL-AAQGVAVLFVSSDLPEVLGVADRIVVMREG 472
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
9-240 |
1.75e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 60.89 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRF-GGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQaiarlgVIR 87
Cdd:PRK10790 341 IDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHS------VLR 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 88 tfQHVRLFKEMTVIenllvaqhqhLKSGIFSGLlktpAFRRAESEAldnAVkW--LERVDLLPFANR-----------QA 154
Cdd:PRK10790 415 --QGVAMVQQDPVV----------LADTFLANV----TLGRDISEE---QV-WqaLETVQLAELARSlpdglytplgeQG 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 155 GNLAYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHhnVSILLIEHDMKLVMGiSDRIYVVNQGT 234
Cdd:PRK10790 475 NNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAHRLSTIVE-ADTILVLHRGQ 551
|
....*.
gi 490378916 235 PLANGT 240
Cdd:PRK10790 552 AVEQGT 557
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
3-204 |
1.90e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 59.09 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 3 HITTPLLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTIlyrekHLEGLTGQAIAR 82
Cdd:PRK13543 6 HTAPPLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQI-----QIDGKTATRGDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 83 LGVIRTFQHVRLFK-EMTVIENLlvaqhqHLKSGIFSgllktpafRRAEsEALDNAvkwLERVDLLPFANRQAGNLAYGQ 161
Cdd:PRK13543 81 SRFMAYLGHLPGLKaDLSTLENL------HFLCGLHG--------RRAK-QMPGSA---LAIVGLAGYEDTLVRQLSAGQ 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490378916 162 QRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLI-AELRT 204
Cdd:PRK13543 143 KKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMIsAHLRG 186
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-246 |
2.20e-10 |
|
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: 60.73 E-value: 2.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 22 LAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILyrekhlegLTGQAIARLGVirtfqHVRLFKeMTVI 101
Cdd:TIGR00957 1300 LVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEII--------IDGLNIAKIGL-----HDLRFK-ITII 1365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 102 ENLLVaqhqhlksgIFSGLLKT---PAFRRAESEaldnaVKW-LERVDLLPFANRQAG-----------NLAYGQQRRLE 166
Cdd:TIGR00957 1366 PQDPV---------LFSGSLRMnldPFSQYSDEE-----VWWaLELAHLKTFVSALPDkldhecaeggeNLSVGQRQLVC 1431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 167 IARCMVTRPEILMLDEPAAGLNpKETndlDDLI-AELRTH-HNVSILLIEHDMKLVMGISdRIYVVNQGTPLANGTPSEI 244
Cdd:TIGR00957 1432 LARALLRKTKILVLDEATAAVD-LET---DNLIqSTIRTQfEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNL 1506
|
..
gi 490378916 245 RQ 246
Cdd:TIGR00957 1507 LQ 1508
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
9-244 |
2.24e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 59.89 E-value: 2.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNgLTMRFGGL-LAVNnveLTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGlTGQAIA------ 81
Cdd:PRK11144 2 LELN-FKQQLGDLcLTVN---LTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFD-AEKGIClppekr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 82 RLGVIrtFQHVRLFKEMTVIENLlvaqhqhlKSGIfsgllktpafRRAESEALDNAVKWLervDLLPFANRQAGNLAYGQ 161
Cdd:PRK11144 77 RIGYV--FQDARLFPHYKVRGNL--------RYGM----------AKSMVAQFDKIVALL---GIEPLLDRYPGSLSGGE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 162 QRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVNQGTPLANGTP 241
Cdd:PRK11144 134 KQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPL 213
|
...
gi 490378916 242 SEI 244
Cdd:PRK11144 214 EEV 216
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
7-248 |
3.24e-10 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 59.43 E-value: 3.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 7 PLLQVNGLTMRF----GGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKP----TSGTILYREKHLEGLTGQ 78
Cdd:PRK15093 2 PLLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLRLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 79 AiaRLGVIRtfQHVRL-FKEMTVIENLLVAQHQHLKSGIFSGLLKTPAFRRAESEaLDNAVKWLERVDL---------LP 148
Cdd:PRK15093 82 E--RRKLVG--HNVSMiFQEPQSCLDPSERVGRQLMQNIPGWTYKGRWWQRFGWR-KRRAIELLHRVGIkdhkdamrsFP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 149 FanrqagNLAYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIY 228
Cdd:PRK15093 157 Y------ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKIN 230
|
250 260
....*....|....*....|
gi 490378916 229 VVNQGTPLANGTPSEIRQHP 248
Cdd:PRK15093 231 VLYCGQTVETAPSKELVTTP 250
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
8-248 |
3.80e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 58.98 E-value: 3.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 8 LLQVNGLTMRFGG----LLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYK----------PTSGTILYR--EKH 71
Cdd:PRK11022 3 LLNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrvmaeklEFNGQDLQRisEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 72 LEGLTGQAIARLgvirtFQhvrlfKEMT-----------VIENLLVaqHQhlksgifSGLLKTpafRRAESEALDNAVKW 140
Cdd:PRK11022 83 RRNLVGAEVAMI-----FQ-----DPMTslnpcytvgfqIMEAIKV--HQ-------GGNKKT---RRQRAIDLLNQVGI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 141 LE---RVDLLPFanrqagNLAYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDM 217
Cdd:PRK11022 141 PDpasRLDVYPH------QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDL 214
|
250 260 270
....*....|....*....|....*....|.
gi 490378916 218 KLVMGISDRIYVVNQGTPLANGTPSEIRQHP 248
Cdd:PRK11022 215 ALVAEAAHKIIVMYAGQVVETGKAHDIFRAP 245
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
33-230 |
5.31e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 59.41 E-value: 5.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 33 QGEIVSLIGPNGAGKTTIFNCLTGFYKPT-----------------SGTILYreKHLEGLTGQAIArlgVIRTFQHV--- 92
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNlgdydeepswdevlkrfRGTELQ--DYFKKLANGEIK---VAHKPQYVdli 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 93 -RLFKEmTVIEnllvaqhqhlksgifsgLLKtpafRRAESEALDNAVkwlERVDLLPFANRQAGNLAYGQQRRLEIARCM 171
Cdd:COG1245 173 pKVFKG-TVRE-----------------LLE----KVDERGKLDELA---EKLGLENILDRDISELSGGELQRVAIAAAL 227
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490378916 172 VTRPEILMLDEPAAGLNPKETNDLDDLIAELrTHHNVSILLIEHDMKLVMGISDRIYVV 230
Cdd:COG1245 228 LRDADFYFFDEPSSYLDIYQRLNVARLIREL-AEEGKYVLVVEHDLAILDYLADYVHIL 285
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-239 |
7.69e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 58.67 E-value: 7.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 30 TINQGEIVSLIGPNGAGKTTIFNCLTGFYKPT-----------------SGTILYreKHLEGLTGQAIArlgVIRTFQHV 92
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNlgdyeeepswdevlkrfRGTELQ--NYFKKLYNGEIK---VVHKPQYV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 93 ----RLFKEmTVIEnllvaqhqhlksgifsgLLKtpafRRAESEALDNAVkwlERVDLLPFANRQAGNLAYGQQRRLEIA 168
Cdd:PRK13409 170 dlipKVFKG-KVRE-----------------LLK----KVDERGKLDEVV---ERLGLENILDRDISELSGGELQRVAIA 224
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490378916 169 RCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRThhNVSILLIEHDMKLVMGISDRIYVVnQGTPLANG 239
Cdd:PRK13409 225 AALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAE--GKYVLVVEHDLAVLDYLADNVHIA-YGEPGAYG 292
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
5-233 |
6.07e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 55.95 E-value: 6.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 5 TTPLLQVNGLTMRFGGllAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIARLG 84
Cdd:PRK09700 262 HETVFEVRNVTSRDRK--KVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 85 VIRTFQHVR---LFKEMTVIENLLVAqhQHLKSGIFSGLL----KTPAFRRAESEALDNAVKWLErvdllpfANRQAGNL 157
Cdd:PRK09700 340 MAYITESRRdngFFPNFSIAQNMAIS--RSLKDGGYKGAMglfhEVDEQRTAENQRELLALKCHS-------VNQNITEL 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490378916 158 AYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELrTHHNVSILLIEHDMKLVMGISDRIYVVNQG 233
Cdd:PRK09700 411 SGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAVFCEG 485
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
151-255 |
8.12e-09 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 55.99 E-value: 8.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 151 NRQAGNLAYGQQRRLEIARCM------VTrpeiLMLDEPAAGLNPKETNDLDDLIAELRTHHNvSILLIEHDMKLVmGIS 224
Cdd:PRK00635 471 ERALATLSGGEQERTALAKHLgaeligIT----YILDEPSIGLHPQDTHKLINVIKKLRDQGN-TVLLVEHDEQMI-SLA 544
|
90 100 110
....*....|....*....|....*....|....*...
gi 490378916 225 DRIYVVNQGTP------LANGTPSEIRQHPDVIKA-YL 255
Cdd:PRK00635 545 DRIIDIGPGAGifggevLFNGSPREFLAKSDSLTAkYL 582
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
9-249 |
8.64e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 54.71 E-value: 8.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRFGGLLaVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKP----TSGTILyrekhlegLTGQAIARlg 84
Cdd:PRK10418 5 IELRNIALQAAQPL-VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVL--------LDGKPVAP-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 85 virtfQHVRLFKEMTVIEN-------LLVAQHQHLKSGIFSGLLKTPAFRRAESEA--LDNAvkwlERV-DLLPFanrqa 154
Cdd:PRK10418 74 -----CALRGRKIATIMQNprsafnpLHTMHTHARETCLALGKPADDATLTAALEAvgLENA----ARVlKLYPF----- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 155 gNLAYGQQRRLEIARCMVTRPEILMLDEPaaglnpkeTNDLD--------DLIAELRTHHNVSILLIEHDMKLVMGISDR 226
Cdd:PRK10418 140 -EMSGGMLQRMMIALALLCEAPFIIADEP--------TTDLDvvaqarilDLLESIVQKRALGMLLVTHDMGVVARLADD 210
|
250 260
....*....|....*....|...
gi 490378916 227 IYVVNQGTPLANGTPSEIRQHPD 249
Cdd:PRK10418 211 VAVMSHGRIVEQGDVETLFNAPK 233
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
24-220 |
1.33e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.96 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 24 VNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTIlYREKHLEgltgqaiarlgvIRTFQHVR--LFKEMTVI 101
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI-HCGTKLE------------VAYFDQHRaeLDPEKTVM 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 102 ENLlvaqhqhlksgifsgllktpafrrAE--SEALDNAVK-----WLErvDLLpFANRQAGN----LAYGQQRRLEIARC 170
Cdd:PRK11147 402 DNL------------------------AEgkQEVMVNGRPrhvlgYLQ--DFL-FHPKRAMTpvkaLSGGERNRLLLARL 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490378916 171 MVTRPEILMLDEPaaglnpkeTNDLD----DLIAELRTHHNVSILLIEHDMKLV 220
Cdd:PRK11147 455 FLKPSNLLILDEP--------TNDLDvetlELLEELLDSYQGTVLLVSHDRQFV 500
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
8-227 |
2.15e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.57 E-value: 2.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 8 LLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYRE------------KHLEG- 74
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQdlivarlqqdppRNVEGt 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 75 ---LTGQAIARLG-VIRTFQHVRLFKEMTVIENLLvAQHQHLKsgifsgllktpafrraesEALDNAVKW---------L 141
Cdd:PRK11147 83 vydFVAEGIEEQAeYLKRYHDISHLVETDPSEKNL-NELAKLQ------------------EQLDHHNLWqlenrinevL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 142 ERVDLLPfaNRQAGNLAYGQQRRLEIARCMVTRPEILMLDEPaaglnpkeTNDLD-DLIAELRT---HHNVSILLIEHDM 217
Cdd:PRK11147 144 AQLGLDP--DAALSSLSGGWLRKAALGRALVSNPDVLLLDEP--------TNHLDiETIEWLEGflkTFQGSIIFISHDR 213
|
250
....*....|
gi 490378916 218 KLVMGISDRI 227
Cdd:PRK11147 214 SFIRNMATRI 223
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
17-228 |
2.29e-08 |
|
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: 52.65 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 17 RFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTG---FYKPTSGTILYreKHLEGLTGQAIARLGVIRTFQHVR 93
Cdd:cd03233 16 GRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANrteGNVSVEGDIHY--NGIPYKEFAEKYPGEIIYVSEEDV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 94 LFKEMTVIENLLvaqhqhlksgiFSGLLKTPAFRRAESEaldnavkwlervdllpfanrqagnlayGQQRRLEIARCMVT 173
Cdd:cd03233 94 HFPTLTVRETLD-----------FALRCKGNEFVRGISG---------------------------GERKRVSIAEALVS 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490378916 174 RPEILMLDEPaaglnpkeTNDLDDLIAelrtHHNVSIL-LIEHDMKLVMGI-----SDRIY 228
Cdd:cd03233 136 RASVLCWDNS--------TRGLDSSTA----LEILKCIrTMADVLKTTTFVslyqaSDEIY 184
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
21-215 |
2.77e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 52.57 E-value: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 21 LLAVNNVELTINQGEIVSLI------------GPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIARLGvirt 88
Cdd:PRK13541 1 MLSLHQLQFNIEQKNLFDLSitflpsaityikGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIG---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 89 fQHVRLFKEMTVIENLlvaqhqHLKSGIFSgllktpafrraESEALDNAVKWLERVDLLpfaNRQAGNLAYGQQRRLEIA 168
Cdd:PRK13541 77 -HNLGLKLEMTVFENL------KFWSEIYN-----------SAETLYAAIHYFKLHDLL---DEKCYSLSSGMQKIVAIA 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490378916 169 RCMVTRPEILMLDEPAAGLNPKETNDLDDLIAeLRTHHNVSILLIEH 215
Cdd:PRK13541 136 RLIACQSDLWLLDEVETNLSKENRDLLNNLIV-MKANSGGIVLLSSH 181
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
23-220 |
6.49e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 52.97 E-value: 6.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 23 AVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHL-----EGLTGQaiarlgvirtfqhvrlfke 97
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAAliaisSGLNGQ------------------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 98 MTVIENLlvaqhqHLKsGIFSGLLKtpafrraeSEALDNAVKWLERVDLLPFANRQAGNLAYGQQRRLEIARCMVTRPEI 177
Cdd:PRK13545 100 LTGIENI------ELK-GLMMGLTK--------EKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490378916 178 LMLDEPAAGLNPKETNDLDDLIAELRtHHNVSILLIEHDMKLV 220
Cdd:PRK13545 165 LVIDEALSVGDQTFTKKCLDKMNEFK-EQGKTIFFISHSLSQV 206
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
36-220 |
6.55e-08 |
|
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: 51.45 E-value: 6.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 36 IVSLIGPNGAGKTTIFNC----LTGFYKPTSgtilYREKHLEGLTGQAiARLGVIR-TFQHVRlFKEMTVIENLLVaqhq 110
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEAlkyaLTGELPPNS----KGGAHDPKLIREG-EVRAQVKlAFENAN-GKKYTITRSLAI---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 111 hLKSGIFSgllktpafRRAESealdnavKWL--ERVDLLPFANRQAGNLAYgqqrRLEIARCMVTRPEILMLDEPAAGLN 188
Cdd:cd03240 94 -LENVIFC--------HQGES-------NWPllDMRGRCSGGEKVLASLII----RLALAETFGSNCGILALDEPTTNLD 153
|
170 180 190
....*....|....*....|....*....|...
gi 490378916 189 P-KETNDLDDLIAELRTHHNVSILLIEHDMKLV 220
Cdd:cd03240 154 EeNIEESLAEIIEERKSQKNFQLIVITHDEELV 186
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
26-220 |
1.05e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 52.72 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 26 NVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKH-LEGLTGQAI-ARLGVIRtfQHVRLF-------- 95
Cdd:PTZ00265 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHnLKDINLKWWrSKIGVVS--QDPLLFsnsiknni 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 96 -------KEMTVIENLL----VAQHQHLKS---------GIFSGLLKTPA------FRR-----AESEALDNAVKWL--E 142
Cdd:PTZ00265 481 kyslyslKDLEALSNYYnedgNDSQENKNKrnscrakcaGDLNDMSNTTDsnelieMRKnyqtiKDSEVVDVSKKVLihD 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 143 RVDLLP-----FANRQAGNLAYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDM 217
Cdd:PTZ00265 561 FVSALPdkyetLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRL 640
|
...
gi 490378916 218 KLV 220
Cdd:PTZ00265 641 STI 643
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
8-225 |
2.03e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 49.95 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 8 LLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYRekhlegltGQAIARlgVIR 87
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFE--------RQSIKK--DLC 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 88 TFQHVRLF--------KEMTVIENLLVAQHqhlksgiFSgllktpafrrAESEALDNAVKWLERVDLLPFAnrqAGNLAY 159
Cdd:PRK13540 71 TYQKQLCFvghrsginPYLTLRENCLYDIH-------FS----------PGAVGITELCRLFSLEHLIDYP---CGLLSS 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490378916 160 GQQRRLEIARCMVTRPEILMLDEPAAGLNPKEtndLDDLIAELRTHHNV--SILLIEHDmKLVMGISD 225
Cdd:PRK13540 131 GQKRQVALLRLWMSKAKLWLLDEPLVALDELS---LLTIITKIQEHRAKggAVLLTSHQ-DLPLNKAD 194
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
9-234 |
2.18e-07 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 50.41 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRFG-GLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQ---AIARLG 84
Cdd:cd03290 1 VQVTNGYFSWGsGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEatrSRNRYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 85 VIRTFQHVRLFKEmTVIENLLvaqhqhlksgifsglLKTPaFRRAESEALDNAVKWLERVDLLPFANR-QAG----NLAY 159
Cdd:cd03290 81 VAYAAQKPWLLNA-TVEENIT---------------FGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQtEIGergiNLSG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490378916 160 GQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDL-DDLIAELRTHHNVSILLIEHDMKLVMGiSDRIYVVNQGT 234
Cdd:cd03290 144 GQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLmQEGILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDGS 218
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
23-220 |
2.55e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 50.58 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 23 AVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTIlyrEKHLE--------GLTGQaiarlgvirtfqhvrl 94
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV---DRNGEvsviaisaGLSGQ---------------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 95 fkeMTVIENLlvaQHQHLKSGifsgllktpaFRRAESEALDNAVkwLERVDLLPFANRQAGNLAYGQQRRLEIARCMVTR 174
Cdd:PRK13546 100 ---LTGIENI---EFKMLCMG----------FKRKEIKAMTPKI--IEFSELGEFIYQPVKKYSSGMRAKLGFSINITVN 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490378916 175 PEILMLDEPAAGLNPKETNDLDDLIAELRtHHNVSILLIEHDMKLV 220
Cdd:PRK13546 162 PDILVIDEALSVGDQTFAQKCLDKIYEFK-EQNKTIFFVSHNLGQV 206
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
9-227 |
2.89e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 49.24 E-value: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRfggllAVNNVELTINQGEIVSLIGPNGAGKTTIfnCLTGFYKptsgtilyrekhlegltgQAIARLgvirt 88
Cdd:cd03238 1 LTVSGANVH-----NLQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLYA------------------SGKARL----- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 89 fqhvrlfkemtvIENLLVAQHQHLksgIFSGLLKTpafrraeseALDNAVKWLErvdllpfANRQAGNLAYGQQRRLEIA 168
Cdd:cd03238 51 ------------ISFLPKFSRNKL---IFIDQLQF---------LIDVGLGYLT-------LGQKLSTLSGGELQRVKLA 99
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490378916 169 RCMVTRPE--ILMLDEPAAGLNPKETNDLDDLIAELRTHHNvSILLIEHDMKlVMGISDRI 227
Cdd:cd03238 100 SELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGN-TVILIEHNLD-VLSSADWI 158
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
9-190 |
3.04e-07 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 50.96 E-value: 3.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMRF--GGLLaVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKhlegltgqaiARLgvi 86
Cdd:COG4178 363 LALEDLTLRTpdGRPL-LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAG----------ARV--- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 87 rtfqhvrlfkemtvienLLVAQHQHLKSGIFSGLLKTPAFRRAESEAldNAVKWLERVDLLPFANR--QAGN----LAYG 160
Cdd:COG4178 429 -----------------LFLPQRPYLPLGTLREALLYPATAEAFSDA--ELREALEAVGLGHLAERldEEADwdqvLSLG 489
|
170 180 190
....*....|....*....|....*....|
gi 490378916 161 QQRRLEIARCMVTRPEILMLDEPAAGLNPK 190
Cdd:COG4178 490 EQQRLAFARLLLHKPDWLFLDEATSALDEE 519
|
|
| BCA_ABC_TP_C |
pfam12399 |
Branched-chain amino acid ATP-binding cassette transporter; This domain family is found in ... |
236-258 |
3.16e-07 |
|
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: 45.32 E-value: 3.16e-07
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
25-187 |
3.17e-07 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 49.55 E-value: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 25 NNVELTINQGEIVSLIGPNGAGKTTIFNCLTGfyKPTSGTIlyrekhlEG---LTGQAIaRLGVIRTFQHVR----LFKE 97
Cdd:cd03232 24 NNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAGVI-------TGeilINGRPL-DKNFQRSTGYVEqqdvHSPN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 98 MTVIENLLvaqhqhlksgiFSGLLKtpafrraesealdnavkwlervdllpfanrqagNLAYGQQRRLEIARCMVTRPEI 177
Cdd:cd03232 94 LTVREALR-----------FSALLR---------------------------------GLSVEQRKRLTIGVELAAKPSI 129
|
170
....*....|
gi 490378916 178 LMLDEPAAGL 187
Cdd:cd03232 130 LFLDEPTSGL 139
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
26-243 |
6.04e-07 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 48.34 E-value: 6.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 26 NVEL-TINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTIlyrekHLEGLTgqaiarlgvirtfqhvrlfkemtvienl 104
Cdd:cd03222 16 LVELgVVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDND-----EWDGIT---------------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 105 LVAQHQHLKsgifsgllktpafrraesealdnavkwlervdllpfanrqagnLAYGQQRRLEIARCMVTRPEILMLDEPA 184
Cdd:cd03222 63 PVYKPQYID-------------------------------------------LSGGELQRVAIAAALLRNATFYLFDEPS 99
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490378916 185 AGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGISDRIYVVnQGTPLANGTPSE 243
Cdd:cd03222 100 AYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVF-EGEPGVYGIASQ 157
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
8-246 |
1.04e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 48.63 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 8 LLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGF--YKPTSGTILYREKHLEGLTGQAIARLGV 85
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 86 IRTFQHVrlfKEMTVIENLLVAQhqhlksgifSGLLKTPAFRRAES-EALDNAVKWLERVDLLPFAN---RQAGNLAY-- 159
Cdd:PRK09580 81 FMAFQYP---VEIPGVSNQFFLQ---------TALNAVRSYRGQEPlDRFDFQDLMEEKIALLKMPEdllTRSVNVGFsg 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 160 GQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRtHHNVSILLIEHDMKLVMGIS-DRIYVVNQGTPLAN 238
Cdd:PRK09580 149 GEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLR-DGKRSFIIVTHYQRILDYIKpDYVHVLYQGRIVKS 227
|
....*...
gi 490378916 239 GTPSEIRQ 246
Cdd:PRK09580 228 GDFTLVKQ 235
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
25-188 |
1.15e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 49.34 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 25 NNVELTINQGEIVSLIGPNGAGKTTIFNCLTGfyKPTSGTILYREKHLEGLTGQAI--ARLGVIRTfQHVRLfKEMTVIE 102
Cdd:TIGR00956 780 NNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTGVITGGDRLVNGRPLDSSfqRSIGYVQQ-QDLHL-PTSTVRE 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 103 NLlvaqhqhlksgIFSGLLKTPAfRRAESEALDNAVKWLERVDLLPFANRQAGNLAYG----QQRRLEIARCMVTRPE-I 177
Cdd:TIGR00956 856 SL-----------RFSAYLRQPK-SVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGlnveQRKRLTIGVELVAKPKlL 923
|
170
....*....|.
gi 490378916 178 LMLDEPAAGLN 188
Cdd:TIGR00956 924 LFLDEPTSGLD 934
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
153-233 |
1.19e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.02 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 153 QAGNLAYGQQRRLEIARCMVTRPEILMLDEPAAGLnpketnD----------LDDLIAELRthhnvSILLIEHDMKLVMG 222
Cdd:NF040905 401 KVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGI------DvgakyeiytiINELAAEGK-----GVIVISSELPELLG 469
|
90
....*....|.
gi 490378916 223 ISDRIYVVNQG 233
Cdd:NF040905 470 MCDRIYVMNEG 480
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
6-233 |
1.46e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.01 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 6 TPLLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTIlyrekhleGLTgQAIaRLGV 85
Cdd:PRK10636 310 NPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI--------GLA-KGI-KLGY 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 86 IrtfqhvrlfkemtvienllvAQHQHlksgifsgllktpAFRRAESEALDNAVKWLERV------DLL---PFANRQ--- 153
Cdd:PRK10636 380 F--------------------AQHQL-------------EFLRADESPLQHLARLAPQEleqklrDYLggfGFQGDKvte 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 154 -AGNLAYGQQRRLEIARCMVTRPEILMLDEPaaglnpkeTNDLD-DL---IAELRTHHNVSILLIEHDMKLVMGISDRIY 228
Cdd:PRK10636 427 eTRRFSGGEKARLVLALIVWQRPNLLLLDEP--------TNHLDlDMrqaLTEALIDFEGALVVVSHDRHLLRSTTDDLY 498
|
....*
gi 490378916 229 VVNQG 233
Cdd:PRK10636 499 LVHDG 503
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
27-244 |
1.99e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.58 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 27 VELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILyrekhlegLTGQAIARLGVirtfqhVRLFKEMTVIENLLV 106
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRIL--------IDGCDISKFGL------MDLRKVLGIIPQAPV 1323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 107 aqhqhlksgIFSGLLKtpaFRRAESEALDNAVKW--LERVDLLPFANR----------QAG-NLAYGQQRRLEIARCMVT 173
Cdd:PLN03130 1324 ---------LFSGTVR---FNLDPFNEHNDADLWesLERAHLKDVIRRnslgldaevsEAGeNFSVGQRQLLSLARALLR 1391
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490378916 174 RPEILMLDEPAAGLNPKEtndlDDLIA-----ELRThhnVSILLIEHDMKLVMGiSDRIYVVNQGTPLANGTPSEI 244
Cdd:PLN03130 1392 RSKILVLDEATAAVDVRT----DALIQktireEFKS---CTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENL 1459
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
156-240 |
5.36e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 47.33 E-value: 5.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 156 NLAYGQQRRLEIARCMVTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNVSILLIEHDMKLVMGiSDRIYVVNQgtP 235
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFNN--P 1434
|
....*
gi 490378916 236 LANGT 240
Cdd:PTZ00265 1435 DRTGS 1439
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
31-244 |
1.11e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 46.51 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 31 INQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILyrekhlegLTGQAIARLGVirtfqhVRLFKEMTVIENLLVaqhq 110
Cdd:PLN03232 1259 VSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIM--------IDDCDVAKFGL------TDLRRVLSIIPQSPV---- 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 111 hlksgIFSGLLKtpaFRRAESEALDNAVKW--LER------VDLLPF---ANRQAG--NLAYGQQRRLEIARCMVTRPEI 177
Cdd:PLN03232 1321 -----LFSGTVR---FNIDPFSEHNDADLWeaLERahikdvIDRNPFgldAEVSEGgeNFSVGQRQLLSLARALLRRSKI 1392
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490378916 178 LMLDEPAAGLNPKETNDLDDLIAElrTHHNVSILLIEHDMKLVMGiSDRIYVVNQGTPLANGTPSEI 244
Cdd:PLN03232 1393 LVLDEATASVDVRTDSLIQRTIRE--EFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQEL 1456
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
25-108 |
1.34e-05 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 44.79 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 25 NNVELTINQGeIVSLIGPNGAGKTTIFNC----LTGFYKPTSGTILYREKHLEGLTGQAIARLGVIR-TFQHVRLFKEMT 99
Cdd:pfam13476 10 RDQTIDFSKG-LTLITGPNGSGKTTILDAiklaLYGKTSRLKRKSGGGFVKGDIRIGLEGKGKAYVEiTFENNDGRYTYA 88
|
....*....
gi 490378916 100 VIENLLVAQ 108
Cdd:pfam13476 89 IERSRELSK 97
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
34-190 |
1.45e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 45.99 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 34 GEIVSLIGPNGAGKTTIFNCLTGfyKPTSGTIlYREKHLEGLTGQAiarlgviRTFQHVRLFKEMTVIENLLVAQHQHLk 113
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAG--RKTGGYI-EGDIRISGFPKKQ-------ETFARISGYCEQNDIHSPQVTVRESL- 974
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 114 sgIFSGLLKTPAfRRAESEALDNAVKWLERVDLLPFANRQAG-----NLAYGQQRRLEIARCMVTRPEILMLDEPAAGLN 188
Cdd:PLN03140 975 --IYSAFLRLPK-EVSKEEKMMFVDEVMELVELDNLKDAIVGlpgvtGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
..
gi 490378916 189 PK 190
Cdd:PLN03140 1052 AR 1053
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
151-227 |
2.70e-05 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 44.17 E-value: 2.70e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490378916 151 NRQAGNLAYGQQRRLEIARCMVTRPE--ILMLDEPAAGLNPKETNDLDDLIAELRTHHNvSILLIEHDMKlVMGISDRI 227
Cdd:cd03270 132 SRSAPTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDLGN-TVLVVEHDED-TIRAADHV 208
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
143-253 |
6.50e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.05 E-value: 6.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 143 RVDLLPFAnRQAGNLAYGQQRRLEIARCM---VTRPEILMLDEPAAGLNpkeTNDLDDLIAELR--THHNVSILLIEHDM 217
Cdd:PRK00635 797 GLDYLPLG-RPLSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLH---THDIKALIYVLQslTHQGHTVVIIEHNM 872
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 490378916 218 KLVMgISDriYVVNQGTP--------LANGTPSE-IRQHPDVIKA 253
Cdd:PRK00635 873 HVVK-VAD--YVLELGPEggnlggylLASCSPEElIHLHTPTAKA 914
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
14-234 |
7.91e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 43.62 E-value: 7.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 14 LTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAIARLGViRTFQHV- 92
Cdd:PRK10636 7 LQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALPQ-PALEYVi 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 93 ---RLFKEMTviENLLVAQHQ---HLKSGIFSGLLKTPAFR-RAESEALDNAvkwlervdlLPFANRQ----AGNLAYGQ 161
Cdd:PRK10636 86 dgdREYRQLE--AQLHDANERndgHAIATIHGKLDAIDAWTiRSRAASLLHG---------LGFSNEQlerpVSDFSGGW 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490378916 162 QRRLEIARCMVTRPEILMLDEPAAGLnpketnDLDDLIAELR--THHNVSILLIEHDMKLVMGISDRIYVVNQGT 234
Cdd:PRK10636 155 RMRLNLAQALICRSDLLLLDEPTNHL------DLDAVIWLEKwlKSYQGTLILISHDRDFLDPIVDKIIHIEQQS 223
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
24-258 |
8.04e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.81 E-value: 8.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 24 VNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSgtilyrekhleglTGQAIARlGVIRTFQHVRLFKEMTVIEN 103
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAE-------------TSSVVIR-GSVAYVPQVSWIFNATVREN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 104 LLvaqhqhlksgiFSGLLKTPAFRRA-ESEALDNAVKWLERVDLLPFANRQAgNLAYGQQRRLEIARCMVTRPEILMLDE 182
Cdd:PLN03232 699 IL-----------FGSDFESERYWRAiDVTALQHDLDLLPGRDLTEIGERGV-NISGGQKQRVSMARAVYSNSDIYIFDD 766
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490378916 183 PAAGLNPKETNDLDD--LIAELRTHHNVSILLIEHDMKLVmgisDRIYVVNQGTPLANGTPSEIRQHPDVIKAYLGEA 258
Cdd:PLN03232 767 PLSALDAHVAHQVFDscMKDELKGKTRVLVTNQLHFLPLM----DRIILVSEGMIKEEGTFAELSKSGSLFKKLMENA 840
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
19-196 |
9.25e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.31 E-value: 9.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 19 GGLLAVNNVELTINQGEIVSLIGPNGAGKTTIF-----NCLTGFykPTSGTILYREKHLEGLTGQAIArlGVIRT-FQHV 92
Cdd:PLN03073 188 GGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLrymamHAIDGI--PKNCQILHVEQEVVGDDTTALQ--CVLNTdIERT 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 93 RLFKEmtviENLLVAQHQHLK----SGIFSGLLKTPAFRRAESEALDNAVKWLERVDLLPFANRQAGNLAY--------- 159
Cdd:PLN03073 264 QLLEE----EAQLVAQQRELEfeteTGKGKGANKDGVDKDAVSQRLEEIYKRLELIDAYTAEARAASILAGlsftpemqv 339
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490378916 160 --------GQQRRLEIARCMVTRPEILMLDEPaaglnpkeTNDLD 196
Cdd:PLN03073 340 katktfsgGWRMRIALARALFIEPDLLLLDEP--------TNHLD 376
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
26-216 |
1.10e-04 |
|
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: 43.00 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 26 NVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSG--------TILY-------------REKHLEGL--TGQAIAR 82
Cdd:TIGR03719 23 DISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGearpqpgiKVGYlpqepqldptktvRENVEEGVaeIKDALDR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 83 LGVIR------TFQHVRLFKEMTVIENLLVAQHQHlksgifsgllktpafrRAESEaLDNAVKWLErvdlLPFANRQAGN 156
Cdd:TIGR03719 103 FNEISakyaepDADFDKLAAEQAELQEIIDAADAW----------------DLDSQ-LEIAMDALR----CPPWDADVTK 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490378916 157 LAYGQQRRLEIARCMVTRPEILMLDEPaaglnpkeTNDLD-DLIAELRTH-HNV--SILLIEHD 216
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEP--------TNHLDaESVAWLERHlQEYpgTVVAVTHD 217
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
9-65 |
1.22e-04 |
|
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: 42.07 E-value: 1.22e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490378916 9 LQVNGLTMRFG-----GLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTI 65
Cdd:cd03250 1 ISVEDASFTWDsgeqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV 62
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
23-182 |
1.27e-04 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 42.78 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 23 AVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILYREKHLEGLTGQAI-ARLGVIRtfQHVRLFKEmTVI 101
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWrSRLAVVS--QTPFLFSD-TVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 102 ENLlvaqhqhlksgifsgLLKTPAFRRAESEALDNAVKWLERVDLLPFA-NRQAGN----LAYGQQRRLEIARCMVTRPE 176
Cdd:PRK10789 407 NNI---------------ALGRPDATQQEIEHVARLASVHDDILRLPQGyDTEVGErgvmLSGGQKQRISIARALLLNAE 471
|
....*.
gi 490378916 177 ILMLDE 182
Cdd:PRK10789 472 ILILDD 477
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
151-256 |
1.72e-04 |
|
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: 42.69 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 151 NRQAGNLAYGQQRRLEIARCMVTRPEILM--LDEPAAGLNPKETNDLDDLIAELRTHHNvSILLIEHDmKLVMGISDriY 228
Cdd:TIGR00630 483 SRAAGTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHQRDNRRLINTLKRLRDLGN-TLIVVEHD-EDTIRAAD--Y 558
|
90 100 110
....*....|....*....|....*....|....*...
gi 490378916 229 VVNQGtP---------LANGTPSEIRQHPDVIK-AYLG 256
Cdd:TIGR00630 559 VIDIG-PgagehggevVASGTPEEILANPDSLTgQYLS 595
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
8-216 |
2.32e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.19 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 8 LLQVNGLTMRFGGLLAVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTIlyrekHLEglTGQaiaRLGVIR 87
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNV-----SLD--PNE---RLGKLR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 88 TFQHVrlFKEMTVIENLLVAqHQHL------KSGIFSGLLKTPA--FRRAESEA----LD------NAVKWLERVDL-LP 148
Cdd:PRK15064 71 QDQFA--FEEFTVLDTVIMG-HTELwevkqeRDRIYALPEMSEEdgMKVADLEVkfaeMDgytaeaRAGELLLGVGIpEE 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490378916 149 FANRQAGNLAYGQQRRLEIARCMVTRPEILMLDEPaaglnpkeTNDLD-DLI---AELRTHHNVSILLIEHD 216
Cdd:PRK15064 148 QHYGLMSEVAPGWKLRVLLAQALFSNPDILLLDEP--------TNNLDiNTIrwlEDVLNERNSTMIIISHD 211
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
9-189 |
2.64e-04 |
|
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: 40.60 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 9 LQVNGLTMR--FGGLLaVNNVELTINQGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTIlyrekhlegltgqaiarlgvi 86
Cdd:cd03223 1 IELENLSLAtpDGRVL-LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI--------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 87 rtfqhvrlfkEMTVIENLL-VAQHQHLKSGIFSGLLKTPafrraesealdnavkWLERVDLlpfanrqagnlayGQQRRL 165
Cdd:cd03223 59 ----------GMPEGEDLLfLPQRPYLPLGTLREQLIYP---------------WDDVLSG-------------GEQQRL 100
|
170 180
....*....|....*....|....
gi 490378916 166 EIARCMVTRPEILMLDEPAAGLNP 189
Cdd:cd03223 101 AFARLLLHKPKFVFLDEATSALDE 124
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
24-189 |
2.75e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 41.53 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 24 VNNVELTINQGeIVSLIGPNGAGKTTIFNCLTGFYKPTSGTIL-----YREKHLEGLTGQAIARLGVI--RTFQHVRLFK 96
Cdd:COG3593 14 IKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSSSRKFdeedfYLGDDPDLPEIEIELTFGSLlsRLLRLLLKEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 97 EMTVIENLLVAQHQHLKSGI--FSGLLKT---PAFRRAESE---ALDNAVKWLERVDLLpFANRQAGNLAY---GQQRRL 165
Cdd:COG3593 93 DKEELEEALEELNEELKEALkaLNELLSEylkELLDGLDLElelSLDELEDLLKSLSLR-IEDGKELPLDRlgsGFQRLI 171
|
170 180 190
....*....|....*....|....*....|.
gi 490378916 166 EIA-------RCMVTRPEILMLDEPAAGLNP 189
Cdd:COG3593 172 LLAllsalaeLKRAPANPILLIEEPEAHLHP 202
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
14-147 |
3.29e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 40.76 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 14 LTMR-FGGLLAVNNVELTinqGEIVSLIGPNGAGKTTIFNCLT-GFYKPTSGTILYREKHLEGLTGQAIARLGVIRTFQH 91
Cdd:COG0419 5 LRLEnFRSYRDTETIDFD---DGLNLIVGPNGAGKSTILEAIRyALYGKARSRSKLRSDLINVGSEEASVELEFEHGGKR 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 490378916 92 VRLFKEMTVIENLLVAQHQHLKSgIFSGLLKTPAFRRAESEALDNAVKWLERVDLL 147
Cdd:COG0419 82 YRIERRQGEFAEFLEAKPSERKE-ALKRLLGLEIYEELKERLKELEEALESALEEL 136
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
33-67 |
1.36e-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: 38.12 E-value: 1.36e-03
10 20 30
....*....|....*....|....*....|....*
gi 490378916 33 QGEIVSLIGPNGAGKTTIFNCLTGFYKPTSGTILY 67
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY 35
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
180-249 |
1.61e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 39.62 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 180 LDEPAAGLNPKETNDLDDLIAELRTHHNvSILLIEHDmKLVMGISDRI------------YVVnqgtplANGTPSEIRQH 247
Cdd:COG0178 511 LDEPSIGLHQRDNDRLIETLKRLRDLGN-TVIVVEHD-EDTIRAADYIidigpgagehggEVV------AQGTPEEILKN 582
|
..
gi 490378916 248 PD 249
Cdd:COG0178 583 PD 584
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
152-244 |
4.02e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.46 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490378916 152 RQAGNLAYGQQRRLEIARCM---VTRPEILMLDEPAAGLNPKETNDLDDLIAELRTHHNvSILLIEHDMKlVMGISDriY 228
Cdd:TIGR00630 825 QPATTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGN-TVVVIEHNLD-VIKTAD--Y 900
|
90 100
....*....|....*....|....
gi 490378916 229 VV--------NQGTPLANGTPSEI 244
Cdd:TIGR00630 901 IIdlgpeggdGGGTVVASGTPEEV 924
|
|
| |
